VMXJ4_BOTJA
ID VMXJ4_BOTJA Reviewed; 47 AA.
AC P0C6S6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Snake venom metalloproteinase jararafibrase-4;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Jararafibrase IV;
DE Flags: Fragment;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=12165326; DOI=10.1016/s0041-0101(02)00116-2;
RA Maruyama M., Sugiki M., Anai K., Yoshida E.;
RT "N-terminal amino acid sequences and some characteristics of
RT fibrinolytic/hemorrhagic metalloproteinases purified from Bothrops jararaca
RT venom.";
RL Toxicon 40:1223-1226(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=8087204; DOI=10.1159/000468668;
RA Maruyama M., Tanigawa M., Sugiki M., Yoshida E., Mihara H.;
RT "Purification and characterization of low molecular weight
RT fibrinolytic/hemorrhagic enzymes from snake (Bothrops jararaca) venom.";
RL Enzyme Protein 47:124-135(1993).
CC -!- FUNCTION: The metalloproteinase is a probable venom zinc protease that
CC induces local hemorrhage in the skin of rats. Degrades type-IV
CC collagen, gelatin, laminin and fibronectin. Has fibrinolytic
CC activities. Has high hemagglutinating activity on red blood cells.
CC Cleaves insulin B chain at 29-His-|-Leu-30, and 38-Ala-|-Leu-39 bonds
CC (PubMed:8087204). {ECO:0000269|PubMed:12165326,
CC ECO:0000269|PubMed:8087204}.
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 1,10-phenanthroline and EDTA.
CC {ECO:0000269|PubMed:8087204}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8087204}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
CC {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR Pfam; PF01421; Reprolysin; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Fibrinolytic toxin; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..>47
FT /note="Snake venom metalloproteinase jararafibrase-4"
FT /id="PRO_0000326427"
FT DOMAIN 6..>47
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 9
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CONFLICT 41
FT /note="K -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 47
SQ SEQUENCE 47 AA; 5801 MW; A3D23545E33ECBCE CRC64;
TPEHQRYIEL FLVVDHGMFM KYNGNSDKIY YYIHQMVNIM KXAYXYL
