ID   VM3B_BOTJA              Reviewed;          25 AA.
AC   P22028;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Zinc metalloproteinase-disintegrin-like botrocetin;
DE            EC=3.4.24.-;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   AltName: Full=von Willebrand factor-dependent platelet coagglutinin;
DE   Contains:
DE     RecName: Full=Disintegrin-like botrocetin;
DE   Flags: Fragment;
OS   Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8724;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=1993206; DOI=10.1021/bi00221a032;
RA   Fujimura Y., Titani K., Usami Y., Suzuki M., Oyama R., Matsui T., Fukui H.,
RA   Sugimoto M., Ruggeri Z.M.;
RT   "Isolation and chemical characterization of two structurally and
RT   functionally distinct forms of botrocetin, the platelet coagglutinin
RT   isolated from the venom of Bothrops jararaca.";
RL   Biochemistry 30:1957-1964(1991).
CC   -!- FUNCTION: Metalloproteinase that binds to von Willebrand factor (VWF)
CC       and induces its interaction with GPIb (GP1BA), resulting in platelet
CC       aggregation.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. Botrocetin and vWF form a soluble complex.
CC       {ECO:0000269|PubMed:1993206}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: There are two distinct forms of the vWF-dependent
CC       platelet coagglutinin. The dimeric form (snaclec) is 34-fold more
CC       active than the metalloprotease botrocetin in promoting vWF binding to
CC       platelets (PubMed:1993206). {ECO:0000305|PubMed:1993206}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P22028; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0035893; P:negative regulation of platelet aggregation in another organism; IDA:CACAO.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion impairing toxin; Direct protein sequencing;
KW   Disulfide bond; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW   Platelet aggregation activating toxin; Secreted; Toxin; Zinc.
FT   CHAIN           <1..>25
FT                   /note="Zinc metalloproteinase-disintegrin-like botrocetin"
FT                   /id="PRO_0000046696"
FT   CHAIN           1..>25
FT                   /note="Disintegrin-like botrocetin"
FT                   /id="PRO_0000422424"
FT   DOMAIN          4..>25
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           17..19
FT                   /note="D/ECD-tripeptide"
FT   BINDING         6
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   DISULFID        18..?
FT                   /evidence="ECO:0000250"
FT   DISULFID        20..?
FT                   /evidence="ECO:0000250"
FT   VARIANT         2
FT                   /note="I -> V"
FT   UNSURE          20
FT                   /note="Assigned by comparison with orthologs"
FT   NON_TER         1
FT   NON_TER         25
SQ   SEQUENCE   25 AA;  2648 MW;  D25D9031A7119AF8 CRC64;
     IISPPVCGNE LLEEGEECDC GTPEN