P83912 · VM2JT_PROJR
- ProteinZinc metalloproteinase-disintegrin jerdonitin
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids484 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Snake venom zinc metalloproteinase that inhibits ADP-induced human platelet aggregation (IC50=120 nM (native) and IC50=248 nM (recombinant)). May act by binding to the receptor GPIIb/GPIIIa (ITGA2B/ITGB3) on the platelet surface (PubMed:14511668).
Degrades the alpha-chain of fibrinogen completely and the beta-chain partially, leaving the gamma chain intact (Ref.2). Also inhibits the growth of several cell lines, including human liver cancer cells (Bel7402), human leukemia cells (K562) and human gastric carcinoma cells (BGC823) (PubMed:19732785).
Degrades the alpha-chain of fibrinogen completely and the beta-chain partially, leaving the gamma chain intact (Ref.2). Also inhibits the growth of several cell lines, including human liver cancer cells (Bel7402), human leukemia cells (K562) and human gastric carcinoma cells (BGC823) (PubMed:19732785).
Miscellaneous
Negative results: does not show hemorrhagic activities after intradermal injection in mice. Does not show pro-coagulant and anti-coagulant activities (Ref.2).
The disintegrin domain belongs to the long disintegrin subfamily.
Cofactor
Note: Binds 1 zinc ion per subunit.
Activity regulation
Fibrinogenolytic activity is completely inhibited by EDTA, but not by PMSF.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 197 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 281 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 330 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 331 | |||||
Sequence: E | ||||||
Binding site | 334 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 340 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 387 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 390 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 402 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 405 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 409 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 412 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 415 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | toxin activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameZinc metalloproteinase-disintegrin jerdonitin
- EC number
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Protobothrops
Accessions
- Primary accessionP83912
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, modified residue, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MIQVLLVTICLAVFPYQGSS | ||||||
Propeptide | PRO_0000028977 | 21-191 | ||||
Sequence: IILESGNIDDYEVVYPRKVTALPKGAVQQKYEDTMQYEFKVNEEPVVLHLEKNKGLFSKDYSETHYSPDGREITTYPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGETYFIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTETNWESDEPIKKLSQIMIPPE | ||||||
Modified residue | 192 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000028978 | 192-484 | Zinc metalloproteinase-disintegrin jerdonitin | |||
Sequence: QQRYIELVIVADHRMYTKYDGDKTEISSKIYETANNLNEIYRHLKIHVVLIGLEMWSSGELSKVTLSADETLDSFGEWRERDLLQRKRHDNAQLLTGMIFNEKIEGRAYKESMCDPKRSVGIVRDHRTRPHLVANRMAHELGHNLGFHHDGDSCTCGANSCIMSATVSNEPSSRFSDCSLFQYSSDIIHNPFTSRCLYNEPSKTDIVSPSVCGNYYMEVGEDCDCGPPANCQNPCCDAATCRLTPGSQCADGLCCDQCRFMKKGTICRIARGDDLDDYCNGISAGCPRNPFHA | ||||||
Disulfide bond | 305↔387 | |||||
Sequence: CDPKRSVGIVRDHRTRPHLVANRMAHELGHNLGFHHDGDSCTCGANSCIMSATVSNEPSSRFSDCSLFQYSSDIIHNPFTSRC | ||||||
Disulfide bond | 345↔369 | |||||
Sequence: CTCGANSCIMSATVSNEPSSRFSDC | ||||||
Disulfide bond | 347↔352 | |||||
Sequence: CGANSC | ||||||
Disulfide bond | 403↔422 | |||||
Sequence: CGNYYMEVGEDCDCGPPANC | ||||||
Disulfide bond | 414↔432 | |||||
Sequence: CDCGPPANCQNPCCDAATC | ||||||
Disulfide bond | 416↔427 | |||||
Sequence: CGPPANCQNPCC | ||||||
Disulfide bond | 426↔449 | |||||
Sequence: CCDAATCRLTPGSQCADGLCCDQC | ||||||
Disulfide bond | 440↔446 | |||||
Sequence: CADGLCC | ||||||
Disulfide bond | 445↔470 | |||||
Sequence: CCDQCRFMKKGTICRIARGDDLDDYC | ||||||
Disulfide bond | 458↔477 | |||||
Sequence: CRIARGDDLDDYCNGISAGC |
Post-translational modification
The N-terminus is blocked.
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 194-392 | Peptidase M12B | ||||
Sequence: RYIELVIVADHRMYTKYDGDKTEISSKIYETANNLNEIYRHLKIHVVLIGLEMWSSGELSKVTLSADETLDSFGEWRERDLLQRKRHDNAQLLTGMIFNEKIEGRAYKESMCDPKRSVGIVRDHRTRPHLVANRMAHELGHNLGFHHDGDSCTCGANSCIMSATVSNEPSSRFSDCSLFQYSSDIIHNPFTSRCLYNEP | ||||||
Domain | 400-484 | Disintegrin | ||||
Sequence: PSVCGNYYMEVGEDCDCGPPANCQNPCCDAATCRLTPGSQCADGLCCDQCRFMKKGTICRIARGDDLDDYCNGISAGCPRNPFHA | ||||||
Motif | 462-464 | Cell attachment site | ||||
Sequence: RGD |
Sequence similarities
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length484
- Mass (Da)54,613
- Last updated2004-05-24 v1
- Checksum8D603EE7C0F48232
Keywords
- Technical term