VM1B1_BOTPA
ID VM1B1_BOTPA Reviewed; 83 AA.
AC P0C6S0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Snake venom metalloproteinase BnP1;
DE Short=SVMP;
DE EC=3.4.24.-;
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]
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=17889921; DOI=10.1016/j.toxicon.2007.08.005;
RA Baldo C., Tanjoni I., Leon I.R., Batista I.F.C., Della-Casa M.S.,
RA Clissa P.B., Weinlich R., Lopes-Ferreira M., Lebrun I.,
RA Amarante-Mendes G.P., Rodrigues V.M., Perales J., Valente R.H.,
RA Moura-da-Silva A.M.;
RT "BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom:
RT biological effects benchmarking relatively to jararhagin, a P-III SVMP.";
RL Toxicon 51:54-65(2008).
CC -!- FUNCTION: This protein is a zinc protease from snake venom that is
CC devoid of significant myotoxic and hemorrhagic activities. It
CC hydrolyzes the Aalpha-chain and more slowly the Bbeta-chain of fibrin
CC and fibrinogen, without affecting the gamma-chains. It induces cell
CC detachment and a apoptosis (anoikis) in endothelial cells.
CC {ECO:0000269|PubMed:17889921}.
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. {ECO:0000269|PubMed:17889921}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17889921}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C6S0; -.
DR SMR; P0C6S0; -.
DR MEROPS; M12.325; -.
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:0006915; P:apoptotic process; 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.
PE 1: Evidence at protein level;
KW Apoptosis; Direct protein sequencing; Fibrinogenolytic toxin;
KW Fibrinolytic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..83
FT /note="Snake venom metalloproteinase BnP1"
FT /id="PRO_0000326271"
FT DOMAIN 8..83
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT UNSURE 28
FT /note="I or L"
FT UNSURE 31
FT /note="I or L"
FT UNSURE 33
FT /note="I or L"
FT UNSURE 48
FT /note="I or L"
FT UNSURE 59
FT /note="I or L"
FT UNSURE 60
FT /note="I or L"
FT UNSURE 65
FT /note="I or L"
FT UNSURE 70
FT /note="I or L"
FT UNSURE 78
FT /note="I or L"
FT UNSURE 79
FT /note="I or L"
FT UNSURE 83
FT /note="I or L"
FT NON_CONS 32..33
FT /evidence="ECO:0000305"
FT NON_CONS 46..47
FT /evidence="ECO:0000305"
FT NON_CONS 62..63
FT /evidence="ECO:0000305"
FT NON_CONS 72..73
FT /evidence="ECO:0000305"
SQ SEQUENCE 83 AA; 9571 MW; F7773FC639FE7FC3 CRC64;
SQIKFKPSYI ELAVVADHGM FTKYNSNINT IRIVHEMVNT VDGFFRTITS FGEWRERDII
PRSCIMASTI SKHNPQCIIN QPI
