VMP3A_DEIAC
ID VMP3A_DEIAC Reviewed; 10 AA.
AC P0DJH3;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like AAV1;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Contains:
DE RecName: Full=Disintegrin-like AAV1-C;
DE Flags: Fragment;
OS Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Deinagkistrodon.
OX NCBI_TaxID=36307;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=17029743; DOI=10.1016/j.biochi.2006.08.009;
RA Wang W.J.;
RT "Purification and functional characterization of AAV1, a novel P-III
RT metalloproteinase, from Formosan Agkistrodon acutus venom.";
RL Biochimie 89:105-115(2007).
CC -!- FUNCTION: Zinc metalloprotease-disintegrin AAV1: snake venom zinc
CC metalloprotease that binds to the platelet collagen receptor
CC glycoprotein VI (GP6) thus inhibiting collagen- and convulxin- (a GP6
CC agonist) induced platelet aggregation and the tyrosine phosphorylation
CC of intracellular signaling proteins (LAT, SYK, p76SLP76, PIK3C, and
CC PLCG2) that follows GP6 activation. Interestingly, blocks platelet
CC aggregation but does not affect shape change. Also degrades the Aalpha
CC chain of fibrinogen (FGA), followed by the Bbeta chain (FGB).
CC {ECO:0000269|PubMed:17029743}.
CC -!- FUNCTION: Disintegrin AAV1-C: 30 kDa fragment of AAV1 autoproteolysed
CC in absence of Ca(2+) that shows more potent inhibition of convulxin-
CC induced platelet aggregation than AAV1. {ECO:0000269|PubMed:17029743}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: The proteinase activity is slightly enhanced by
CC Ca(2+) and Mg(2+). Inhibited by EDTA and phenanthroline, but not by
CC PMSF. {ECO:0000269|PubMed:17029743}.
CC -!- SUBUNIT: Monomeric (57 kDa), and polymeric (180 kDa) forms have been
CC detected under non-reducing conditions on SDS-PAGE, whereas only one
CC monomeric form is observed under reducing conditions.
CC {ECO:0000269|PubMed:17029743}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: N-glycosylated.
CC -!- MISCELLANEOUS: Does not cleave glycoprotein VI (GP6), gelatin (an
CC irreversibly hydrolyzed form of collagen), fibronectin, prothrombin,
CC and gamma chain of fibrinogen. May not bind to alpha-2/beta-1 integrin
CC (ITGA2/ITGB1) (PubMed:17029743). {ECO:0000305|PubMed:17029743}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Platelet aggregation inhibiting toxin;
KW Protease; Secreted; Toxin; Zinc; Zymogen.
FT CHAIN <1..>10
FT /note="Zinc metalloproteinase-disintegrin-like AAV1"
FT /id="PRO_0000417323"
FT CHAIN 1..>10
FT /note="Disintegrin-like AAV1-C"
FT /id="PRO_0000417324"
FT DOMAIN 5..>10
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT BINDING 7
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT DISULFID 8..?
FT NON_TER 1
FT NON_TER 10
SQ SEQUENCE 10 AA; 986 MW; C8922AA2D77775A2 CRC64;
DVVSPPVCGN
