Unnamed: 0
int64
2
562k
Entry
stringlengths
6
10
Sequence
stringlengths
11
999
Protein names
stringlengths
5
558
Organism
stringclasses
392 values
Organism (ID)
int64
595
2.89M
Length
int64
11
999
Mass
int64
1.06k
118k
Keywords
stringlengths
4
380
Gene Ontology IDs
stringlengths
10
754
Protein existence
stringclasses
5 values
Annotation
float64
1
5
Subcellular location [CC]
stringlengths
30
2.26k
Signal peptide
stringclasses
677 values
Transmembrane
stringlengths
32
2.52k
Pfam
stringlengths
8
72
InterPro
stringlengths
10
180
PDB
stringlengths
5
2.65k
Taxonomic lineage
stringclasses
178 values
Gene Names
stringlengths
2
299
Toxin
bool
2 classes
species
stringclasses
111 values
cdhit_cluster
int64
0
4.65k
cdhit_rep
stringlengths
5
10
cdhit_rep_is_ref
bool
1 class
cdhit_pct_id
float64
779
Q9P3V0
MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIVIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV
Meiotic driver wtf4
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
284,812
366
40,360
Alternative initiation;Cytoplasm;Endoplasmic reticulum;Membrane;Reference proteome;Toxin;Transmembrane;Transmembrane helix;Vacuole
GO:0000324; GO:0005737; GO:0005774; GO:0005789; GO:0072324; GO:0110134
Inferred from homology
5
SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000250|UniProtKB:A0A218N034}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
null
TRANSMEM 89..109; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 119..139; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 149..169; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 185..205; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 221..241; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 245..265; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 275..295; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 309..329; /note="Helical"; /evidence="ECO:0000255"
PF03303;
IPR004982;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), Taphrinomycotina (subphylum), Schizosaccharomycetes (class), Schizosaccharomycetales (order), Schizosaccharomycetaceae (family), Schizosaccharomyces (genus), Schizosaccharomyces pombe (species)
wtf4 wtf13 SPCC548.03c
true
Schizosaccharomyces pombe
3
row_729
false
null
167
O84616
MMEVFMNFLDQLDLIIQNKHMLEHTFYVKWSKGELTKEQLQAYAKDYYLHIKAFPKYLSAIHSRCDDLEARKLLLDNLMDEENGYPNHIDLWKQFVFALGVTPEELEAHEPSEAAKAKVATFMRWCTGDSLAAGVAALYSYESQIPRIAREKIRGLTEYFGFSNPEDYAYFTEHEEADVRHAREEKALIEMLLKDDADKVLEASQEVTQSLYGFLDSFLDPGTCCSCHQSY
4-aminobenzoate synthase (EC 1.3.3.-) (Chlamydia protein associating with death domains) (CADD) (para-aminobenzoate synthase) (PABA synthase)
Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)
272,561
231
26,734
3D-structure;Host cytoplasm;Iron;Metal-binding;Oxidoreductase;Reference proteome;Secreted;Toxin;Virulence
GO:0005576; GO:0006790; GO:0016491; GO:0030430; GO:0044281; GO:0046872; GO:0090729; GO:0141072
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11805081}. Host cytoplasm {ECO:0000269|PubMed:11805081}. Note=Secreted into the host cytoplasm, where it co-localizes with Fas in the proximity of the inclusion body. {ECO:0000269|PubMed:11805081}.
null
null
PF03070;
IPR027572;IPR016084;IPR039068;IPR004305;
1RCW;8VA9;8VAB;8VAG;8VAI;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), PVC group (clade), Chlamydiota (phylum), Chlamydiia (class), Chlamydiales (order), Chlamydiaceae (family), Chlamydia/Chlamydophila group (no rank), Chlamydia (genus), Chlamydia trachomatis (species)
CT_610
true
Chlamydia trachomatis
0
row_154
false
null
4,596
Q4JHE2
MNVFFMFSLLFLAALESCADDRRRPLEECFQEADYEEFLEIARNGLNETSNPKHVVVVGAGMAGLSAAYVLAGAGHNVTLLEASERVGGRVNTYRNETEGWYVNLGPMRLPERHRIIREYIRKFGLKLNEFLQENENAWYFIRNIRKRVWEVKKDPGVFKYPVEPSEEGKSASQLYRESLEKVIEELKRTNCSYILNKYDTYSTKEYLIKEGNLSRGAVDMIGKLPNEDSSYYLSFIESLKSDDLFSYEKRFDEIVGGFDQLPISMYQAIAEMVHLNAQVIKIQHNAEEVRVAYQTPAKTLSYVTADYVIVCSTSRAARRIYFEPPLPPKKAHALRSIHYRSGTKIFLTCTRKFWEADGIHGGKSTTDLPSRFIYYPNHNFTSDVGVIVAYTLADDADFFQALDIKTSADIVINDLSLIHQLPKEEIQALCYPSMIKKWSLDKYAMGAITSFTPYQFQDFIETVAAPVGRIYFAGEYTARVHGWLDSTIKSGLTAARDVNRASQKPSRRQLSNDNEL
L-amino-acid oxidase (LAAO) (LAO) (EC 1.4.3.2)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
517
59,058
Antibiotic;Antimicrobial;Apoptosis;Cytolysis;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Hemolysis;Hemostasis impairing toxin;Oxidoreductase;Secreted;Signal;Toxin
GO:0001716; GO:0005576; GO:0006915; GO:0009063; GO:0031640; GO:0042742; GO:0090729
Evidence at transcript level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16261251}.
SIGNAL 1..18; /evidence="ECO:0000250|UniProtKB:P81382"
null
PF01593;
IPR002937;IPR036188;IPR001613;IPR050281;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
0
row_4374
false
null
513
P82807
MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRSNSLFEEIRPGNIERECIEEKCSKEEAREVFEDNEKTETFWNVYVDGDQCSSNPCHYRGTCKDGIGSYTCTCLPNYEGKNCEKVLYQSCRVDNGNCWHFCKRVQSETQCSCAESYRLGVDGHSCVAEGDFSCGRNIKARNKREASLPDFVQSQKATLLKKSDNPSPDIRIVNGMDCKLGECPWQAVLINEKGEVFCGGTILSPIHVLTAAHCINQTKSVSVIVGEIDISRKETRRLLSVDKIYVHTKFVPPNYYYVHQNFDRVAYDYDIAIIRMKTPIQFSENVVPACLPTADFANEVLMKQDSGIVSGFGRIRFKEPTSNTLKVITVPYVDRHTCMLSSDFRITQNMFCAGYDTLPQDACQGDSGGPHITAYRDTHFITGIISWGEGCARKGKYGVYTKVSRFIPWIKKIMSLK
Venom prothrombin activator notecarin-D1 (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Notecarin-D1 light chain; Notecarin-D1 heavy chain]
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
455
51,464
Blood coagulation cascade activating toxin;Calcium;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Prothrombin activator;Repeat;Secreted;Signal;Toxin
GO:0004252; GO:0005509; GO:0005576; GO:0005615; GO:0006508; GO:0007596; GO:0016504; GO:0035807; GO:0044469; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10779512, ECO:0000269|PubMed:12403650}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF00008;PF14670;PF00594;PF00089;
IPR017857;IPR001881;IPR000742;IPR000152;IPR018097;IPR035972;IPR000294;IPR012224;IPR050442;IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;IPR033116;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
1
row_477
false
null
2,024
Q3HXY5
MSMLCYTLIIAFLIGIWAAPKSEDNVPLGSPATSDLSDTSCAQTHEGLKTSRNTDQRHPAPKKAEDQELGSVANIIVDPKLFQKRRFQSSRVLFSTQPPPLSRDEQSVEFLDNEDTLNRNIRAKRENHPVHNQGEHSVCDSVSDWVIKTTATDIRGNMVTVMVDINRDNEVYKQYFFETKCRNPNPNPVQSECRGIDSRLWNSYCTTTRTFVRALTMEGNQASWRFIRIDTACVCVIIRKTDNF
Venom nerve growth factor 3 (v-NGF-3) (vNGF-3)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
244
27,789
Cleavage on pair of basic residues;Disulfide bond;Growth factor;Lipid-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Secreted;Signal;Toxin
GO:0005163; GO:0005615; GO:0007169; GO:0008021; GO:0008083; GO:0008191; GO:0008289; GO:0021675; GO:0030424; GO:0030425; GO:0038180; GO:0043524; GO:0048812; GO:0050804; GO:0090729
Evidence at transcript level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P61898}.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF00243;
IPR029034;IPR020408;IPR002072;IPR020425;IPR019846;IPR020433;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
2
row_1943
false
null
2,025
Q3HXY6
MSMLCYTLIIAFLIGIWAAPKSEDNVPLGSPATSDLSDTSCAQTHEGLKTSRNTDQRHPAPKKAEDQELGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQSVEFLDNEDTLNRNIRAKRENHPVHNQGEHSVCDSVSDWVIKTTATDIRGNMVTVMVDINRNNEVYKQYFFETKCRNPNPNPVQSERRGIDSRLWNSYCTTTQTFVRALTMEGNQASWRFIRIDTACVCVIIRKTDNF
Venom nerve growth factor 2 (v-NGF-2) (vNGF-2)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
244
27,795
Cleavage on pair of basic residues;Disulfide bond;Growth factor;Lipid-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Secreted;Signal;Toxin
GO:0005163; GO:0005615; GO:0007169; GO:0008021; GO:0008083; GO:0008191; GO:0008289; GO:0021675; GO:0030424; GO:0030425; GO:0038180; GO:0043524; GO:0048812; GO:0050804; GO:0090729
Evidence at transcript level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P61898}.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF00243;
IPR029034;IPR020408;IPR002072;IPR020425;IPR020433;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
3
row_1944
false
null
7,075
Q3SB04
MIAFIVLLSLAAVLQQSSGTVDFASESSNKKDYQKEIVDKHNALRRSVKPTARNMLRMEWNSHAAQNAKRWADRCTFAHSPPHTRTVGKLRCGENIFMSSQPFAWSGVVQAWYDEVKKFVYGIGAKPPGSVIGHYTQVVWYKSHLLGCASAKCSSTKYLYVCQYCPAGNIRGSIATPYKSGPTCGDCPSACVNGLCTNPCKYEDDFSNCKALAKNSKCQTEWIKSKCPAACFCHNKII
Cysteine-rich venom protein pseudechetoxin-like (CRVP)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
238
26,327
Disulfide bond;Ion channel impairing toxin;Neurotoxin;Secreted;Signal;Toxin
GO:0005576; GO:0090729; GO:0099106
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..19; /evidence="ECO:0000250"
null
PF00188;PF08562;
IPR018244;IPR014044;IPR035940;IPR042076;IPR001283;IPR013871;IPR034117;IPR003582;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
4
row_6797
false
null
2,265
Q9PSN5
NLYQFGNMIQCANHGRRPTRHYMDYGCYCGKGGSGTPVDELDRCCQTHDDCYGEAEKLPACNYMMSGPYYNTYSYECNEGELTCKDNNDECKAFICNCDRTAAICFARAPYNDANWNIDTKTRCQ
Acidic phospholipase A2 HTe (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
125
14,262
Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Myotoxin;Neurotoxin;Secreted;Toxin
GO:0005102; GO:0005509; GO:0005543; GO:0005576; GO:0006633; GO:0006644; GO:0016042; GO:0047498; GO:0048146; GO:0050482; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted.
null
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
5
row_2181
false
null
173
P00608
NLVQFSYLIQCANHGKRPTWHYMDYGCYCGAGGSGTPVDELDRCCKIHDDCYDEAGKKGCFPKMSAYDYYCGENGPYCRNIKKKCLRFVCDCDVEAAFCFAKAPYNNANWNIDTKKRCQ
Basic phospholipase A2 notexin (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
119
13,593
3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Myotoxin;Neurotoxin;Presynaptic neurotoxin;Secreted;Toxin
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0047498; GO:0050482; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
null
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
1AE7;4E4C;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
6
row_160
false
null
3,038
P01384
MKTLLLTLVVVTIVCLDLGDSLICYMGPKTPRTCPRGQNLCYTKTWCDAFCSSRGKVVELGCAATCPIAKSYEDVTCCSTDNCNPFPVRPRPHP
Alpha-elapitoxin-Nss2a (Alpha-EPTX-Nss2a) (Long neurotoxin 1) (LNTX-1) (Notechis III-4)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
94
10,289
Acetylcholine receptor inhibiting toxin;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Signal;Toxin
GO:0005576; GO:0030550; GO:0090729; GO:0099106
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:497256}.
SIGNAL 1..21; /evidence="ECO:0000269|PubMed:497256"
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
7
row_2936
false
null
5,201
A8HDK0
MKTLLLTLVVVTIVFLDLGYTMTCCNQQSSQPKTTTTCAESSCYKKTWRDHRGTITERGCGCPNVKPGVQINCCKTDECNN
Short neurotoxin 1 (SNTX-1)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
81
8,982
Acetylcholine receptor inhibiting toxin;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Signal;Toxin
GO:0005576; GO:0030550; GO:0090729; GO:0099106
Inferred from homology
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..21; /evidence="ECO:0000250"
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
8
row_4968
false
null
7,065
Q3SAE7
SGSKTAKIGDGCFGLPLDRIGSTSGMGCGSVPKPTPGGS
Natriuretic peptide NsNP-b
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
39
3,681
Disulfide bond;Hypotensive agent;Secreted;Toxin;Vasoactive;Vasodilator
GO:0005179; GO:0005576; GO:0008217; GO:0042311; GO:0090729
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16908092}.
null
null
PF00212;
IPR000663;IPR030480;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
9
row_6787
false
null
7,066
Q3SAE8
SGSEVAKIGDGCFGLPLDRIGSASGMGCRSVPKPTPGGS
Natriuretic peptide NsNP-a
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
39
3,749
Disulfide bond;Hypotensive agent;Secreted;Toxin;Vasoactive;Vasodilator
GO:0005179; GO:0005576; GO:0008217; GO:0042311; GO:0090729
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16908092}.
null
null
PF00212;
IPR000663;IPR030480;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
10
row_6788
false
null
6,357
P0DL19
SNKKDYQKEIVDKHNALRRSVK
Cysteine-rich venom protein notescatin (CRVP) (Notescatin-a) (Notescatin-b)
Notechis scutatus scutatus (Mainland tiger snake) (Common tiger snake)
70,142
22
2,657
Direct protein sequencing;Disulfide bond;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
2
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
11
row_6109
false
null
1,468
P0CY52
SNSLFEEVRPIVNGMDCKLG
Venom prothrombin activator notanarin-D (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Notanarin-D light chain; Notanarin-D heavy chain]
Notechis scutatus niger (Peninsula tiger snake) (Notechis ater niger)
1,027,870
20
2,209
Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;EGF-like domain;Gamma-carboxyglutamic acid;Hemostasis impairing toxin;Hydrolase;Protease;Prothrombin activator;Secreted;Toxin
GO:0004252; GO:0005576; GO:0006508; GO:0016504; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12403650}.
null
null
null
null
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Notechis (genus), Notechis scutatus (species)
null
true
Notechis scutatus
12
row_1407
false
null
3,941
P25687
AVITGACERDLQCGKGTCCAVSLWIKSVRVCTPVGTSGEDCHPASHKIPFSGQRMHHTCPCAPNLACVQTSPKKFKCLSKS
Toxin MIT1 (MIT 1) (Black mamba intestinal toxin 1) (Black mamba venom protein A)
Dendroaspis polylepis polylepis (Black mamba)
8,620
81
8,604
3D-structure;Direct protein sequencing;Disulfide bond;G-protein coupled receptor impairing toxin;Secreted;Toxin
GO:0001935; GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10567694}.
null
null
PF06607;
IPR009523;IPR023569;
1IMT;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
0
row_3786
false
null
186
P00981
SGHLLLLLGLLTLWAELTPVSGAAKYCKLPLRIGPCKRKIPSFYYKWKAKQCLPFDYSGCGGNANRFKTIEECRRTCVG
Kunitz-type serine protease inhibitor homolog dendrotoxin K (DTX-K) (Venom basic protease inhibitor K)
Dendroaspis polylepis polylepis (Black mamba)
8,620
79
8,852
3D-structure;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Potassium channel impairing toxin;Secreted;Signal;Toxin;Voltage-gated potassium channel impairing toxin
GO:0004867; GO:0005615; GO:0015459; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8504088, ECO:0000269|PubMed:857902}.
SIGNAL <1..?
null
PF00014;
IPR002223;IPR036880;IPR020901;IPR050098;
1DTK;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
1
row_173
false
null
314
P0DKR6
MKTLLLTLLVVTIVCLDLGYSLKCYQHGKVVTCHRDMKFCYHNTGMPFRNLKLILQGCSSSCSETENNKCCSTDRCNK
Mambalgin-1 (Mamb-1) (Pi-Dp1)
Dendroaspis polylepis polylepis (Black mamba)
8,620
78
8,853
3D-structure;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Pharmaceutical;Proton-gated sodium channel impairing toxin;Secreted;Signal;Toxin
GO:0005576; GO:0090729; GO:0099106
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23034652}.
SIGNAL 1..21; /evidence="ECO:0000269|PubMed:23034652"
null
PF21947;
IPR003571;IPR045860;IPR054131;
2MJY;5DO6;5DU1;5DZ5;7CFT;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
2
row_296
false
null
974
C0HJD7
RTCNKTFSDQSKICPPGENICYTKTWCDAFCSQRGKRVELGCAATCPKVKAGVEIKCCSTDNCNKFQFGKPR
Alpha-elapitoxin-Dpp2d (Alpha-EPTX-Dpp2d)
Dendroaspis polylepis polylepis (Black mamba)
8,620
72
8,002
3D-structure;Acetylcholine receptor inhibiting toxin;Amidation;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Toxin
GO:0005576; GO:0030550; GO:0090729; GO:0099106
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24867092}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
4LFT;8DA0;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
3
row_919
false
null
4,201
P80494
LTCVTSKSIFGITTENCPDGQNLCFKKWYYLNHRYSDITWGCAATCPKPTNVRETIHCCETDKCNE
Muscarinic toxin alpha (MT-alpha)
Dendroaspis polylepis polylepis (Black mamba)
8,620
66
7,554
3D-structure;Direct protein sequencing;Disulfide bond;G-protein coupled receptor impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8536706}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
7ULS;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
4
row_4036
false
null
3,931
P25518
LTCVTSKSIFGITTEDCPDGQNLCFKRRHYVVPKIYDITRGCVATCPIPENYDSIHCCKTEKCNN
Adrenergic toxin rho-elapitoxin-Dp1b (rho-EPTX-Dp1b) (Muscarinic toxin CM-3) (Protein CM-3)
Dendroaspis polylepis polylepis (Black mamba)
8,620
65
7,344
Direct protein sequencing;Disulfide bond;G-protein coupled receptor impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4029488}.
null
null
PF21947;
IPR003572;IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
5
row_3776
false
null
6,740
P25681
TICYSHTTTSRAILKDCGENSCYRKSRRHPPKMVLGRGCGCPPGDDYLEVKCCTSPDKCNY
Acetylcholinesterase toxin C (Fasciculin)
Dendroaspis polylepis polylepis (Black mamba)
8,620
61
6,817
Direct protein sequencing;Disulfide bond;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
6
row_6488
false
null
1,321
P00979
QPLRKLCILHRNPGRCYQKIPAFYYNQKKKQCEGFTWSGCGGNSNRFKTIEECRRTCIRK
Kunitz-type serine protease inhibitor homolog dendrotoxin I (DTX-I) (Dendrotoxin-1) (Venom basic protease inhibitor 1)
Dendroaspis polylepis polylepis (Black mamba)
8,620
60
7,155
3D-structure;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Potassium channel impairing toxin;Secreted;Toxin;Voltage-gated potassium channel impairing toxin
GO:0004867; GO:0005615; GO:0015459; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted.
null
null
PF00014;
IPR002223;IPR036880;IPR020901;IPR050098;
1DEM;1DEN;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
7
row_1262
false
null
3,051
P01414
RICYSHKASLPRATKTCVENTCYKMFIRTHRQYISERGCGCPTAMWPYQTECCKGDRCNK
Toxin FS-2 (FS2)
Dendroaspis polylepis polylepis (Black mamba)
8,620
60
7,026
3D-structure;Calcium channel impairing toxin;Cardiotoxin;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Secreted;Toxin;Voltage-gated calcium channel impairing toxin
GO:0005246; GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:880951}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
1TFS;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
8
row_2949
false
null
3,052
P01416
RICYNHQSTTRATTKSCEENSCYKKYWRDHRGTIIERGCGCPKVKPGVGIHCCQSDKCNY
Short neurotoxin 1 (Neurotoxin alpha)
Dendroaspis polylepis polylepis (Black mamba)
8,620
60
6,915
3D-structure;Acetylcholine receptor inhibiting toxin;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Toxin
GO:0005576; GO:0030550; GO:0090729; GO:0099106
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:5033401}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
1NTX;8V13;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
9
row_2950
false
null
3,033
P00984
LQHRTFCKLPAEPGPCKASIPAFYYNWAAKKCQLFHYGGCKGNANRFSTIEKCRHACVG
Kunitz-type serine protease inhibitor dendrotoxin E (DTX-E) (Protein E) (Venom basic protease inhibitor E)
Dendroaspis polylepis polylepis (Black mamba)
8,620
59
6,620
Copper;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Potassium channel impairing toxin;Protease inhibitor;Secreted;Serine protease inhibitor;Toxin;Voltage-gated potassium channel impairing toxin
GO:0004867; GO:0005576; GO:0015459; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:668688}.
null
null
PF00014;
IPR002223;IPR036880;IPR020901;IPR050098;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
10
row_2932
false
null
1,322
P00983
RPYACELIVAAGPCMFFISAFYYSKGANKCYPFTYSGCRGNANRFKTIEECRRTCVV
Mambaquaretin-7 (MQ7) (Kunitz-type serine protease inhibitor homolog dendrotoxin B) (DTX-B) (Mambaquaretin-8) (MQ8) (Protein B) (Upsilon-Dp2b) (Upsilon-Dp2c) (Venom basic protease inhibitor B)
Dendroaspis polylepis polylepis (Black mamba)
8,620
57
6,476
Direct protein sequencing;Disulfide bond;G-protein coupled receptor impairing toxin;Secreted;Toxin
GO:0004867; GO:0005615; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7309000}.
null
null
PF00014;
IPR002223;IPR036880;IPR020901;IPR050098;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
11
row_1263
false
null
1,504
P0DKS3
LKCFQHGKVVTCHRDMKFCYHNTGMPFRNLKLILQGCSSSCSETENNKCCSTDRCNK
Mambalgin-2 (Ma-2) (Mamb-2) (Pi-Dp2)
Dendroaspis polylepis polylepis (Black mamba)
8,620
57
6,547
3D-structure;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Pharmaceutical;Proton-gated sodium channel impairing toxin;Secreted;Toxin
GO:0005576; GO:0090729; GO:0099106
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23034652}.
null
null
PF21947;
IPR003571;IPR045860;IPR054131;
2MFA;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
12
row_1441
false
null
2,406
A0A4P1LYC9
TICHIQISKTHGILKTCEENSCYKMSVRGWIIGRGCGCPSAVRPRQVQCCTSDKCNY
Dendroaspis polylepis MT9 (Three-finger toxin) (3FTx)
Dendroaspis polylepis polylepis (Black mamba)
8,620
57
6,364
3D-structure;Direct protein sequencing;Disulfide bond;G-protein coupled acetylcholine receptor impairing toxin;G-protein coupled receptor impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
6R5M;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
13
row_2319
false
null
2,662
C0HLA6
RPSFCNLPVKPGPCNGFFSAFYYSQKKNKCHSFTYGGCKGNANRFSTIEECRRTCVG
Mambaquaretin-3 (MQ3) (Upsilon-Dp2a)
Dendroaspis polylepis polylepis (Black mamba)
8,620
57
6,405
Direct protein sequencing;Disulfide bond;G-protein coupled receptor impairing toxin;Secreted;Toxin
GO:0004867; GO:0005615; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:35122240}.
null
null
PF00014;
IPR002223;IPR036880;IPR020901;IPR050098;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
null
true
Dendroaspis polylepis
14
row_2572
false
null
1,665
P19855
MKLLLLLIVSASMLIESLVNADGYIRKRDGCKLSCLFGNEGCNKECKSYGGSYGYCWTWGLACWCEGLPDDKTWKSETNTCG
Beta-insect depressant toxin LqqIT2 (Insect toxin 2)
Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) (Deathstalker scorpion)
6,885
82
9,100
Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Secreted;Signal;Toxin;Voltage-gated sodium channel impairing toxin
GO:0005576; GO:0006952; GO:0019871; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2029523, ECO:0000269|PubMed:2311768, ECO:0000269|PubMed:8431601}.
SIGNAL 1..21; /evidence="ECO:0000269|PubMed:2029523, ECO:0000269|PubMed:2311768, ECO:0000269|PubMed:8431601"
null
PF00537;
IPR044062;IPR003614;IPR036574;IPR018218;IPR002061;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Chelicerata (subphylum), Arachnida (class), Scorpiones (order), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Leiurus (genus), Leiurus quinquestriatus (species)
null
true
Leiurus quinquestriatus
0
row_1594
false
null
3,889
P19856
KKNGYAVDSSGKAPECLLSNYCYNECTKVHYADKGYCCLLSCYCVGLSDDKKVLEISDARKKYCDFVTIN
Beta-insect excitatory toxin LqqIT1 (Insect toxin 1) (LqqIT1')
Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) (Deathstalker scorpion)
6,885
70
7,849
Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Secreted;Toxin;Voltage-gated sodium channel impairing toxin
GO:0005576; GO:0006952; GO:0019871; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2311768}.
null
null
PF00537;
IPR044062;IPR003614;IPR036574;IPR002061;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Chelicerata (subphylum), Arachnida (class), Scorpiones (order), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Leiurus (genus), Leiurus quinquestriatus (species)
null
true
Leiurus quinquestriatus
1
row_3734
false
null
196
P01489
GVRDAYIADDKNCVYTCGSNSYCNTECTKNGAESGYCQWLGKYGNACWCIKLPDKVPIRIPGKCR
Alpha-toxin Lqq4 (Lqq IV) (LqqIV) (Toxin IV)
Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) (Deathstalker scorpion)
6,885
65
7,202
3D-structure;Amidation;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Secreted;Toxin;Voltage-gated sodium channel impairing toxin
GO:0005576; GO:0006952; GO:0019871; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:37501371, ECO:0000269|Ref.1}.
null
null
PF00537;
IPR044062;IPR003614;IPR036574;IPR018218;IPR002061;
8BO0;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Chelicerata (subphylum), Arachnida (class), Scorpiones (order), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Leiurus (genus), Leiurus quinquestriatus (species)
null
true
Leiurus quinquestriatus
2
row_183
false
null
1,338
P01481
LKDGYIVDDKNCTFFCGRNAYCNDECKKKGGESGYCQWASPYGNACWCYKLPDRVSIKEKGRCN
Alpha-mammal toxin Lqq5 (Lqq V) (LqqV) (Neurotoxin V)
Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) (Deathstalker scorpion)
6,885
64
7,301
Amidation;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Secreted;Toxin;Voltage-gated sodium channel impairing toxin
GO:0005576; GO:0006952; GO:0019871; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:658402}.
null
null
PF00537;
IPR044062;IPR003614;IPR036574;IPR018218;IPR002061;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Chelicerata (subphylum), Arachnida (class), Scorpiones (order), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Leiurus (genus), Leiurus quinquestriatus (species)
null
true
Leiurus quinquestriatus
3
row_1279
false
null
3,094
P01487
VRDAYIAKNYNCVYECFRDSYCNDLCTKNGASSGYCQWAGKYGNACWCYALPDNVPIRVPGKCH
Alpha-insect toxin Lqq3 (Lqq III) (LqqIII)
Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) (Deathstalker scorpion)
6,885
64
7,240
3D-structure;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Secreted;Toxin;Voltage-gated sodium channel impairing toxin
GO:0005576; GO:0006952; GO:0019871; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted.
null
null
PF00537;
IPR044062;IPR003614;IPR036574;IPR018218;IPR002061;
1LQQ;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Chelicerata (subphylum), Arachnida (class), Scorpiones (order), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Leiurus (genus), Leiurus quinquestriatus (species)
null
true
Leiurus quinquestriatus
4
row_2992
false
null
3,996
P45639
MCMPCFTTDHQMARKCDDCCGGKGRGKCYGPQCLCR
Chlorotoxin (CTX) (ClTx) (Tozuleristide)
Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) (Deathstalker scorpion)
6,885
36
4,005
3D-structure;Chloride channel impairing toxin;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Knottin;Metalloenzyme inhibitor;Metalloprotease inhibitor;Neurotoxin;Protease inhibitor;Secreted;Toxin;Voltage-gated chloride channel impairing toxin
GO:0005576; GO:0017081; GO:0030414; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8383429}.
null
null
PF05294;
IPR036574;IPR007958;
1CHL;5L1C;6ATW;7SOH;7X41;7X43;7X44;7X4D;8C5G;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Chelicerata (subphylum), Arachnida (class), Scorpiones (order), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Leiurus (genus), Leiurus quinquestriatus (species)
null
true
Leiurus quinquestriatus
5
row_3839
false
null
6,757
P45661
GLIDVRCYDSSQCE
Leiurutoxin-3 (Leiurutoxin III) (Potassium channel toxin alpha-KTx)
Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) (Deathstalker scorpion)
6,885
14
1,588
Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Potassium channel impairing toxin;Secreted;Toxin
GO:0005576; GO:0015459; GO:0090729
Evidence at protein level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1280139}.
null
null
null
null
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Chelicerata (subphylum), Arachnida (class), Scorpiones (order), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Leiurus (genus), Leiurus quinquestriatus (species)
null
true
Leiurus quinquestriatus
6
row_6505
false
null
232
P09545
MPKLNRCAIAIFTILSAISSPTLLANINEPSGEAADIISQVADSHAIKYYNAADWQAEDNALPSLAELRDLVINQQKRVLVDFSQISDAEGQAEMQAQFRKAYGVGFANQFIVITEHKGELLFTPFDQAEEVDPQLLEAPRTARLLARSGFASPAPANSETNTLPHVAFYISVNRAISDEECTFNNSWLWKNEKGSRPFCKDANISLIYRVNLERSLQYGIVGSATPDAKIVRISLDDDSTGAGIHLNDQLGYRQFGASYTTLDAYFREWSTDAIAQDYRFVFNASNNKAQILKTFPVDNINEKFERKEVSGFELGVTGGVEVSGDGPKAKLEARASYTQSRWLTYNTQDYRIERNAKNAQAVSFTWNRQQYATAESLLNRSTDALWVNTYPVDVNRISPLSYASFVPKMDVIYKASATETGSTDFIIDSSVNIRPIYNGAYKHYYVVGAHQSYHGFEDTPRRRITKSASFTVDWDHPVFTGGRPVNLQLASFNNRCIQVDAQGRLAANTCDSQQSAQSFIYDQLGRYVSASNTKLCLDGEALDALQPCNQNLTQRWEWRKGTDELTNVYSGESLGHDKQTGELGLYASSNDAVSLRTITAYTDVFNAQESSPILGYTQGKMNQQRVGQDHRLYVRAGAAIDALGSASDLLVGGNGGSLSSVDLSGVKSITATSGDFQYGGQQLVALTFTYQDGRQQTVGSKAYVTNAHEDRFDLPAAAKITQLKIWSDDWLVKGVQFDLN
Hemolysin
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
243,277
741
81,962
3D-structure;Cytolysis;Direct protein sequencing;Disulfide bond;Hemolysis;Host cell membrane;Host membrane;Lectin;Membrane;Reference proteome;Secreted;Signal;Toxin;Transmembrane;Transmembrane beta strand;Virulence
GO:0005576; GO:0016020; GO:0020002; GO:0030246; GO:0042802; GO:0051715; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15978620}. Host cell membrane {ECO:0000269|PubMed:15978620}; Multi-pass membrane protein {ECO:0000269|PubMed:15978620}. Note=In the hemolytic biotype El Tor the 80 kDa hemolysin precursor is secreted as monomer. After binding to target membranes the protein assembles into a heptameric prepore complex. Proteolytic cleavage triggers a conformation change that is required for membrane insertion and pore formation.
SIGNAL 1..25; /evidence="ECO:0000269|PubMed:2174833"
null
PF16458;PF12563;PF07968;
IPR032496;IPR022220;IPR043080;IPR044883;IPR036404;IPR016183;IPR036435;IPR035992;IPR000772;
1XEZ;3O44;4GX7;7YL9;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species), Vibrio cholerae O1 (serogroup), Vibrio cholerae serotype O1 biovar El Tor (no rank)
hlyA VC_A0219
true
Vibrio cholerae
0
row_217
false
null
6,755
P38442
MSIFIHHGAPGSYKTSGALWLRLLPAIKSGRHIITNVRGLNLERMAKYLKMDVSDISIEFIDTDHPDGRLTMARFWHWARKDAFLFIDECGRIWPPRLTVTNLKALDTPPDLVAEDRPESFEVAFDMHRHHGWDICLTTPNIAKVHNMIREAAEIGYRHFNRATVGLGAKFTLTTHDAANSGQMDSHALTRQVKKIPSPIFKMYASTTTGKARDTMAGTALWKDRKILFLFGMVFLMFSYSFYGLHDNPIFTGGNDATIESEQSEPQSKATVGNAVGSKAVAPASFGFCIGRLCVQDGFVTVGDERYRLVDNLDIPYRGLWATGHHIYKDTLTVFFETESGSVPTELFASSYRYKVLPLPDFNHFVVFDTFAAQALWVEVKRGLPIKTENDKKGLNSIF
Zona occludens toxin (Zonular occludens toxin) (Zot)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
243,277
399
44,903
Enterotoxin;Reference proteome;Toxin;Virulence
GO:0090729
Evidence at protein level
2
null
null
null
PF05707;
IPR027417;IPR008900;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species), Vibrio cholerae O1 (serogroup), Vibrio cholerae serotype O1 biovar El Tor (no rank)
zot VC_1458
true
Vibrio cholerae
1
row_6503
false
null
207
P01555
MVKIIFVFFIFLSSFSYANDDKLYRADSRPPDEIKQSGGLMPRGQSEYFDRGTQMNINLYDHARGTQTGFVRHDDGYVSTSISLRSAHLVGQTILSGHSTYYIYVIATAPNMFNVNDVLGAYSPHPDEQEVSALGGIPYSQIYGWYRVHFGVLDEQLHRNRGYRDRYYSNLDIAPAADGYGLAGFPPEHRAWREEPWIHHAPPGCGNAPRSSMSNTCDEKTQSLGVKFLDEYQSKVKRQIFSGYQSDIDTHNRIKDEL
Cholera enterotoxin subunit A (Cholera enterotoxin, A chain) [Cleaved into: Cholera enterotoxin subunit A1 (EC 2.4.2.-) (Cholera enterotoxin A1 chain) (Cholera enterotoxin alpha chain) (NAD(+)--diphthamide ADP-ribosyltransferase); Cholera enterotoxin subunit A2 (Cholera enterotoxin A2 chain) (Cholera enterotoxin gamma chain)]
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
243,277
258
29,336
3D-structure;Direct protein sequencing;Disulfide bond;Enterotoxin;Glycosyltransferase;NAD;Nucleotidyltransferase;Reference proteome;Signal;Toxin;Transferase;Virulence
GO:0005534; GO:0005615; GO:0008289; GO:0016757; GO:0016779; GO:0042531; GO:0042597; GO:0090729; GO:0141104; GO:1902494
Evidence at protein level
5
null
SIGNAL 1..18; /evidence="ECO:0000269|PubMed:7238869, ECO:0000269|PubMed:955672"
null
PF01375;
IPR001144;
1S5B;1S5C;1S5D;1S5E;1S5F;1XTC;2A5D;2A5F;2A5G;8OXS;8Q6I;8QRE;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species), Vibrio cholerae O1 (serogroup), Vibrio cholerae serotype O1 biovar El Tor (no rank)
ctxA toxA VC_1457
true
Vibrio cholerae
2
row_194
false
null
208
P01556
MIKLKFGVFFTVLLSSAYAHGTPQNITDLCAEYHNTQIYTLNDKIFSYTESLAGKREMAIITFKNGAIFQVEVPGSQHIDSQKKAIERMKDTLRIAYLTEAKVEKLCVWNNKTPHAIAAISMAN
Cholera enterotoxin subunit B (Cholera enterotoxin B chain) (Cholera enterotoxin gamma chain) (Choleragenoid)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
243,277
124
13,957
3D-structure;Direct protein sequencing;Disulfide bond;Enterotoxin;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Signal;Toxin;Virulence
GO:0005534; GO:0005576; GO:0016020; GO:0020002; GO:0042531; GO:0042597; GO:0046812; GO:0090729; GO:1902494
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
SIGNAL 1..21; /evidence="ECO:0000269|PubMed:903362, ECO:0000269|PubMed:903363"
null
PF01376;
IPR008992;IPR001835;
1CHP;1CHQ;1CT1;1FGB;1G8Z;1JR0;1MD2;1RCV;1RD9;1RDP;1RF2;1S5B;1S5C;1S5D;1S5E;1S5F;1XTC;2CHB;3CHB;3EFX;5ELC;5ELE;5ELF;5LZG;5LZJ;6HJD;6HMW;6HMY;6HSV;7LVB;8OXS;8Q6I;8QRE;9EWF;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species), Vibrio cholerae O1 (serogroup), Vibrio cholerae serotype O1 biovar El Tor (no rank)
ctxB toxB VC_1456
true
Vibrio cholerae
3
row_195
false
null
6,754
P38441
MLMMDTLYDWLIDGFTWLVIKLGIMWIESKIFVIQFFWEMSQKVIDMFTIYPLIQQAIDMLPPQYSGFLFFLGLDQALAIVLQALMTRFALRALNL
Accessory cholera enterotoxin (Ace)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
243,277
96
11,347
Enterotoxin;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Toxin;Transmembrane;Transmembrane helix;Virulence
GO:0005576; GO:0016020; GO:0020002; GO:0090729
Predicted
2
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
null
TRANSMEM 76..96; /note="Helical"; /evidence="ECO:0000255"
PF10734;
IPR019670;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Vibrionales (order), Vibrionaceae (family), Vibrio (genus), Vibrio cholerae (species), Vibrio cholerae O1 (serogroup), Vibrio cholerae serotype O1 biovar El Tor (no rank)
ace VC_1459
true
Vibrio cholerae
4
row_6502
false
null
212
P04512
MEKLTDLNYTLSVITLMNNTLHTILEDPGMAYFPYIASVLTGLFALNKASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMDRVVKEMRRQLEMIDKLTTREIEQVELLKRIYDKLTVQTTGEIDMTKEINQKNVRTLEEWESGKNPYEPREVTAAM
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain Both))
37,137
175
20,267
3D-structure;Activation of host autophagy by virus;Calcium;Direct protein sequencing;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Reference proteome;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08434, ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091, ECO:0000269|PubMed:17376898}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091, ECO:0000269|PubMed:17035333}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
null
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
PF01452;
IPR002107;
1G1I;1G1J;2O1K;
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Simian rotavirus A (no rank), Simian rotavirus A/SA11 (no rank)
null
true
Rotavirus A
0
row_199
false
null
958
B3SRV6
MDKLADLNYTLSVITLMNDTLHSIIQDPGMAYFPYIASVLTVLFTLHKASIPTMKIALKTSKCSYKVIKYCIVTIINTLLKLAGYKEQVTTKDEIEQQMDRIVKEMRRQLEMIDKLTTREIEQVELLKRIHDNLITRSVDVIDMSKEFNQKNIKTLDEWESGKNPYEPSEVTASM
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
Rotavirus A (strain RVA/Human/United States/P/1974/G3P1A[8]) (RV-A)
10,957
175
20,237
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
Inferred from homology
4
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
null
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
PF01452;
IPR002107;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G3 (no rank)
null
true
Rotavirus A
1
row_903
false
null
1,293
O11982
MEKLADLNYTLGVITLLNDTLHNILEEPGMVYFPYVASALTVLFTMHKASLPAMKLAMRTSQCSYRIIKRVVVTLINTLLRLGGYNDYLTDKDETEKQINRVVKELRQQLTMIEKLTTREIEQVELLKRIYDMMVVRHDREIDMSKETNQKAFNTLHDWGNDRNYDDNTDVIAPL
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
Rotavirus A (isolate RVA/Mouse/Brazil/EHP/1981/G16P[20]) (RV-A)
578,840
175
20,413
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
Evidence at transcript level
4
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
null
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
PF01452;
IPR002107;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G16 (no rank)
null
true
Rotavirus A
2
row_1234
false
null
1,303
O56850
MEKLTDLNYTLSVITLMNDTLHTIMEDPGMAYFPYIASVLTVLFTLHKASIPTMKIALRTSRCSYKVIKYCIVSIFNTLLKLAGYKEQITTKDEIEKQMDRVVKEMRRQLEMIDKLTTREIEQVELLKRIHDMLIIKPVDKIDMSQEFNQRQFKTLNEWAEGENPYEPKEVTASL
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
Rotavirus A (strain RVA/Human/Japan/AU-1/1982/G3P3[9]) (RV-A)
39,013
175
20,513
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
Evidence at transcript level
4
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
null
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
PF01452;
IPR002107;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G3 (no rank)
null
true
Rotavirus A
3
row_1244
false
null
1,694
P30031
MEKLTVLNYTLNVITLMNSTLHTILEDPGMAYFPYIASVLTVLFTLHRASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLADYKEQITTKDEIEKQMDRVAKEMRRQLEMIDKLTTREIEQVKLLKRIYDKLMVRATDGIDMTKEINQKNVKTLEEWKSGKNPYEPKEVTAAM
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
Rotavirus A (isolate RVA/Human/United Kingdom/A64/1987/G10P11[14]) (RV-A)
578,827
175
20,360
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
Inferred from homology
4
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
null
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
PF01452;
IPR002107;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G10 (no rank), Rotavirus G10P11 (no rank)
null
true
Rotavirus A
4
row_1623
false
null
2,034
Q3ZK64
MDKLTDLNYTLSVITLMNSTLHKILEDPGMAYFPYIASVLTVLFTLHKASIPTMKIALKTSRCSYKVIKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMDRVVREMRRQLEMIDKLTTREIEQVELLRRIYDRLTVQKTDEIDMSKEINQKNVRTLDEWENGKNPYEPSEVTASL
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
Rotavirus A (isolate RVA/Human/Belgium/B4106/2000/G3P11[14]) (RV-A) (Rotavirus A (isolate B4106))
578,843
175
20,487
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
Inferred from homology
4
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
null
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
PF01452;
IPR002107;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G3 (no rank)
null
true
Rotavirus A
5
row_1952
false
null
2,280
Q9PYC8
MEKLTDLNYTLSVITLMNSTLHTILEDPGMAYFPYIASVLTVLFTLHKASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMERVVKEMRRHFKMIDKLTTREIEQVGLLKRIHDKLDIRAVDEIDMTKEINQKNVRTLEEWEWGKNPYEPKEVTAAM
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
Rotavirus A (isolate RVA/Cow/United States/B223/1983/G10P8[11]) (RV-A)
1,835,656
175
20,446
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
Inferred from homology
4
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
null
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
PF01452;
IPR002107;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G10 (no rank), Rotavirus G10P11 (no rank)
null
true
Rotavirus A
6
row_2196
false
null
2,295
Q9WAI7
MDKLADLNYTLSVVTLMNDTLHSIIQDPGMAYFPYVASVLTVLFALHKASIPTMKMALKTSKCSYKVIKYCIVPIINTLFKLAGFQEPITTKDEIEQPMDGIVKEIRRPLEMIDKLTTPEIEQVELLKSLHDHLITRPVDVIDMSKEFNQKNIKTLDEWDSGKNPYEPSEVTASM
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
Rotavirus A (strain RVA/Human/Japan/MO/1982/G3P1A[8]) (RV-A)
10,956
175
19,905
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
Inferred from homology
4
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
null
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
PF01452;
IPR002107;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Rotavirus G1 (no rank)
null
true
Rotavirus A
7
row_2211
false
null
2,187
Q8V790
MENATTINETLVEEVYNMTMSYFEHNVIIMKYFPFLASILTIAFTAWKMGKSTFKVTKTVAGSGFKVVRVIVITIFNCIMRLFGSKTEIVSDDRLDALASKILAQINNQVKVIEQLTKRELEQVKLLADIYEMLKFKKDEVDMSFETNKKEYEKWVKDPYQPTRAVSLD
Non-structural glycoprotein 4 (NSP4) (NCVP5) (NS28)
Rotavirus A (strain RVA/Turkey/Ireland/Ty-1/1978/G7P[17]) (RV-A)
12,584
169
19,572
Activation of host autophagy by virus;Calcium;Enterotoxin;Glycoprotein;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Ion channel;Ion transport;Membrane;Metal-binding;Secreted;Signal-anchor;Toxin;Transmembrane;Transmembrane helix;Transport;Viral ion channel;Virulence
GO:0005576; GO:0015267; GO:0016020; GO:0016032; GO:0034220; GO:0039520; GO:0044155; GO:0044169; GO:0046872; GO:0090729
Inferred from homology
4
SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Host membrane, host caveola {ECO:0000255|HAMAP-Rule:MF_04091}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04091}. Secreted {ECO:0000255|HAMAP-Rule:MF_04091}. Note=NSP4 also localizes in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus-infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. {ECO:0000255|HAMAP-Rule:MF_04091}.
null
TRANSMEM 29..51; /note="Helical; Signal-anchor for type III membrane protein"; /evidence="ECO:0000255|HAMAP-Rule:MF_04091"
PF01452;
IPR002107;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus A (species), Avian rotavirus A (no rank)
null
true
Rotavirus A
8
row_2103
false
null
215
P04977
MRCTRAIRQTARTGWLTWLAILAVTAPVTSPAWADDPPATVYRYDSRPPEDVFQNGFTAWGNNDNVLDHLTGRSCQVGSSNSAFVSTSSSRRYTEVYLEHRMQEAVEAERAGRGTGHFIGYIYEVRADNNFYGAASSYFEYVDTYGDNAGRILAGALATYQSEYLAHRRIPPENIRRVTRVYHNGITGETTTTEYSNARYVSQQTRANPNPYTSRRSVASIVGTLVRMAPVIGACMARQAESSEAMAAWSERAGEAMVLVYYESIAYSF
Pertussis toxin subunit 1 (PTX S1) (Islet-activating protein S1) (IAP S1) (NAD-dependent ADP-ribosyltransferase) (EC 2.4.2.-)
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
257,313
269
29,974
3D-structure;Direct protein sequencing;Disulfide bond;Glycosyltransferase;NAD;Nucleotidyltransferase;Pharmaceutical;Reference proteome;Secreted;Signal;Toxin;Transferase;Virulence;Whooping cough
GO:0003950; GO:0005576; GO:0016779; GO:0090729; GO:0141104
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11854200}. Note=The individual chains are secreted by a sec-dependent mechanism into the periplasm. Then, S1 associates with the outer membrane before it joins with the B subunit to form the secretion-competent holotoxin. The type IV secretion system ptl mediates secretion of assembled toxin through the outer membrane.
SIGNAL 1..34
null
PF02917;
IPR003898;
1BCP;1PRT;1PTO;6RO0;7SKI;7SKK;7SKY;7SNE;7U6Z;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
ptxA BP3783
true
Bordetella pertussis
0
row_201
false
null
3,124
P04979
MLINNKKLLHHILPILVLALLGMRTAQAVAPGIVIPPKALFTQQGGAYGRCPNGTRALTVAELRGNAELQTYLRQITPGWSIYGLYDGTYLGQAYGGIIKDAPPGAGFIYRETFCITTIYKTGQPAADHYYSKVTATRLLASTNSRLCAVFVRDGQSVIGACASPYEGRYRDMYDALRRLLYMIYMSGLAVRVHVSKEEQYYDYEDATFQTYALTGISLCNPAASIC
Pertussis toxin subunit 3 (PTX S3) (Islet-activating protein S3) (IAP S3)
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
257,313
227
24,988
3D-structure;Disulfide bond;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Signal;Toxin;Virulence;Whooping cough
GO:0005576; GO:0016020; GO:0020002; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
SIGNAL 1..28
null
PF03440;PF02918;
IPR005138;IPR037015;IPR016187;IPR008992;IPR003899;IPR020063;
1BCP;1PRT;1PTO;6RO0;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
ptxC BP3787
true
Bordetella pertussis
1
row_3022
false
null
1,355
P04978
MPIDRKTLCHLLSVLPLALLGSHVARASTPGIVIPPQEQITQHGGPYGRCANKTRALTVAELRGSGDLQEYLRHVTRGWSIFALYDGTYLGGEYGGVIKDGTPGGAFDLKTTFCIMTTRNTGQPATDHYYSNVTATRLLSSTNSRLCAVFVRSGQPVIGACTSPYDGKYWSMYSRLRKMLYLIYVAGISVRVHVSKEEQYYDYEDATFETYALTGISICNPGSSLC
Pertussis toxin subunit 2 (PTX S2) (Islet-activating protein S2) (IAP S2)
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
257,313
226
24,799
3D-structure;Disulfide bond;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Signal;Toxin;Virulence;Whooping cough
GO:0005576; GO:0016020; GO:0020002; GO:0090729; GO:0141071
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
SIGNAL 1..27
null
PF03440;PF02918;
IPR005138;IPR037015;IPR016187;IPR008992;IPR003899;IPR020063;
1BCP;1PRT;1PTO;6RO0;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
ptxB BP3784
true
Bordetella pertussis
2
row_1296
false
null
3,161
P0A3R5
MLRRFPTRTTAPGQGGARRSRVRALAWLLASGAMTHLSPALADVPYVLVKTNMVVTSVAMKPYEVTPTRMLVCGIAAKLGAAASSPDAHVPFCFGKDLKRPGSSPMEVMLRAVFMQQRPLRMFLGPKQLTFEGKPALELIRMVECSGKQDCP
Pertussis toxin subunit 4 (PTX S4) (Islet-activating protein S4) (IAP S4)
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
257,313
152
16,544
3D-structure;Disulfide bond;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Signal;Toxin;Virulence;Whooping cough
GO:0005576; GO:0016020; GO:0020002; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
SIGNAL 1..42
null
PF09275;
IPR008992;IPR015355;
1BCP;1PRT;1PTO;6RO0;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
ptxD BP3785
true
Bordetella pertussis
3
row_3048
false
null
3,125
P04981
MQRQAGLPLKANPMHTIASILLSVLGIYSPADVAGLPTHLYKNFTVQELALKLKGKNQEFCLTAFMSGRSLVRACLSDAGHEHDTWFDTMLGFAISAYALKSRIALTVEDSPYPGTPGDLLELQICPLNGYCE
Pertussis toxin subunit 5 (PTX S5) (Islet-activating protein S5) (IAP S5)
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
257,313
133
14,500
3D-structure;Disulfide bond;Host cell membrane;Host membrane;Membrane;Reference proteome;Secreted;Signal;Toxin;Virulence;Whooping cough
GO:0005576; GO:0016020; GO:0020002; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305}.
SIGNAL 1..34
null
PF09276;
IPR008992;IPR015356;
1BCP;1PRT;1PTO;6RO0;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Alcaligenaceae (family), Bordetella (genus), Bordetella pertussis (species)
ptxE BP3786
true
Bordetella pertussis
4
row_3023
false
null
231
P09385
MKCILFKWVLCLLLGFSSVSYSREFTIDFSTQQSYVSSLNSIRTEISTPLEHISQGTTSVSVINHTPPGSYFAVDIRGLDVYQARFDHLRLIIEQNNLYVAGFVNTATNTFYRFSDFTHISVPGVTTVSMTTDSSYTTLQRVAALERSGMQISRHSLVSSYLALMEFSGNTMTRDASRAVLRFVTVTAEALRFRQIQREFRQALSETAPVYTMTPGDVDLTLNWGRISNVLPEYRGEDGVRVGRISFNNISAILGTVAVILNCHHQGARSVRAVNEESQPECQITGDRPVIKINNTLWESNTAAAFLNRKSQFLYTTGK
Shiga-like toxin 2 subunit A (SLT-2 A subunit) (SLT-2a) (SLT-IIa) (EC 3.2.2.22) (Verocytotoxin 2 subunit A) (Verotoxin 2 subunit A) (rRNA N-glycosidase 2)
Escherichia phage 933W (Bacteriophage 933W)
10,730
319
35,714
3D-structure;Disulfide bond;Hydrolase;Modulation of host virulence by virus;Protein synthesis inhibitor;Reference proteome;Secreted;Signal;Toxin;Viral exotoxin;Virulence
GO:0005576; GO:0017148; GO:0030598; GO:0090729; GO:0098676
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..22; /evidence="ECO:0000255"
null
PF00161;
IPR036041;IPR001574;IPR017988;IPR016138;IPR016139;IPR016331;
1R4P;2GA4;7UJJ;8SZ2;
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
stxA2 stx2A L0103
true
Traversvirus tv933W
0
row_216
false
null
1,365
P09386
MKKMFMAVLFALASVNAMAADCAKGKIEFSKYNEDDTFTVKVDGKEYWTSRWNLQPLLQSAQLTGMTVTIKSSTCESGSGFAEVQFNND
Shiga-like toxin 2 subunit B (SLT-2 B subunit) (SLT-2b) (SLT-IIb) (Verocytotoxin 2 subunit B) (Verotoxin 2 subunit B)
Escherichia phage 933W (Bacteriophage 933W)
10,730
89
9,874
3D-structure;Disulfide bond;Modulation of host virulence by virus;Reference proteome;Secreted;Signal;Toxin;Viral exotoxin;Virulence
GO:0005576; GO:0019836; GO:0090729; GO:0098676
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..19; /evidence="ECO:0000255"
null
PF02258;
IPR008992;IPR003189;
1R4P;2GA4;6FE4;7UJJ;
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
stxB2 stx2B L0104
true
Traversvirus tv933W
1
row_1306
false
null
715
Q805F6
MIQVLLVTLCLAAFPYQGSSIILESGNVNDYEVLYPQKVIALPKGAVQPKYEDTMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSSDGRKITTNPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGETYLIEPLKLPDSEAHAVYKYENVEKEDEAPKMCGVTQTNWKSDKPIKKASQLNLTPEQQGFPQRYIELVVVADHRMFTKYNSNLNTIRIWVHELVNTMNVFYRPLNIRVSLTDLEVWSNRDLINVQPAAADTLEAFGDWRETVLLNRISHDNAQLLTAIELDGETIGLANRGTMCDPKLSTGIVQDHSAINLWVAVTMAHEMGHNLGISHDGNQCHCDANSCIMSEELREQLSFEFSDCSQNQYQTYLTDHNPQCMLNEPLRTDIVSTPVSGNELLETGEESDFDAPANPCCDAATCKLTTGSQCADGLCCDQCKFMKEGTVCRRARGDDLDDYCNGISAGCPRNPFHA
Zinc metalloproteinase/disintegrin [Cleaved into: Snake venom metalloproteinase (SVMP) (EC 3.4.24.-); Disintegrin acostatin-beta]
Agkistrodon contortrix contortrix (Southern copperhead)
8,713
483
54,026
3D-structure;Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Signal;Toxin;Zinc;Zymogen
GO:0004222; GO:0005576; GO:0005886; GO:0006508; GO:0046872; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF00200;PF01562;PF01421;
IPR018358;IPR001762;IPR036436;IPR024079;IPR001590;IPR002870;IPR034027;
3C05;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Agkistrodon (genus), Agkistrodon contortrix (species)
null
true
Agkistrodon contortrix
0
row_669
false
null
518
P82981
VVGGDECNINEHRFLVAIFNSNGFVCSGTLINQEWVLTAAHCDSTDFQIKLGAHSKKVLNEDEQIRNPKEKFICPNKKNDEVLDKDIMLIKLDSRVSNSEHIAPLSLPSSPPSVGSVCHIMGWGSITPIEVTFPDVPHCAYINLLDDAACQPGYPEVLPEYRTLCAGILEGGKDTCNYDSGGPLICNGQFQGIVSYGAHPCGQSLKPGIYTKVFDYNDWIQSIIAGNTAATCPP
Thrombin-like enzyme contortrixobin (SVTLE) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP) (Venombin B)
Agkistrodon contortrix contortrix (Southern copperhead)
8,713
234
25,413
Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin
GO:0004252; GO:0005576; GO:0006508; GO:0030141; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
null
null
PF00089;
IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Agkistrodon (genus), Agkistrodon contortrix (species)
null
true
Agkistrodon contortrix
1
row_482
false
null
234
P09872
VIGGDECNINEHRFLALVYANGSLCGGTLINQEWVLTARHCDRGNMRIYLGMHNLKVLNKDALRRFPKEKYFCLNTRNDTIWDKDIMLIRLNRPVRNSAHIAPLSLPSNPPSVGSVCRIMGWGTITSPNATLPDVPHCANINILDYAVCQAAYKGLAATTLCAGILEGGKDTCKGDSGGPLICNGQFQGILSVGGNPCAQPRKPGIYTKVFDYTDWIQSIISGNTDATCPP
Protein C activator (EC 3.4.21.-) (ACC-C) (Snake venom serine protease) (SVSP)
Agkistrodon contortrix contortrix (Southern copperhead)
8,713
231
25,106
3D-structure;Blood coagulation cascade inhibiting toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin
GO:0004252; GO:0005576; GO:0006508; GO:0030141; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
null
null
PF00089;
IPR009003;IPR043504;IPR001314;IPR001254;IPR033116;
2AIP;2AIQ;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Agkistrodon (genus), Agkistrodon contortrix (species)
null
true
Agkistrodon contortrix
2
row_219
false
null
407
P28891
QQRFPQRYVQLVIVADHRMNTKYNGDSDKIRQWVHQIVNTINEIYRPLNIQFTLVGLEIWSNQDLITVTSVSHDTLASFGNWRETDLLRRQRHDNAQLLTAIDFDGDTVGLAYVGGMCQLKHSTGVIQDHSAINLLVALTMAHELGHNLGMNHDGNQCHCGANSCVMAAMLSDQPSKLFSDCSKKDYQTFLTVNNPQCILNKP
Snake venom metalloproteinase fibrolase (SVMP) (EC 3.4.24.72) (Fibrinolytic metalloproteinase) (Fibrinolytic proteinase) (Alfimeprase)
Agkistrodon contortrix contortrix (Southern copperhead)
8,713
203
22,908
Direct protein sequencing;Disulfide bond;Fibrinolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Pharmaceutical;Protease;Pyrrolidone carboxylic acid;Secreted;Toxin;Zinc
GO:0004222; GO:0005576; GO:0005886; GO:0006508; GO:0046872; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1304358, ECO:0000269|PubMed:1898066}.
null
null
PF01421;
IPR024079;IPR001590;IPR034027;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Agkistrodon (genus), Agkistrodon contortrix (species)
null
true
Agkistrodon contortrix
3
row_373
false
null
968
B8QCG6
FLIGIWAAPKSEDNVPLGSPATSDLSDTSCAKTHEALKTSRNIDQHYPAPKKAEDQEFGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQNVDNANSLNRNIRAKREDHPVHNRGEYSVCDSVNVWVANKTTATDIRGNVVTVMVDVNINNNVYKQYFFETKCRNPNPVPTGCRGIDARHWNSYC
Venom nerve growth factor (v-NGF) (vNGF)
Agkistrodon contortrix contortrix (Southern copperhead)
8,713
190
21,385
Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Growth factor;Lipid-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Secreted;Signal;Toxin
GO:0005163; GO:0005615; GO:0007169; GO:0008021; GO:0008083; GO:0008289; GO:0021675; GO:0030414; GO:0030424; GO:0030425; GO:0038180; GO:0043524; GO:0048812; GO:0050804; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21801740}.
SIGNAL <1..7; /evidence="ECO:0000255"
null
PF00243;
IPR029034;IPR020408;IPR002072;IPR020425;IPR019846;IPR020433;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Agkistrodon (genus), Agkistrodon contortrix (species)
null
true
Agkistrodon contortrix
4
row_913
false
null
716
Q805F7
MIQVLLVTLCLAVFPYQGSSIILESGNVNDYEVVYPRKVTALPKGAIQPKNPCCDAATCKLTPGSQCAEGLCCDQCKFIKAGKICRRARGDNPDYRCTGQSGDCPRKHFYA
Disintegrin acostatin-alpha [Cleaved into: Disintegrin acostatin-alpha, processed form]
Agkistrodon contortrix contortrix (Southern copperhead)
8,713
111
12,093
3D-structure;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Platelet aggregation inhibiting toxin;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin
GO:0005576; GO:0005886; GO:0007155; GO:0030195; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF00200;
IPR018358;IPR001762;IPR036436;
3C05;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Agkistrodon (genus), Agkistrodon contortrix (species)
null
true
Agkistrodon contortrix
5
row_670
false
null
1,470
P0DF97
MSNKKTFKKYSRVAGLLTAALIIGNLVTANAESNKQNTASTETTTTNEQPKPESSELTTEKAGQKTDDMLNSNDMIKLAPKEMPLESAEKEEKKSEDKKKSEEDHTEEINDKIYSLNYNELEVLAKNGETIENFVPKEGVKKADKFIVIERKKKNINTTPVDISIIDSVTDRTYPAALQLANKGFTENKPDAVVTKRNPQKIHIDLPGMGDKATVEVNDPTYANVSTAIDNLVNQWHDNYSGGNTLPARTQYTESMVYSKSQIEAALNVNSKILDGTLGIDFKSISKGEKKVMIAAYKQIFYTVSANLPNNPADVFDKSVTFKELQRKGVSNEAPPLFVSNVAYGRTVFVKLETSSKSNDVEAAFSAALKGTDVKTNGKYSDILENSSFTAVVLGGDAAEHNKVVTKDFDVIRNVIKDNATFSRKNPAYPISYTSVFLKNNKIAGVNNRTEYVETTSTEYTSGKINLSHQGAYVAQYEILWDEINYDDKGKEVITKRRWDNNWYSKTSPFSTVIPLGANSRNIRIMARECTGLAWEWWRKVIDERDVKLSKEINVNISGSTLSPYGSITYK
Streptolysin O (SLO) (Thiol-activated cytolysin)
Streptococcus pyogenes serotype M3 (strain SSI-1)
193,567
571
63,638
3D-structure;Cytolysis;Hemolysis;Host cell membrane;Host membrane;Lipid-binding;Membrane;Secreted;Signal;Toxin;Transmembrane;Transmembrane beta strand;Virulence
GO:0005576; GO:0015485; GO:0016020; GO:0020002; GO:0031640; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C2J9}. Host cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q04IN8}. Note=Probably secreted as soluble protein by the accessory Sec system (By similarity). It then inserts into the host cell membrane and forms pores formed by transmembrane beta-strands (By similarity). {ECO:0000250|UniProtKB:P0C2J9, ECO:0000250|UniProtKB:Q04IN8}.
SIGNAL 1..33; /evidence="ECO:0000255"
TRANSMEM 260..273; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 280..289; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 358..367; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 375..387; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"
PF17440;PF01289;
IPR035390;IPR038700;IPR001869;IPR036363;IPR036359;
4HSC;
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species), Streptococcus pyogenes serotype M3 (serotype)
slo SPs0132
true
Streptococcus pyogenes
0
row_1409
false
null
242
P0C0J1
MNKKKLGVRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRGDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP
Streptopain (EC 3.4.22.10) (Exotoxin type B) (Group A streptococcal cysteine protease) (Streptococcal cysteine proteinase) (SPE B) (Streptococcus peptidase A) (SPP)
Streptococcus pyogenes serotype M1
301,447
398
43,130
3D-structure;Autocatalytic cleavage;Direct protein sequencing;Host cytoplasm;Hydrolase;Methylation;Protease;Reference proteome;Secreted;Signal;Thiol protease;Toxin;Virulence;Zymogen
GO:0004197; GO:0005576; GO:0005829; GO:0006508; GO:0034050; GO:0042783; GO:0043655; GO:0044164; GO:0051604; GO:0090729; GO:0140321
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7516997}. Host extracellular space {ECO:0000269|PubMed:18160402, ECO:0000269|PubMed:7516997}. Host cytoplasm {ECO:0000269|PubMed:35545676}.
SIGNAL 1..27; /evidence="ECO:0000250|UniProtKB:P0C0J0"
null
PF13734;PF01640;
IPR038765;IPR000200;IPR025896;IPR044934;
2JTC;
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species)
speB SPy_2039 M5005_Spy1735
true
Streptococcus pyogenes
1
row_226
false
null
293
P0DD38
MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP
Streptopain (EC 3.4.22.10) (Exotoxin type B) (SPE B) (Streptococcal cysteine proteinase) (Streptococcus peptidase A) (SPP)
Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315)
198,466
398
43,174
Autocatalytic cleavage;Host cytoplasm;Hydrolase;Methylation;Protease;Secreted;Signal;Thiol protease;Toxin;Virulence;Zymogen
GO:0004197; GO:0005576; GO:0006508; GO:0034050; GO:0042783; GO:0043655; GO:0044164; GO:0090729; GO:0140321
Inferred from homology
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7516997}. Host extracellular space {ECO:0000269|PubMed:7516997}. Host cytoplasm {ECO:0000250|UniProtKB:P0C0J0}.
SIGNAL 1..27; /evidence="ECO:0000250|UniProtKB:P0C0J0"
null
PF13734;PF01640;
IPR038765;IPR000200;IPR025896;IPR044934;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species), Streptococcus pyogenes serotype M3 (serotype)
speB SpyM3_1742
true
Streptococcus pyogenes
2
row_277
false
null
6,821
P62561
MENNKKVLKKMVFFVLVTFLGLTISQEVFAQQDPDPSQLHRSSLVKNLQNIYFLYEGDPVTHENVKSVDQLLSHDLIYNVSGPNYDKLKTELKNQEMATLFKDKNVDIYGVEYYHLCYLCENAERSACIYGGVTNHEGNHLEIPKKIVVKVSIDGIQSLSFDIETNKKMVTAQELDYKVRKYLTDNKQLYTNGPSKYETGYIKFIPKNKESFWFDFFPEPEFTQSKYLMIYKDNETLDSNTSQIEVYLTTK
Exotoxin type A (Erythrogenic toxin) (SPE A) (Scarlet fever toxin)
Streptococcus pyogenes serotype M18 (strain MGAS8232)
186,103
251
29,246
3D-structure;Disulfide bond;Signal;Toxin;Virulence
GO:0005576; GO:0090729
Evidence at protein level
2
null
SIGNAL 1..30; /evidence="ECO:0000250"
null
PF02876;PF01123;
IPR008992;IPR006126;IPR006173;IPR016091;IPR013307;IPR006123;IPR006177;
1L0Y;
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species), Streptococcus pyogenes serotype M18 (serotype)
speA spyM18_0393
true
Streptococcus pyogenes
3
row_6568
false
null
6,085
P0C0I7
MRYNCRYSHIDKKIYSMIICLSFLLYSNVVQANSYNTTNRHNLESLYKHDSNLIEADSIKNSPDIVTSHMLKYSVKDKNLSVFFEKDWISQEFKDKEVDIYALSAQEVCECPGKRYEAFGGITLTNSEKKEIKVPVNVWDKSKQQPPMFITVNKPKVTAQEVDIKVRKLLIKKYDIYNNREQKYSKGTVTLDLNSGKDIVFDLYYFGNGDFNSMLKIYSNNERIDSTQFHVDVSIS
Exotoxin type H (SPE H)
Streptococcus pyogenes serotype M1
301,447
236
27,485
Reference proteome;Secreted;Signal;Toxin;Virulence
GO:0005576; GO:0090729
Inferred from homology
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..32; /evidence="ECO:0000255"
null
PF02876;PF01123;
IPR008992;IPR006126;IPR006173;IPR016091;IPR013307;IPR006123;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species)
speH SPy_1008
true
Streptococcus pyogenes
4
row_5843
false
null
4,763
Q8NKX2
MKKINIIKIVFIITVILISTISPIIKSDSKKDISNVKSDLLYAYTITPYDYKDCRVNFSTTHTLNIDTQKYRGKDYYISSEMSYEASQKFKRDDHVDVFGLFYILNSHTGEYIYGGITPAQNNKVNHKLLGNLFISGESQQNLNNKIILEKDIVTFQEIDFKIRKYLMDNYKIYDATSPYVSGRIEIGTKDGKHEQIDLFDSPNEGTRSDIFAKYKDNRIINMKNFSHFDIYLEK
Exotoxin type C (SPE C)
Streptococcus pyogenes serotype M18 (strain MGAS8232)
186,103
235
27,372
3D-structure;Direct protein sequencing;Signal;Toxin;Virulence;Zinc
GO:0005576; GO:0090729
Evidence at protein level
3
null
SIGNAL 1..27; /evidence="ECO:0000269|PubMed:3045005"
null
PF02876;PF01123;
IPR008992;IPR006126;IPR006173;IPR016091;IPR013307;IPR006123;IPR006177;
1AN8;1HQR;1KTK;
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species), Streptococcus pyogenes serotype M18 (serotype)
speC spyM18_0778
true
Streptococcus pyogenes
5
row_4539
false
null
6,312
P0DG08
MKTNILTIIILSCVFSYGSQLAYADENLKDLKRSLRFAYNITPCDYENVEIAFVTTNSIHINTKQKRSECILYVDSIVSLGITDQFIKGDKVDVFGLPYNFSPPYVDNIYGGIVKHSNQGNKSLQFVGILNQDGKETYLPSEVVRIKKKQFTLQEFDLKIRKFLMEKYNIYDSESRYTSGSLFLATKDSKHYEVDLFNKDDKLLSRDSFFKRYKDNKIFNSEEISHFDIYLKTY
Exotoxin type G (Pyrogenic exotoxin G) (SPE G)
Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315)
198,466
234
27,282
Signal;Toxin;Virulence
GO:0005576; GO:0090729
Inferred from homology
2
null
SIGNAL 1..24; /evidence="ECO:0000255"
null
PF02876;PF01123;
IPR008992;IPR006126;IPR006173;IPR016091;IPR013307;IPR006123;IPR006177;
null
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Streptococcaceae (family), Streptococcus (genus), Streptococcus pyogenes (species), Streptococcus pyogenes serotype M3 (serotype)
speG SpyM3_0155
true
Streptococcus pyogenes
6
row_6064
false
null
256
P0C2E9
MIRFKKTKLIASIAMALCLFSQPVISFSKDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKTGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTAVVLGGDAQEHNKVVTKDFDEIRKVIKDNATFSTKNPAYPISYTSVFLKDNSVAAVHNKTDYIETTSTEYSKGKINLDHSGAYVAQFEVAWDEVSYDKEGNEVLTHKTWDGNYQDKTAHYSTVIPLEANARNIRIKARECTGLAWEWWRDVISEYDVPLTNNINVSIWGTTLYPGSSITYN
Perfringolysin O (PFO) (Theta-toxin) (Thiol-activated cytolysin)
Clostridium perfringens (strain 13 / Type A)
195,102
500
55,830
3D-structure;Cytolysis;Direct protein sequencing;Hemolysis;Host cell membrane;Host membrane;Lipid-binding;Membrane;Reference proteome;Secreted;Signal;Toxin;Transmembrane;Transmembrane beta strand;Virulence
GO:0001897; GO:0005576; GO:0015485; GO:0016020; GO:0020002; GO:0044179; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2878682}. Host cell membrane; Multi-pass membrane protein {ECO:0000305|PubMed:15851031}. Note=Secreted as soluble protein that then inserts into the host cell membrane and forms huge pores formed by transmembrane beta-strands. {ECO:0000305|PubMed:15851031}.
SIGNAL 1..28; /evidence="ECO:0000269|PubMed:2878682"
TRANSMEM 189..202; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 209..218; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 287..296; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"; TRANSMEM 304..316; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:Q04IN8"
PF17440;PF01289;
IPR035390;IPR038700;IPR001869;IPR036363;IPR036359;
1M3I;1M3J;1PFO;2BK1;2BK2;5DHL;5DIM;
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Clostridia (class), Eubacteriales (order), Clostridiaceae (family), Clostridium (genus), Clostridium perfringens (species)
pfo pfoA pfoR CPE0163
true
Clostridium perfringens
0
row_240
false
null
250
P0C216
MKRKICKALICATLATSLWAGASTKVYAWDGKIDGTGTHAMIVTQGVSILENDLSKNEPESVRKNLEILKENMHELQLGSTYPDYDKNAYDLYQDHFWDPDTDNNFSKDNSWYLAYSIPDTGESQIRKFSALARYEWQRGNYKQATFYLGEAMHYFGDIDTPYHPANVTAVDSAGHVKFETFAEERKEQYKINTAGCKTNEDFYADILKNKDFNAWSKEYARGFAKTGKSIYYSHASMSHSWDDWDYAAKVTLANSQKGTAGYIYRFLHDVSEGNDPSVGKNVKELVAYISTSGEKDAGTDDYMYFGIKTKDGKTQEWEMDNPGNDFMTGSKDTYTFKLKDENLKIDDIQNMWIRKRKYTAFPDAYKPENIKIIANGKVVVDKDINEWISGNSTYNIK
Phospholipase C (PLC) (EC 3.1.4.3) (Alpha-toxin) (Hemolysin) (Lecithinase) (Phosphatidylcholine cholinephosphohydrolase)
Clostridium perfringens (strain 13 / Type A)
195,102
398
45,530
3D-structure;Calcium;Cytolysis;Hemolysis;Hydrolase;Metal-binding;Reference proteome;Secreted;Signal;Toxin;Virulence;Zinc
GO:0005576; GO:0008270; GO:0031640; GO:0034480; GO:0050429; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
SIGNAL 1..28; /evidence="ECO:0000250"
null
PF01477;PF00882;
IPR001024;IPR036392;IPR008947;IPR029002;IPR001531;
1CA1;1GYG;1QM6;1QMD;
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Clostridia (class), Eubacteriales (order), Clostridiaceae (family), Clostridium (genus), Clostridium perfringens (species)
plc cpa CPE0036
true
Clostridium perfringens
1
row_234
false
null
253
P0C250
MGKLTILVLVAAVLLSTQVMVQGDGDQPADRNAVRRDDNPGGTRGRFMNILRRTGCPWDPWCG
Contryphan-Lo (Contryphan-Lo1) (Lo959) [Cleaved into: Contryphan-Lo Lo902]
Conus buxeus loroisii (Cone snail) (Conus loroisii)
410,709
63
6,897
3D-structure;Amidation;Calcium channel impairing toxin;D-amino acid;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Secreted;Signal;Toxin;Voltage-gated calcium channel impairing toxin
GO:0005246; GO:0005576; GO:0008200; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16387709, ECO:0000269|PubMed:16945451}.
SIGNAL 1..23; /evidence="ECO:0000255"
null
PF02950;
IPR004214;IPR011062;
2M6G;2M6H;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Spiralia (clade), Lophotrochozoa (clade), Mollusca (phylum), Gastropoda (class), Caenogastropoda (subclass), Neogastropoda (order), Conoidea (superfamily), Conidae (family), Conus (genus), Dendroconus (subgenus), Conus buxeus (species)
null
true
Conus buxeus
0
row_237
false
null
832
A0A1P8NVU0
MGKLTILVLVAAVLLSTQAMVQDQPADRNAVRRNDNPGGASRKSINVLHRNECPWQPWCG
Contryphan-Lo2 (Lo1158)
Conus buxeus loroisii (Cone snail) (Conus loroisii)
410,709
60
6,598
Amidation;D-amino acid;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Secreted;Signal;Toxin
GO:0005576; GO:0008200; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28152596}.
SIGNAL 1..19; /evidence="ECO:0000255"
null
PF02950;
IPR004214;IPR011062;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Spiralia (clade), Lophotrochozoa (clade), Mollusca (phylum), Gastropoda (class), Caenogastropoda (subclass), Neogastropoda (order), Conoidea (superfamily), Conidae (family), Conus (genus), Dendroconus (subgenus), Conus buxeus (species)
null
true
Conus buxeus
1
row_781
false
null
1,700
P31854
MRTLWIVAVWLMGVEGNLFQFGNMINHMVGKHAVWSYLSYGCYCGWGGQGKPQDATDRCCFVHDCCYGRANGCDPKLSTYSYNFQNGNIVCGNKYGCLRHICECDRVAAICFQKNMNTYNKKYKNYSSSNCQENSDKC
Basic phospholipase A2 Pla2Vb (VbbPLA2) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Vipera berus berus (Common viper)
31,156
138
15,716
Blood coagulation cascade inhibiting toxin;Calcium;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal;Toxin
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0047498; GO:0050482; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8499481}.
SIGNAL 1..16; /evidence="ECO:0000269|PubMed:8499481"
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera berus (species)
null
true
Vipera berus
0
row_1629
false
null
255
P0C2D7
ADDKNPLEECFREDDYEEFLEIAKNGLKKTSNPKHIVYPVKPSEQLYEESLRDQLPTSMHRYPSMIQKIFFAGEYTANAHGWIDSTIK
L-amino-acid oxidase (LAAO) (LAO) (EC 1.4.3.2)
Vipera berus berus (Common viper)
31,156
88
10,295
Antibiotic;Antimicrobial;Apoptosis;Cytolysis;Direct protein sequencing;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Hemolysis;Hemostasis impairing toxin;Oxidoreductase;Platelet aggregation inhibiting toxin;Secreted;Toxin
GO:0005576; GO:0006915; GO:0031640; GO:0042742; GO:0050025; GO:0090729; GO:0106329
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16574513}.
null
null
null
null
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera berus (species)
null
true
Vipera berus
1
row_239
false
null
3,270
P0C6A6
NSGNPCCDPVTCKPRRGEHCVSGPCCRNCKFLNAGTICKYARGDDMNDYCTGISSDCPRNPYKD
Disintegrin VB7A
Vipera berus berus (Common viper)
31,156
64
7,009
Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Platelet aggregation inhibiting toxin;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12667142}.
null
null
PF00200;
IPR018358;IPR001762;IPR036436;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera berus (species)
null
true
Vipera berus
2
row_3153
false
null
3,271
P0C6A7
ELLQNSGNPCCDPVTCKPREGEHCISGPCCRNCKFKRAGTVCLDAKGDWMNNYCTGISSDCPRN
Disintegrin VB7B
Vipera berus berus (Common viper)
31,156
64
6,998
Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Platelet aggregation inhibiting toxin;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12667142}.
null
null
PF00200;
IPR001762;IPR036436;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera berus (species)
null
true
Vipera berus
3
row_3154
false
null
313
P0DJN7
MRTFWIVAVLLVGVEGNLLQFNKMIKIMTKKNAIPFYTSYGCYCGWGGRGRPKDATDRCCFVHDCCYEKLTDCSPKTARYSYSWKSGVIICGEGTPCEKQICECDRAAAVCFGANLSTYKKRYMFYPDLLCTDPSEKC
Basic phospholipase A2 Cll-N6 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Crotalus lepidus lepidus (Mottled rock rattlesnake)
992,932
138
15,648
Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Myotoxin;Secreted;Signal;Toxin
GO:0004623; GO:0005576; GO:0016042; GO:0046872; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15032748}.
SIGNAL 1..16; /evidence="ECO:0000269|PubMed:15032748"
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus lepidus (species)
null
true
Crotalus lepidus
0
row_295
false
null
1,189
C0LZJ5
IVSPPVCGNELLENGEECDCGSPANCRNPCCDAASCRLHSWVECESGECCDQCRFVTAGTECRATRSECDLAGQCTGQSADCPIDRFHRNGQPCLQNYGYCYNGKCPIMHHQCYYLFGANATVAQDACFEENKNGIGDFYCRKQSDRLIPCAPEDVKCGRLFCEILPNTRCKHAPGDNGMVDPGTKCEDKKVCFNRKCVDVNTVY
Disintegrin-like leberagin-C
Macrovipera lebetina transmediterranea (Blunt-nosed viper) (Vipera lebetina transmediterranea)
384,075
205
22,634
Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Platelet aggregation inhibiting toxin;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted.
null
null
PF08516;PF00200;
IPR006586;IPR018358;IPR001762;IPR036436;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Macrovipera (genus), Macrovipera lebetinus (species)
null
true
Macrovipera lebetinus
0
row_1134
false
null
964
B5U6Z2
MRTLWIVAVCLMGVEGHLTQFGDMINKKTGTFGLLSYVYYGCYCGLGGKGKPQDATDRCCFVHDCCYGTVNGCDPKLSTYSYSFQNGDIVCGDDDPCLRAVCECDRVAAICFGENMNTYDKKYMLYSLFDCMEESEKC
Acidic phospholipase A2 MVL-PLA2 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Macrovipera lebetina transmediterranea (Blunt-nosed viper) (Vipera lebetina transmediterranea)
384,075
138
15,399
Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal;Toxin
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0047498; GO:0050482; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..16; /evidence="ECO:0000269|PubMed:19351557"
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Macrovipera (genus), Macrovipera lebetinus (species)
null
true
Macrovipera lebetinus
1
row_909
false
null
3,274
P0C6B0
MNSANPCCDPITCKPRRGEHCVSGPCCRNCKFLNPGTICKRTMLDGLNDYCTGVTSDCPRNPWKSEEED
Disintegrin VLO5B
Macrovipera lebetina obtusa (Levant blunt-nosed viper) (Vipera lebetina obtusa)
209,528
69
7,670
Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Platelet aggregation inhibiting toxin;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12667142}.
null
null
PF00200;
IPR018358;IPR001762;IPR036436;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Macrovipera (genus), Macrovipera lebetinus (species)
null
true
Macrovipera lebetinus
2
row_3157
false
null
3,272
P0C6A8
MNSGNPCCDPVTCKPRRGEHCVSGPCCRNCKFLNAGTICKRARGDDMNDYCTGISPDCPRNPWKG
Disintegrin VLO4
Macrovipera lebetina obtusa (Levant blunt-nosed viper) (Vipera lebetina obtusa)
209,528
65
7,108
Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Platelet aggregation inhibiting toxin;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12667142}.
null
null
PF00200;
IPR018358;IPR001762;IPR036436;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Macrovipera (genus), Macrovipera lebetinus (species)
null
true
Macrovipera lebetinus
3
row_3155
false
null
3,273
P0C6A9
NSGNPCCDPVTCQPRRGEHCVSGKCCRNCKFLRAGTVCKRAVGDDMDDYCTGISSDCPRNPYKD
Disintegrin VLO5A
Macrovipera lebetina obtusa (Levant blunt-nosed viper) (Vipera lebetina obtusa)
209,528
64
7,005
Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Platelet aggregation inhibiting toxin;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12667142}.
null
null
PF00200;
IPR018358;IPR001762;IPR036436;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Macrovipera (genus), Macrovipera lebetinus (species)
null
true
Macrovipera lebetinus
4
row_3156
false
null
1,869
P83469
CTTGPCCRQCKLKPAGTTCWKTSLTSHYCTGKSCDCPLYPG
Disintegrin obtustatin
Macrovipera lebetina obtusa (Levant blunt-nosed viper) (Vipera lebetina obtusa)
209,528
41
4,401
3D-structure;Angiogenesis;Cell adhesion impairing toxin;Developmental protein;Differentiation;Direct protein sequencing;Disulfide bond;Secreted;Toxin
GO:0001525; GO:0005576; GO:0030154; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12538900}.
null
null
null
IPR001762;IPR036436;
1MPZ;
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Macrovipera (genus), Macrovipera lebetinus (species)
null
true
Macrovipera lebetinus
5
row_1794
false
null
342
P0DRC8
QFSDCSKDEYQRYLT
Snake venom metalloproteinase Mlp4.2 (SVMP) (EC 3.4.24.-)
Macrovipera lebetina transmediterranea (Blunt-nosed viper) (Vipera lebetina transmediterranea)
384,075
15
1,883
Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Magnesium;Metal-binding;Metalloprotease;Myotoxin;Protease;Secreted;Toxin;Zinc
GO:0004222; GO:0005576; GO:0006508; GO:0044523; GO:0046872; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20398688}.
null
null
null
null
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Macrovipera (genus), Macrovipera lebetinus (species)
null
true
Macrovipera lebetinus
6
row_319
false
null
3,937
P25674
IRCFITPDVTSQACPDGHVCYTKMWCDNFCGMRGKRVDLGCAATCPTVKPGVDIKCCSTDNCNPFPTRKRS
Long neurotoxin 1 (Toxin CM-5)
Naja haje haje (Egyptian cobra)
8,642
71
7,821
Acetylcholine receptor inhibiting toxin;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Toxin
GO:0005576; GO:0030550; GO:0090729; GO:0099106
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:718974}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja haje (species)
null
true
Naja haje
0
row_3782
false
null
6,039
P01401
LTCLICPEKYCNKVHTCRNGENQCFKRFNERKLLGKRYTRGCAATCPEAKPREIVECCTTDRCNK
Weak toxin CM-11
Naja haje haje (Egyptian cobra)
8,642
65
7,546
Direct protein sequencing;Disulfide bond;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:710433}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja haje (species)
null
true
Naja haje
1
row_5798
false
null
4,146
P62394
LKCHNTQLPFIYKTCPEGKNLCFKTTLKKLPLKIPIKRGCAATCPKSSALLKVVCCSTDKCN
Cytotoxin 11 (Toxin CM-12)
Naja haje haje (Egyptian cobra)
8,642
62
6,842
Direct protein sequencing;Disulfide bond;Membrane;Secreted;Target cell membrane;Target membrane;Toxin
GO:0005576; GO:0016020; GO:0044218; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:710433}. Target cell membrane {ECO:0000250|UniProtKB:P62375}.
null
null
PF21947;
IPR003572;IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja haje (species)
null
true
Naja haje
2
row_3981
false
null
3,938
P25675
MICHNQQSSQPPTIKTCPGETNCYKKQWRDHRGTIIERGCGCPSVKKGVGIYCCKTDKCNR
Short neurotoxin 2 (Toxin CM-10a)
Naja haje haje (Egyptian cobra)
8,642
61
6,888
Acetylcholine receptor inhibiting toxin;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Toxin
GO:0005576; GO:0030550; GO:0090729; GO:0099106
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:718974}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja haje (species)
null
true
Naja haje
3
row_3783
false
null
4,161
P68418
LECHNQQSSQPPTTKTCPGETNCYKKRWRDHRGSITERGCGCPSVKKGIEINCCTTDKCNN
Short neurotoxin 1 (Toxin CM-6)
Naja haje haje (Egyptian cobra)
8,642
61
6,844
Acetylcholine receptor inhibiting toxin;Direct protein sequencing;Disulfide bond;Ion channel impairing toxin;Neurotoxin;Postsynaptic neurotoxin;Secreted;Toxin
GO:0005576; GO:0030550; GO:0090729; GO:0099106
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:718974}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja haje (species)
null
true
Naja haje
4
row_3996
false
null
6,048
P01415
FTCFTTPSDTSETCPDGQNICYEKRWNSHQGVEIKGCVASCPEFESRFRYLLCCRIDNCNK
Weak toxin CM-2
Naja haje haje (Egyptian cobra)
8,642
61
7,033
Direct protein sequencing;Disulfide bond;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:710433}.
null
null
PF21947;
IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja haje (species)
null
true
Naja haje
5
row_5807
false
null
3,076
P01457
LKCHQLVPPFWKTCPEGKNLCYKMYMVSSSTVPVKRGCIDVCPKNSALVKYVCCNTDKCN
Cytotoxin 5 (Toxin CM-8)
Naja haje haje (Egyptian cobra)
8,642
60
6,773
Cardiotoxin;Cytolysis;Direct protein sequencing;Disulfide bond;Membrane;Secreted;Target cell membrane;Target membrane;Toxin
GO:0005576; GO:0016020; GO:0031640; GO:0044218; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:667107}. Target cell membrane {ECO:0000250|UniProtKB:P60301}.
null
null
PF21947;
IPR003572;IPR003571;IPR045860;IPR018354;IPR054131;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja haje (species)
null
true
Naja haje
6
row_2974
false
null
346
P0DUG4
NVYQYRKMLQCAMPNGGPFECCQTHDNCYGEAEKLKACTSTHSSPYFK
Phospholipase A2 TI-Nh (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Thrombin inhibitor from Naja haje)
Naja haje haje (Egyptian cobra)
8,642
48
5,481
Blood coagulation cascade inhibiting toxin;Calcium;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Metal-binding;Platelet aggregation inhibiting toxin;Secreted;Toxin
GO:0004623; GO:0005576; GO:0006644; GO:0046872; GO:0050482; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19622365}.
null
null
null
IPR036444;IPR033113;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja haje (species)
null
true
Naja haje
7
row_321
false
null
4,336
P84807
DVDFNSESTRRKNKQKEIVDLHNSLKKTV
Cysteine-rich venom protein 25-A (CRVP-25h-A)
Naja haje haje (Egyptian cobra)
8,642
29
3,430
Direct protein sequencing;Disulfide bond;Secreted;Toxin
GO:0005576; GO:0006952; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15670767}.
null
null
null
null
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja haje (species)
null
true
Naja haje
8
row_4168
false
null
4,335
P84804
DSSNLPPNQKQIVD
Cysteine-rich venom protein 23 (CRVP-23h)
Naja haje haje (Egyptian cobra)
8,642
14
1,555
Direct protein sequencing;Disulfide bond;Secreted;Toxin
GO:0005576; GO:0006952; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15670767}.
null
null
null
null
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja haje (species)
null
true
Naja haje
9
row_4167
false
null
352
P0DUN5
HLLQFNKNAIPFYAFYGCYCGWGGRCCFVHDCCYGKWDIYPYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC
Basic phospholipase A2 Bbil-TX (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Bothrops bilineatus smaragdinus (Two-striped forest-pitviper)
2,815,652
98
11,409
Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Myotoxin;Neurotoxin;Presynaptic neurotoxin;Secreted;Toxin
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0042130; GO:0047498; GO:0050482; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23509754}.
null
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Bothrops (genus), Bothrops bilineatus (species)
null
true
Bothrops bilineatus
0
row_326
false
null
1,358
P06200
MTENWKFRRRTFLKHGAQAATLAGLSGLFPETLRRALAVEPDIRTGTIQDVQHVVILMQENRSFDHYFGHLNGVRGFNDPRALKRQDGKPVWYQNYKYEFSPYHWDTKVTSAQWVSSQNHEWSAFHAIWNQGRNDKWMAVQYPEAMGYFKRGDIPYYYALADAFTLCEAYHQSMMGPTNPNRLYHMSGRAAPSGDGKDVHIGNDMGDGTIGASGTVDWTTYPERLSAAGVDWRVYQEGGYRSSSLWYLYVDAYWKYRLQEQNNYDCNALAWFRNFKNAPRDSDLWQRAMLARGVDQLRKDVQENTLPQVSWIVAPYCYCEHPWWGPSFGEYYVTRVLEALTSNPEVWARTVFILNYDEGDGFYDHASAPVPPWKDGVGLSTVSTAGEIEVSSGLPIGLGHRVPLIAISPWSKGGKVSAEVFDHTSVLRFLERRFGVVEENISPWRRAVCGDLTSLFDFQGAGDTQVAPDLTNVPQSDARKEDAYWQQFYRPSPKYWSYEPKSLPGQEKGQRPTLAVPYQLHATLALDIAAGKLRLTLGNDGMSLPGNPQGHSAAVFQVQPREVGNPRFYTVTSYPVVQESGEELGRTLNDELDDLLDANGRYAFEVHGPNGFFREFHGNLHLAAQMARPEVSVTYQRNGNLQLNIRNLGRLPCSVTVTPNPAYTREGSRRYELEPNQAISEVWLLRSSQGWYDLSVTASNTEANYLRRLAGHVETGKPSRSDPLLDIAAT
Hemolytic phospholipase C (EC 3.1.4.3) (Heat-labile hemolysin) (PLC-H) (Phosphatidylcholine cholinephosphohydrolase)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
208,964
730
82,667
Cytolysis;Hemolysis;Hydrolase;Reference proteome;Signal;Toxin;Virulence
GO:0005615; GO:0015628; GO:0016042; GO:0016298; GO:0033188; GO:0034480; GO:0044179; GO:0090729
Inferred from homology
4
null
SIGNAL 1..38; /note="Tat-type signal"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
null
PF04185;PF05506;
IPR017850;IPR017767;IPR007312;IPR008475;IPR006311;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas aeruginosa group (no rank), Pseudomonas aeruginosa (species)
plcH PA0844
true
Pseudomonas aeruginosa
0
row_1299
false
null
361
P11439
MHLTPHWIPLVASLGLLAGGSFASAAEEAFDLWNECAKACVLDLKDGVRSSRMSVDPAIADTNGQGVLHYSMVLEGGNDALKLAIDNALSITSDGLTIRLEGGVEPNKPVRYSYTRQARGSWSLNWLVPIGHEKPSNIKVFIHELNAGNQLSHMSPIYTIEMGDELLAKLARDATFFVRAHESNEMQPTLAISHAGVSVVMAQAQPRREKRWSEWASGKVLCLLDPLDGVYNYLAQQRCNLDDTWEGKIYRVLAGNPAKHDLDIKPTVISHRLHFPEGGSLAALTAHQACHLPLETFTRHRQPRGWEQLEQCGYPVQRLVALYLAARLSWNQVDQVIRNALASPGSGGDLGEAIREQPEQARLALTLAAAESERFVRQGTGNDEAGAASADVVSLTCPVAAGECAGPADSGDALLERNYPTGAEFLGDGGDISFSTRGTQNWTVERLLQAHRQLEERGYVFVGYHGTFLEAAQSIVFGGVRARSQDLDAIWRGFYIAGDPALAYGYAQDQEPDARGRIRNGALLRVYVPRSSLPGFYRTGLTLAAPEAAGEVERLIGHPLPLRLDAITGPEEEGGRLETILGWPLAERTVVIPSAIPTDPRNVGGDLDPSSIPDKEQAISALPDYASQPGKPPREDLK
Exotoxin A (ETA) (EC 2.4.2.36) (NAD(+)--diphthamide ADP-ribosyltransferase) (Pseudomonas exotoxin) (PE)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
208,964
638
69,284
3D-structure;Direct protein sequencing;Disulfide bond;Glycosyltransferase;NAD;Nucleotidyltransferase;Reference proteome;Signal;Toxin;Transferase;Virulence
GO:0001907; GO:0016779; GO:0047286; GO:0090729; GO:0141155
Evidence at protein level
5
null
SIGNAL 1..25; /evidence="ECO:0000269|PubMed:6201861"
null
PF09101;PF09009;PF09102;
IPR013320;IPR015185;IPR015099;IPR015186;IPR036478;
1AER;1DMA;1IKP;1IKQ;1XK9;1ZM2;1ZM3;1ZM4;1ZM9;2ZIT;3B78;3B82;3B8H;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Pseudomonadales (order), Pseudomonadaceae (family), Pseudomonas (genus), Pseudomonas aeruginosa group (no rank), Pseudomonas aeruginosa (species)
eta PA1148
true
Pseudomonas aeruginosa
1
row_334
false
null