ID   VM1BJ_BOTJA             Reviewed;          60 AA.
AC   P0C7A9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Snake venom metalloproteinase bothrojaractivase;
DE            Short=SVMP;
DE            EC=3.4.24.-;
DE   Flags: Fragments;
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, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=18262582; DOI=10.1016/j.toxicon.2007.09.005;
RA   Berger M., Pinto A.F.M., Guimaraes J.A.;
RT   "Purification and functional characterization of bothrojaractivase, a
RT   prothrombin-activating metalloproteinase isolated from Bothrops jararaca
RT   snake venom.";
RL   Toxicon 51:488-501(2008).
CC   -!- FUNCTION: Prothrombin (F2) activator that is cofactor-independent. Also
CC       has fibrinolytic and fibrinogenolytic activity. It degrades the Aalpha-
CC       chain and more slowly the Bbeta-chain of fibrin and fibrinogen, while
CC       the gamma-chain is only partially and slowly affected. A dose-dependent
CC       procoagulant activity is shown in human plasma.
CC       {ECO:0000269|PubMed:18262582}.
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: Completely inhibited by EDTA and EGTA. Partially
CC       inhibited by serine proteinase inhibitors PMSF and benzamidine. Not
CC       inhibited by cysteine proteinase inhibitors mercury ions and E-64. Is
CC       active without cofactors, although the presence of low concentrations
CC       of calcium and zinc ions enhanced its ability to convert prothrombin
CC       (F2) into active thrombin. {ECO:0000269|PubMed:18262582}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:18262582};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18262582}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18262582}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18262582}.
CC   -!- MASS SPECTROMETRY: Mass=22829; Mass_error=45; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18262582};
CC   -!- MISCELLANEOUS: Does not present direct thrombin-like or amidolytic
CC       activities. {ECO:0000305|PubMed:18262582}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0C7A9; -.
DR   SMR; P0C7A9; -.
DR   MEROPS; M12.341; -.
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   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Calcium;
KW   Direct protein sequencing; Fibrinogenolytic toxin; Fibrinolytic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Prothrombin activator; Secreted; Toxin; Zinc.
FT   CHAIN           <1..>60
FT                   /note="Snake venom metalloproteinase bothrojaractivase"
FT                   /id="PRO_0000329994"
FT   DOMAIN          1..>60
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         4
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        17..18
FT                   /evidence="ECO:0000305"
FT   NON_CONS        32..33
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         60
SQ   SEQUENCE   60 AA;  7166 MW;  E0EEA950A50EF304 CRC64;
     RYIELAVVAD HGMFTKYRVH ELVNTVNGFF RSKQDLIKVQ KDKTLTSFGE WRERDLLPRI