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Snake venom metalloproteinase BnP1 (SVMP) (EC 3.4.24.-) (Fragments)

 VM1B1_BOTPA             Reviewed;          83 AA.
P0C6S0;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
18-MAR-2008, sequence version 1.
22-NOV-2017, entry version 43.
RecName: Full=Snake venom metalloproteinase BnP1;
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, FUNCTION,
ENZYME REGULATION, 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. {ECO:0000269|PubMed:17889921}.
-!- 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:0000269|PubMed:17889921}.
-!- 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; P0C6S0; -.
SMR; P0C6S0; -.
MEROPS; M12.172; -.
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.
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 83 Snake venom metalloproteinase BnP1.
/FTId=PRO_0000326271.
DOMAIN 8 83 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
METAL 11 11 Calcium 1. {ECO:0000250}.
METAL 77 77 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 80 80 Calcium 1. {ECO:0000250}.
UNSURE 28 28 I or L.
UNSURE 31 31 I or L.
UNSURE 33 33 I or L.
UNSURE 48 48 I or L.
UNSURE 59 59 I or L.
UNSURE 60 60 I or L.
UNSURE 65 65 I or L.
UNSURE 70 70 I or L.
UNSURE 78 78 I or L.
UNSURE 79 79 I or L.
UNSURE 83 83 I or L.
NON_CONS 32 33 {ECO:0000305}.
NON_CONS 46 47 {ECO:0000305}.
NON_CONS 62 63 {ECO:0000305}.
NON_CONS 72 73 {ECO:0000305}.
SEQUENCE 83 AA; 9571 MW; F7773FC639FE7FC3 CRC64;
SQIKFKPSYI ELAVVADHGM FTKYNSNINT IRIVHEMVNT VDGFFRTITS FGEWRERDII
PRSCIMASTI SKHNPQCIIN QPI


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