ID   VM3M_ECHML              Reviewed;          27 AA.
AC   P81797;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Zinc metalloproteinase multactivase catalytic subunit;
DE            EC=3.4.24.-;
DE   AltName: Full=Snake venom metalloproteinase;
DE            Short=SVMP;
DE   Flags: Fragment;
OS   Echis multisquamatus (Central Asian sand viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=93050 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC   TISSUE=Venom;
RX   PubMed=9443815; DOI=10.1093/oxfordjournals.jbchem.a021862;
RA   Yamada D., Morita T.;
RT   "Purification and characterization of a Ca2+ -dependent prothrombin
RT   activator, multactivase, from the venom of Echis multisquamatus.";
RL   J. Biochem. 122:991-997(1997).
CC   -!- FUNCTION: This carinactivase-like calcium-dependent prothrombin (F2)
CC       activator activates prothrombin via recognition of the calcium ion
CC       bound conformation of its gamma-carboxyglutamic acid (GLA) domain, and
CC       the subsequent conversion of prothrombin to active thrombin is
CC       catalyzed by the catalytic subunit. {ECO:0000269|PubMed:9443815}.
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 homologous disulfide-linked lectins (AC P81798).
CC       {ECO:0000269|PubMed:9443815}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC       subfamily. P-IIId sub-subfamily. {ECO:0000305}.
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DR   PIR; PC4420; PC4420.
DR   MEROPS; M12.177; -.
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..>27
FT                   /note="Zinc metalloproteinase multactivase catalytic
FT                   subunit"
FT                   /id="PRO_0000078202"
FT   DOMAIN          12..>27
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT   BINDING         14
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   NON_TER         27
SQ   SEQUENCE   27 AA;  3210 MW;  02572A32B1E54CD3 CRC64;
     FPPHKGKFDK KFIELVIIVD HSXXTYK