VM3AH_NAJAT
ID VM3AH_NAJAT Reviewed; 16 AA.
AC P0DJJ1;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Zinc metalloproteinase atrahagin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Fragment;
OS Naja atra (Chinese cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8656;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=16310401; DOI=10.1016/j.biocel.2005.10.011;
RA Wei J.-F., Mo Y.-Z., Qiao L.-Y., Wei X.-L., Chen H.-Q., Xie H., Fu Y.-L.,
RA Wang W.-Y., Xiong Y.-L., He S.-H.;
RT "Potent histamine-releasing activity of atrahagin, a novel snake venom
RT metalloproteinase.";
RL Int. J. Biochem. Cell Biol. 38:510-520(2006).
CC -!- FUNCTION: Snake venom zinc metalloprotease that causes mast cell
CC degranulation and histamine release. Selectively degrades the alpha-
CC chain of human fibrinogen (FGA). {ECO:0000269|PubMed:16310401}.
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 and EGTA, but not by PMSF and
CC leupeptin. {ECO:0000269|PubMed:16310401}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16310401}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Does not degrade the beta- and the gamma-chain of
CC fibrinogen. Does not induce skin hemorrhage when subcutaneously
CC injected into mice (5 or 50 ug) (PubMed:16310401).
CC {ECO:0000305|PubMed:16310401}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0DJJ1; -.
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 Calcium; Direct protein sequencing; Fibrinogenolytic toxin; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..>16
FT /note="Zinc metalloproteinase atrahagin"
FT /id="PRO_0000418046"
FT DOMAIN 14..>16
FT /note="Peptidase M12B"
FT NON_TER 16
SQ SEQUENCE 16 AA; 2005 MW; 0C4542DA0EE68F8D CRC64;
TNTPEDDRYL QDYVYI