A0A6B7FMR5 · VMMP3_VIPAA
- ProteinDisintegrin-like/cysteine-rich protein MPIII-3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids324 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | plasma membrane | |
Molecular Function | metal ion binding | |
Molecular Function | toxin activity |
Keywords
- Molecular function
- Ligand
Community annotation
Inhibits platelet aggregation induced by ADP, arachidonic acid and/or collagen.
Source | Submission date | Contributor |
---|---|---|
PubMed:35448841 | 0000-0003-1233-9864 |
Names & Taxonomy
Protein names
- Recommended nameDisintegrin-like/cysteine-rich protein MPIII-3
- Short namesD'C protein MPIII-3
- Alternative names
Community suggested name: VaaMPIII-3; MPIII-3; Metalloproteinase-like protein of class P-III; Snake venom metalloproteinase of subclass P-IIIe MPIII-3.
Source | Submission date | Contributor |
---|---|---|
PubMed:35448841 | 0000-0003-1233-9864 |
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Viperinae > Vipera
Accessions
- Primary accessionA0A6B7FMR5
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MIQVLLVIICLAVFPYQVSS | ||||||
Propeptide | PRO_0000457327 | 21-173 | Or 174 (in a minor form) | |||
Sequence: IILESGNINNYEVVYPQKVTALPKGAIQQLEQKYEDAMQYQFKVKGEPVVLHLEKNKDFFPEDYSETHYSPDDREITTNPPVEDHCYYYGHIQNDADSTASISACNGLKGYFTLRGVTYLIEPLKIPESEAHAIYKYENVEKEDEDPKKCEFR | ||||||
Chain | PRO_5025634875 | 174-324 | Disintegrin-like/cysteine-rich protein MPIII-3 | |||
Sequence: RAGTECRPARSECDVAEYCTGQSAECPTDVFHSNGKPCLNNFGYCYNGNCPIMYHQCYALFGPNATVGQDGCFEWNKKGESYFYCRKENDVPIPCAPEDIKCGRLFCELIKNTCKYDYSEDPDYGMVDHGTKCGDGKVCINRHCVDVTTAY | ||||||
Disulfide bond | 179↔199 | Alternate | ||||
Sequence: CRPARSECDVAEYCTGQSAEC | ||||||
Disulfide bond | 186↔218 | |||||
Sequence: CDVAEYCTGQSAECPTDVFHSNGKPCLNNFGYC | ||||||
Disulfide bond | 192↔199 | Alternate | ||||
Sequence: CTGQSAEC | ||||||
Disulfide bond | 211↔223 | |||||
Sequence: CLNNFGYCYNGNC | ||||||
Disulfide bond | 230↔280 | |||||
Sequence: CYALFGPNATVGQDGCFEWNKKGESYFYCRKENDVPIPCAPEDIKCGRLFC | ||||||
Glycosylation | 237 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 245↔287 | |||||
Sequence: CFEWNKKGESYFYCRKENDVPIPCAPEDIKCGRLFCELIKNTC | ||||||
Disulfide bond | 258↔268 | |||||
Sequence: CRKENDVPIPC | ||||||
Disulfide bond | 275↔312 | |||||
Sequence: CGRLFCELIKNTCKYDYSEDPDYGMVDHGTKCGDGKVC | ||||||
Disulfide bond | 306↔317 | |||||
Sequence: CGDGKVCINRHC |
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
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 168-207 | Disintegrin; truncated | ||||
Sequence: KKCEFRRAGTECRPARSECDVAEYCTGQSAECPTDVFHSN | ||||||
Region | 179-192 | Inhibits platelet aggregation | ||||
Sequence: CRPARSECDVAEYC | ||||||
Motif | 185-187 | D/ECD-tripeptide | ||||
Sequence: ECD |
Sequence similarities
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length324
- Mass (Da)36,837
- Last updated2020-06-17 v1
- Checksum4839FD590F5FC58E
Keywords
- Technical term