ID   VMXCA_CROAT             Reviewed;          25 AA.
AC   Q9PS48;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Snake venom metalloproteinase catroxase;
DE            Short=SVMP;
DE            EC=3.4.21.-;
DE   Flags: Fragment;
OS   Crotalus atrox (Western diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8730;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=1520324; DOI=10.1016/s0006-291x(05)81505-0;
RA   Chiou S.-H., Hung C.-C., Huang K.-F.;
RT   "Characterization of a protease with alpha- and beta-fibrinogenase activity
RT   from the Western diamondback rattlesnake, Crotalus atrox.";
RL   Biochem. Biophys. Res. Commun. 187:389-396(1992).
CC   -!- FUNCTION: Metalloprotease that is highly active against alpha-(FGA) and
CC       beta-chains (FGB) of fibrinogen molecules.
CC       {ECO:0000269|PubMed:1520324}.
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, beta-mercaptoethanol, but not
CC       by PMSF, p-tosyl-L-phenylalanine chloromethyl ketone, p-tosyl-L-lysine
CC       chloromethyl ketone, soybean trypsin inhibitor and aprotinin.
CC       {ECO:0000269|PubMed:1520324}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1520324}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Acidic protein of about 24 kDa.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC       {ECO:0000305}.
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DR   PIR; PC1119; PC1119.
DR   AlphaFoldDB; Q9PS48; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase 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; Direct protein sequencing; Fibrinogenolytic toxin;
KW   Hemostasis impairing toxin; Hydrolase; Metal-binding; Protease; Secreted;
KW   Toxin; Zinc.
FT   CHAIN           1..>25
FT                   /note="Snake venom metalloproteinase catroxase"
FT                   /id="PRO_0000407590"
FT   BINDING         9
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   NON_TER         25
SQ   SEQUENCE   25 AA;  2998 MW;  2E38386ED8DDC68C CRC64;
     TPDHQRYVEL FIVVDHGMYT KYNGD