VM11_BOTPA
ID VM11_BOTPA Reviewed; 175 AA.
AC C0HJU2;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=Snake venom metalloproteinase BpMP-1 {ECO:0000303|PubMed:22008900};
DE Short=SVMP {ECO:0000303|PubMed:22008900};
DE EC=3.4.24.- {ECO:0000269|PubMed:22008900};
DE AltName: Full=Fibrinogenolytic metalloproteinase {ECO:0000303|PubMed:22008900};
DE Flags: Fragments;
OS Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi pauloensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=1042543;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom {ECO:0000303|PubMed:22008900};
RX PubMed=22008900; DOI=10.1016/j.cbpb.2011.10.002;
RA Naves de Souza D.L., Gomes M.S., Ferreira F.B., Rodrigues R.S., Ache D.C.,
RA Richardson M., Borges M.H., Rodrigues V.M.;
RT "Biochemical and enzymatic characterization of BpMP-I, a fibrinogenolytic
RT metalloproteinase isolated from Bothropoides pauloensis snake venom.";
RL Comp. Biochem. Physiol. 161:102-109(2012).
CC -!- FUNCTION: Non-hemorrhagic snake venom zinc metalloprotease that
CC hydrolyzes the Aalpha-chain of fibrinogen, more slowly the Bbeta-chain
CC and shows no effect on the gamma chain. Has no coagulant activity on
CC bovine plasma and fibrinogen. {ECO:0000269|PubMed:22008900}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22008900};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P85314};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, 1,10-phenanthroline and beta-
CC mercaptoethanol. Not inhibited by the serine protease inhibitors
CC aprotinin and benzamidin. {ECO:0000269|PubMed:22008900}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Highest activity at neutral to basic pH. Reduced activity at pH 3.0.
CC {ECO:0000269|PubMed:22008900};
CC Temperature dependence:
CC Activity is highest at 4 degrees Celsius, decreases with increasing
CC temperatures and is lost at 60 degrees Celsius.
CC {ECO:0000269|PubMed:22008900};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22008900}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22008900}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:22008900}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305|PubMed:22008900}.
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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 CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF01421; Reprolysin; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..175
FT /note="Snake venom metalloproteinase BpMP-1"
FT /id="PRO_0000433783"
FT DOMAIN 1..>175
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 3
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P85314"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P85314"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P85314"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P85314"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P85314"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P85314"
FT BINDING 174
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P85314"
FT DISULFID 98..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 131..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 133..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT NON_CONS 56..57
FT /evidence="ECO:0000305|PubMed:22008900"
FT NON_TER 1
FT /evidence="ECO:0000305|PubMed:22008900"
FT NON_TER 175
FT /evidence="ECO:0000305|PubMed:22008900"
SQ SEQUENCE 175 AA; 19538 MW; D3B1FDE876EF5D81 CRC64;
YIELAVVADH GMFTKYNSNV NTIRTWVHEM VNSLNGFFRS MXVDDASLVN LEVWSKTLTS
FGEWRDLLPR ISHDHAQLLT TIVFDQQTIG IAYTAGMCDP SQSVAVVMDH VAVTMAHELG
HNLGMDHDDT CTCGAKSCIM ASTISKGLSF EFSDCSQNQY QTYVTKHNPQ CILNK
