ID   VM3C1_ECHCA             Reviewed;          32 AA.
AC   Q9PRP9;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Zinc metalloproteinase carinactivase-1 catalytic subunit;
DE            Short=CA-1 catalytic subunit;
DE            EC=3.4.24.-;
DE   AltName: Full=Carinactivase-1 62 kDa subunit;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Flags: Fragment;
OS   Echis carinatus (Saw-scaled viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=40353;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, COFACTOR, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=8617803; DOI=10.1074/jbc.271.9.5200;
RA   Yamada D., Sekiya F., Morita T.;
RT   "Isolation and characterization of carinactivase, a novel prothrombin
RT   activator in Echis carinatus venom with a unique catalytic mechanism.";
RL   J. Biol. Chem. 271:5200-5207(1996).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=10336237; DOI=10.1016/s0049-3848(98)00212-6;
RA   Yamada D., Morita T.;
RT   "CA-1 method, a novel assay for quantification of normal prothrombin using
RT   a Ca2+ -dependent prothrombin activator, carinactivase-1.";
RL   Thromb. Res. 94:221-226(1999).
CC   -!- FUNCTION: Calcium-dependent prothrombin (F2) activator. This protein
CC       may activate prothrombin via recognition by the regulatory subunit of
CC       the calcium ion bound conformation of its gamma-carboxyglutamic acid
CC       (GLA) domain, and the subsequent conversion of prothrombin to active
CC       thrombin is catalyzed by the catalytic subunit.
CC       {ECO:0000269|PubMed:8617803}.
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: Heterodimer of a metalloproteinase subunit and a regulatory
CC       subunit comprising two disulfide-linked lectins (14 kDa and 17 kDa
CC       chains) (AC Q9PRP7 and AC Q9PRP8). {ECO:0000269|PubMed:8617803}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- BIOTECHNOLOGY: Used for quantification of normal prothrombin (CA-1
CC       method). {ECO:0000269|PubMed:10336237}.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIId sub-subfamily. {ECO:0000305}.
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DR   MEROPS; M12.172; -.
DR   BRENDA; 3.4.24.49; 2035.
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.
PE   1: Evidence at protein level;
KW   Blood coagulation cascade activating toxin; Calcium;
KW   Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Prothrombin activator;
KW   Secreted; Toxin; Zinc.
FT   CHAIN           1..>32
FT                   /note="Zinc metalloproteinase carinactivase-1 catalytic
FT                   subunit"
FT                   /id="PRO_0000078201"
FT   DOMAIN          10..>32
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   NON_TER         32
SQ   SEQUENCE   32 AA;  3751 MW;  1A1B1496A3D26449 CRC64;
     SRKQKFDKKF IKLVIVVDHS MVXKXNNDLI AI