ID   VM3BA_BOTAS             Reviewed;          63 AA.
AC   P84035;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Snake venom metalloproteinase basparin-A;
DE            Short=SVMP;
DE            EC=3.4.24.-;
DE   Flags: Fragments;
OS   Bothrops asper (Terciopelo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=8722;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND GLYCOSYLATION.
RC   TISSUE=Venom;
RX   PubMed=13679078; DOI=10.1016/s0003-9861(03)00385-0;
RA   Loria G.D., Rucavado A., Kamiguti A.S., Theakston R.D.G., Fox J.W.,
RA   Alape A., Gutierrez J.M.;
RT   "Characterization of 'basparin A,' a prothrombin-activating
RT   metalloproteinase, from the venom of the snake Bothrops asper that inhibits
RT   platelet aggregation and induces defibrination and thrombosis.";
RL   Arch. Biochem. Biophys. 418:13-24(2003).
CC   -!- FUNCTION: Snake venom zinc metalloproteinase that catalyzes the
CC       conversion of prothrombin (F2) to alpha-thrombin through formation of a
CC       thrombin intermediate, without requiring additional cofactors. Also
CC       inhibits collagen-dependent platelet aggregation in vitro, an effect
CC       that does not depend on proteolytic activity. In vivo, at low doses,
CC       induces defibrin(ogen)ation when injected intravenously or
CC       intramuscularly into mice. At higher doses, causes sudden death by
CC       intravenous administration due to numerous occluding thrombi in
CC       pulmonary vessels. {ECO:0000269|PubMed:13679078}.
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: Clotting activity on human plasma is not abrogated
CC       by the plasma proteinase inhibitors alpha(2) macroglobulin and
CC       murinoglobulin.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:13679078}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:13679078}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:13679078}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:13679078}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:13679078}.
CC   -!- MISCELLANEOUS: Does not degrade components of the extracellular matrix.
CC       Does not induce local tissue alterations, such as hemorrhage,
CC       myonecrosis, and edema, in mice. Does not induce systemic hemorrhage,
CC       thrombocytopenia nor prolongation of the bleeding time following
CC       intravenous administration.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P84035; -.
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:0016504; F:peptidase activator 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   Blood coagulation cascade activating toxin; Direct protein sequencing;
KW   Disulfide bond; Fibrinogenolytic toxin; Fibrinolytic toxin; Glycoprotein;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Prothrombin activator; Secreted; Toxin; Zinc.
FT   CHAIN           <1..>63
FT                   /note="Snake venom metalloproteinase basparin-A"
FT                   /id="PRO_0000078189"
FT   DOMAIN          <1..>33
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   ACT_SITE        30
FT                   /evidence="ECO:0000250|UniProtKB:P30431,
FT                   ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-
FT                   ProRule:PRU10095"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..45
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   NON_CONS        12..13
FT                   /evidence="ECO:0000303|PubMed:13679078"
FT   NON_CONS        22..23
FT                   /evidence="ECO:0000303|PubMed:13679078"
FT   NON_CONS        33..34
FT                   /evidence="ECO:0000303|PubMed:13679078"
FT   NON_CONS        41..42
FT                   /evidence="ECO:0000303|PubMed:13679078"
FT   NON_CONS        51..52
FT                   /evidence="ECO:0000303|PubMed:13679078"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:13679078"
FT   NON_TER         63
FT                   /evidence="ECO:0000303|PubMed:13679078"
SQ   SEQUENCE   63 AA;  6839 MW;  73BEF2E9F4386351 CRC64;
     SHDNAQLLTA IKAYIATMCD PKMAVIMAHE IGHGGYYGYC RKIPCAPEDV KDDDIGMVLP
     GTK