VM3CX_DABRR
ID VM3CX_DABRR Reviewed; 19 AA.
AC P86536;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Coagulation factor X-activating enzyme heavy chain {ECO:0000250|UniProtKB:Q7LZ61, ECO:0000303|PubMed:20203422};
DE EC=3.4.24.58;
DE AltName: Full=Coagulation factor X-activating enzyme chain alpha {ECO:0000250|UniProtKB:Q7LZ61, ECO:0000303|PubMed:20203422};
DE AltName: Full=RVV-X heavy chain {ECO:0000250|UniProtKB:Q7LZ61, ECO:0000303|PubMed:20203422};
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Fragment;
OS Daboia russelii (Russel's viper) (Vipera russelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=8707;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom {ECO:0000269|PubMed:20203422};
RX PubMed=20203422; DOI=10.2220/biomedres.31.71;
RA Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G.,
RA Athauda S.B., Moriyama A.;
RT "Molecular diversity in venom proteins of the Russell's viper (Daboia
RT russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka.";
RL Biomed. Res. 31:71-81(2010).
CC -!- FUNCTION: Catalytic subunit of coagulation factor X-activating enzyme,
CC a zinc-protease enzyme that acts in hemostasis. Activates coagulation
CC factor X (F10) by cleaving the Arg-Ile bond at position 234 and is also
CC able to activate coagulation factor IX (F9) and protein C (PROC) by
CC specific cleavage of Arg-Ile and Arg-Val bonds (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specifically activates several components of the blood
CC clotting system, including coagulation factor X, coagulation factor
CC IX and protein C by cleavage of Arg-|-Xaa bonds. Has no action on
CC insulin B chain.; EC=3.4.24.58;
CC Evidence={ECO:0000250|UniProtKB:Q7LZ61};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q4VM07};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q4VM07};
CC -!- SUBUNIT: Heterotrimer; disulfide-linked. The heterotrimer consists of 1
CC heavy chain and 2 light chains (lectins): LC1 and LC2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20203422}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20203422}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q7LZ61}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIId sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P86536; -.
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: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; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..>19
FT /note="Coagulation factor X-activating enzyme heavy chain"
FT /id="PRO_0000394729"
FT DOMAIN 10..>19
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT NON_TER 19
FT /evidence="ECO:0000303|PubMed:20203422"
SQ SEQUENCE 19 AA; 2152 MW; DBCD26FBC25D2B47 CRC64;
VATSEQFNKT FIELVIVVD
