A0A6B7FMR5 · VMMP3_VIPAA

Function

function

Abolishes platelet aggregation induced by collagen, ADP (IC50=292 nM) and arachidonic-acid. The inhibition of collagen-induced platelet aggregation may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. The inhibition of ADP- or arachidonic-acid-induced platelet aggregation may be due to it acting as an antagonist of the ADP receptors or thromboxane-prostanoid receptors of the platelets, respectively. Does not interact with integrins alpha-IIb (ITGA2B) or beta-3 (ITGB3) nor platelet glycoproteins VI (GP6) or IX (GP9) in vitro, however, the detection is dependent on experimental conditions and may happen in vivo. Able to bind to platelet glycoprotein Ib alpha chain (GP1BA) receptor in vitro, although this interaction may have pathologically only limited effect in vivo as it is not able to abolish the von Willebrand factor (vWF)-dependent platelet agglutination induced by ristocetin. Does not affect blood coagulation.

Miscellaneous

Arises from a gene lacking the catalytic metalloproteinase (MP) domain and the N-terminal part of the disintegrin-like (D) domain. The latter results in truncated D domain (D').

Activity regulation

Activity may be regulated by the intramolecular thiol-disulfide exchange or disulfide bond switching.

Biotechnology

Potentially useful in the development of antithrombotic drugs, particularly due to the possible control of its activity via the redox potential.

pH Dependence

Structurally relatively unstable in pure water, but more stable in various buffers between pH 5-9. Most stable in 20 mM HEPES buffer at pH 7 with the addition of 2 mM Ca2+.

Temperature Dependence

Unfolds at 47 degrees Celsius in pure water, but structurally more stable in various buffers up to 60 degrees Celsius.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site187Ca2+ (UniProtKB | ChEBI)
Binding site190Ca2+ (UniProtKB | ChEBI)
Binding site202Ca2+ (UniProtKB | ChEBI)
Binding site203Ca2+ (UniProtKB | ChEBI)

GO annotations

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

Keywords

Community curation (1)

Community annotation

Inhibits platelet aggregation induced by ADP, arachidonic acid and/or collagen.

SourceSubmission dateContributor
PubMed:354488410000-0003-1233-9864

Names & Taxonomy

Protein names

  • Recommended name
    Disintegrin-like/cysteine-rich protein MPIII-3
  • Short names
    D'C protein MPIII-3
  • Alternative names
    • Metalloproteinase-like protein of class P-III MPIII-3
    • Snake venom metalloproteinase precursor-derived protein MPIII-3
      (SVMP precursor-derived protein MPIII-3
      )
    • Snake venom metalloproteinase-like
      (SVMP-like
      )
    • Vaa-MPIII-3
    • VaaMPIII-3
Community curation (1)

Community suggested name: VaaMPIII-3; MPIII-3; Metalloproteinase-like protein of class P-III; Snake venom metalloproteinase of subclass P-IIIe MPIII-3.

SourceSubmission dateContributor
PubMed:354488410000-0003-1233-9864

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Viperinae > Vipera

Accessions

  • Primary accession
    A0A6B7FMR5

Subcellular Location

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for signal, propeptide, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-20
PropeptidePRO_000045732721-173Or 174 (in a minor form)
ChainPRO_5025634875174-324Disintegrin-like/cysteine-rich protein MPIII-3
Disulfide bond179↔199Alternate
Disulfide bond186↔218
Disulfide bond192↔199Alternate
Disulfide bond211↔223
Disulfide bond230↔280
Glycosylation237N-linked (GlcNAc...) asparagine
Disulfide bond245↔287
Disulfide bond258↔268
Disulfide bond275↔312
Disulfide bond306↔317

Post-translational modification

N-glycosylated. Exists in at least six differently N-glycosylated forms. The glycans likely have a stabilizing purpose.
Cys-199 forms a disulfide bond with Cys-192 in 90% and with Cys-179 in 10% of the protein molecules; alternative disulfide bonds may have a major effect on the conformation of the protein.

Keywords

Expression

Tissue specificity

Expressed by the venom gland (at protein level) (PubMed:31017792, PubMed:35448841).
Expressed by the venom gland (PubMed:31017792).

Interaction

Subunit

Monomer (PubMed:31017792, PubMed:35448841).
Is able to form a homodimer (PubMed:35448841).

Family & Domains

Features

Showing features for domain, region, motif.

TypeIDPosition(s)Description
Domain168-207Disintegrin; truncated
Region179-192Inhibits platelet aggregation
Motif185-187D/ECD-tripeptide

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    324
  • Mass (Da)
    36,837
  • Last updated
    2020-06-17 v1
  • Checksum
    4839FD590F5FC58E
MIQVLLVIICLAVFPYQVSSIILESGNINNYEVVYPQKVTALPKGAIQQLEQKYEDAMQYQFKVKGEPVVLHLEKNKDFFPEDYSETHYSPDDREITTNPPVEDHCYYYGHIQNDADSTASISACNGLKGYFTLRGVTYLIEPLKIPESEAHAIYKYENVEKEDEDPKKCEFRRAGTECRPARSECDVAEYCTGQSAECPTDVFHSNGKPCLNNFGYCYNGNCPIMYHQCYALFGPNATVGQDGCFEWNKKGESYFYCRKENDVPIPCAPEDIKCGRLFCELIKNTCKYDYSEDPDYGMVDHGTKCGDGKVCINRHCVDVTTAY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MG958499
EMBL· GenBank· DDBJ
QBF53416.1
EMBL· GenBank· DDBJ
mRNA

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