ID   VM3AL_TRIAB             Reviewed;          53 AA.
AC   P0DJH2;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Zinc metalloproteinase-disintegrin-like alborhagin;
DE            EC=3.4.24.-;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Contains:
DE     RecName: Full=Disintegrin-like alborhagin-C;
DE   Flags: Fragments;
OS   Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops
OS   albolabris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX   NCBI_TaxID=8765;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=11344165; DOI=10.1074/jbc.m011352200;
RA   Andrews R.K., Gardiner E.E., Asazuma N., Berlanga O., Tulasne D.,
RA   Nieswandt B., Smith A.I., Berndt M.C., Watson S.P.;
RT   "A novel viper venom metalloproteinase, alborhagin, is an agonist at the
RT   platelet collagen receptor GPVI.";
RL   J. Biol. Chem. 276:28092-28097(2001).
RN   [2]
RP   FUNCTION.
RX   PubMed=18064326; DOI=10.1160/th07-06-0402;
RA   Wijeyewickrema L.C., Gardiner E.E., Moroi M., Berndt M.C., Andrews R.K.;
RT   "Snake venom metalloproteinases, crotarhagin and alborhagin, induce
RT   ectodomain shedding of the platelet collagen receptor, glycoprotein VI.";
RL   Thromb. Haemost. 98:1285-1290(2007).
CC   -!- FUNCTION: [Zinc metalloproteinase-disintegrin-like alborhagin]: Induces
CC       platelet activation and glycoprotein VI (GP6)-dependent platelet
CC       aggregation. Induces ectodomain cleavage of GP6 by activating
CC       endogenous platelet metalloproteinases (probably ADAM10). Has
CC       fibrinogenolytic activity against the alpha chain of fibrinogen (FGA).
CC       Recognizes distinct binding sites as convulxin, since alborhagin has
CC       minimal effect on convulxin binding to GPVI-expressing cells.
CC       {ECO:0000269|PubMed:18064326}.
CC   -!- FUNCTION: Disintegrin alborhagin-C: 42 kDa fragment of alborhagin
CC       autoproteolysed that does not show platelet activation.
CC       {ECO:0000269|PubMed:18064326}.
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: Alborhagin-induced platelet aggregation, but not
CC       shape change, is inhibited by EDTA, suggesting that the platelet
CC       activation (shape change) is independent of divalent cation or
CC       metalloproteinase activity.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- PTM: Contains numerous disulfide bonds. {ECO:0000250}.
CC   -!- PTM: Glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIIb sub-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; Fibrinogenolytic toxin; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Platelet aggregation activating toxin; Protease; Secreted; Toxin; Zinc.
FT   CHAIN           <1..>53
FT                   /note="Zinc metalloproteinase-disintegrin-like alborhagin"
FT                   /id="PRO_0000417321"
FT   CHAIN           37..>53
FT                   /note="Disintegrin-like alborhagin-C"
FT                   /id="PRO_0000417322"
FT   UNSURE          1
FT                   /note="Assigned by comparison with orthologs"
FT   UNSURE          12
FT                   /note="R or K"
FT   UNSURE          21
FT                   /note="Assigned by comparison with orthologs"
FT   UNSURE          23
FT                   /note="Assigned by comparison with orthologs"
FT   NON_CONS        11..12
FT                   /evidence="ECO:0000305"
FT   NON_CONS        22..23
FT                   /evidence="ECO:0000305"
FT   NON_CONS        36..37
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         53
SQ   SEQUENCE   53 AA;  6228 MW;  2DF0ACC7D2852FEA CRC64;
     RYIPYDQEDV KRQMVAAIGI EDKNTVTRAN YYTLDLXIDT VTPDVNRNEL KEK