P83912 · VM2JT_PROJR

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).

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

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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.

TypeIDPosition(s)Description
Binding site197Ca2+ 1 (UniProtKB | ChEBI)
Binding site281Ca2+ 1 (UniProtKB | ChEBI)
Binding site330Zn2+ (UniProtKB | ChEBI); catalytic
Active site331
Binding site334Zn2+ (UniProtKB | ChEBI); catalytic
Binding site340Zn2+ (UniProtKB | ChEBI); catalytic
Binding site387Ca2+ 1 (UniProtKB | ChEBI)
Binding site390Ca2+ 1 (UniProtKB | ChEBI)
Binding site402Ca2+ 2 (UniProtKB | ChEBI)
Binding site405Ca2+ 2 (UniProtKB | ChEBI)
Binding site409Ca2+ 2 (UniProtKB | ChEBI)
Binding site412Ca2+ 2 (UniProtKB | ChEBI)
Binding site415Ca2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componentplasma membrane
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Molecular Functiontoxin activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Zinc metalloproteinase-disintegrin jerdonitin
  • EC number
  • Alternative names
    • Snake venom metalloproteinase (SVMP)

Organism names

Accessions

  • Primary accession
    P83912

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, modified residue, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-20
PropeptidePRO_000002897721-191
Modified residue192Pyrrolidone carboxylic acid
ChainPRO_0000028978192-484Zinc metalloproteinase-disintegrin jerdonitin
Disulfide bond305↔387
Disulfide bond345↔369
Disulfide bond347↔352
Disulfide bond403↔422
Disulfide bond414↔432
Disulfide bond416↔427
Disulfide bond426↔449
Disulfide bond440↔446
Disulfide bond445↔470
Disulfide bond458↔477

Post-translational modification

The N-terminus is blocked.

Keywords

Expression

Tissue specificity

Expressed by the venom gland.

Interaction

Subunit

Monomer.

Structure

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain194-392Peptidase M12B
Domain400-484Disintegrin
Motif462-464Cell attachment site

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    484
  • Mass (Da)
    54,613
  • Last updated
    2004-05-24 v1
  • Checksum
    8D603EE7C0F48232
MIQVLLVTICLAVFPYQGSSIILESGNIDDYEVVYPRKVTALPKGAVQQKYEDTMQYEFKVNEEPVVLHLEKNKGLFSKDYSETHYSPDGREITTYPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGETYFIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTETNWESDEPIKKLSQIMIPPEQQRYIELVIVADHRMYTKYDGDKTEISSKIYETANNLNEIYRHLKIHVVLIGLEMWSSGELSKVTLSADETLDSFGEWRERDLLQRKRHDNAQLLTGMIFNEKIEGRAYKESMCDPKRSVGIVRDHRTRPHLVANRMAHELGHNLGFHHDGDSCTCGANSCIMSATVSNEPSSRFSDCSLFQYSSDIIHNPFTSRCLYNEPSKTDIVSPSVCGNYYMEVGEDCDCGPPANCQNPCCDAATCRLTPGSQCADGLCCDQCRFMKKGTICRIARGDDLDDYCNGISAGCPRNPFHA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY364231
EMBL· GenBank· DDBJ
AAQ63966.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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