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Snake venom metalloproteinase BnP2 (SVMP) (EC 3.4.24.-) (Fragments)

 VM1B2_BOTPA             Reviewed;          69 AA.
P0C6S1;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 1.
22-NOV-2017, entry version 44.
RecName: Full=Snake venom metalloproteinase BnP2;
Short=SVMP;
EC=3.4.24.-;
Flags: Fragments;
Bothrops pauloensis (Neuwied's lancehead) (Bothrops neuwiedi
pauloensis).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
NCBI_TaxID=1042543;
[1]
PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
TISSUE=Venom;
PubMed=17889921; DOI=10.1016/j.toxicon.2007.08.005;
Baldo C., Tanjoni I., Leon I.R., Batista I.F.C., Della-Casa M.S.,
Clissa P.B., Weinlich R., Lopes-Ferreira M., Lebrun I.,
Amarante-Mendes G.P., Rodrigues V.M., Perales J., Valente R.H.,
Moura-da-Silva A.M.;
"BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom:
biological effects benchmarking relatively to jararhagin, a P-III
SVMP.";
Toxicon 51:54-65(2008).
-!- FUNCTION: This protein is a zinc protease from snake venom that is
devoid of significant myotoxic and hemorrhagic activities. It
hydrolyzes the Aalpha-chain and more slowly the Bbeta-chain of
fibrin and fibrinogen, without affecting the gamma-chains. It
induces cell detachment and a apoptosis (anoikis) in endothelial
cells (By similarity). {ECO:0000250}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by EDTA. {ECO:0000250}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17889921}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.
P-I subfamily. {ECO:0000305}.
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ProteinModelPortal; P0C6S1; -.
SMR; P0C6S1; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
Pfam; PF01421; Reprolysin; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
1: Evidence at protein level;
Apoptosis; Direct protein sequencing; Fibrinogenolytic toxin;
Fibrinolytic toxin; Hemostasis impairing toxin; Hydrolase;
Metal-binding; Metalloprotease; Protease; Secreted; Toxin; Zinc.
CHAIN <1 >69 Snake venom metalloproteinase BnP2.
/FTId=PRO_0000326272.
DOMAIN <1 >69 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
METAL 3 3 Calcium 1. {ECO:0000250}.
UNSURE 20 20 I or L.
UNSURE 23 23 I or L.
UNSURE 45 45 I or L.
UNSURE 48 48 I or L.
UNSURE 55 55 I or L.
UNSURE 66 66 I or L.
UNSURE 67 67 I or L.
NON_CONS 24 25 {ECO:0000305}.
NON_CONS 53 54 {ECO:0000305}.
NON_TER 1 1
NON_TER 69 69
SEQUENCE 69 AA; 8008 MW; 5F312D4039F2781C CRC64;
YIELAVVADH GMFTKYNSNI DTIRVHEMVN TVDGFFRSMN VDASIANIEV WSKTITSFGE
WRERDIIPR


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