ID   VM3BG_BOTAL             Reviewed;          62 AA.
AC   P0C7B1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Zinc metalloproteinase-disintegrin-like BaG;
DE            EC=3.4.24.-;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Flags: Fragments;
OS   Bothrops alternatus (Urutu) (Rhinocerophis alternatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=64174;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=12893294; DOI=10.1016/s0003-9861(03)00298-4;
RA   Cominetti M.R., Ribeiro J.U., Fox J.W., Selistre-de-Araujo H.S.;
RT   "BaG, a new dimeric metalloproteinase/disintegrin from the Bothrops
RT   alternatus snake venom that interacts with alpha5beta1 integrin.";
RL   Arch. Biochem. Biophys. 416:171-179(2003).
CC   -!- FUNCTION: Snake venom Zinc metalloproteinase that inhibits ADP-induced
CC       platelet aggregation and inhibits the alpha-5/beta-1 (ITGA5/ITGB1)
CC       integrin, a fibronectin receptor. Has caseinolytic activity. Induces
CC       the detachment of cells that are bound to fibronectin.
CC       {ECO:0000269|PubMed:12893294}.
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: Inhibited by EDTA, and 1,10-phenanthroline.
CC       {ECO:0000269|PubMed:12893294}.
CC   -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:12893294}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12893294}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:12893294}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: Has no effect on alpha-2/beta-1 (ITGA2/ITGB1) integrin.
CC       Does not have hemorrhagic activity (PubMed:12893294).
CC       {ECO:0000305|PubMed:12893294}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIIc sub-subfamily. {ECO:0000305}.
CC   -!- CAUTION: Gly-60 is present instead of the conserved His which is
CC       expected to be zinc-binding residue. There is therefore some
CC       uncertainty concerning the enzymatic activity of this protein.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0C7B1; -.
DR   SMR; P0C7B1; -.
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.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion impairing toxin; Direct protein sequencing; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Platelet aggregation inhibiting toxin; Protease; Secreted; Toxin; Zinc.
FT   CHAIN           <1..>62
FT                   /note="Zinc metalloproteinase-disintegrin-like BaG"
FT                   /id="PRO_0000330007"
FT   DOMAIN          <24..>54
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT                   ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_CONS        12..13
FT                   /evidence="ECO:0000305"
FT   NON_CONS        23..24
FT                   /evidence="ECO:0000305"
FT   NON_CONS        37..38
FT                   /evidence="ECO:0000305"
FT   NON_CONS        54..55
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         62
SQ   SEQUENCE   62 AA;  6650 MW;  8D9C917461155023 CRC64;
     SISACNGLKG HFLIEPLKLS DSEKTDLLNR SHDNAQLSPI NLVVAVIMAH EMGHGMVLPG
     TK