VM1B2_BOTPA
ID VM1B2_BOTPA Reviewed; 69 AA.
AC P0C6S1;
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 BnP2;
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, 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 (By
CC similarity). {ECO:0000250}.
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:0000250}.
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; P0C6S1; -.
DR SMR; P0C6S1; -.
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.
DR PROSITE; PS50215; ADAM_MEPRO; 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..>69
FT /note="Snake venom metalloproteinase BnP2"
FT /id="PRO_0000326272"
FT DOMAIN <1..>69
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 3
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT UNSURE 20
FT /note="I or L"
FT UNSURE 23
FT /note="I or L"
FT UNSURE 45
FT /note="I or L"
FT UNSURE 48
FT /note="I or L"
FT UNSURE 55
FT /note="I or L"
FT UNSURE 66
FT /note="I or L"
FT UNSURE 67
FT /note="I or L"
FT NON_CONS 24..25
FT /evidence="ECO:0000305"
FT NON_CONS 53..54
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 69
SQ SEQUENCE 69 AA; 8008 MW; 5F312D4039F2781C CRC64;
YIELAVVADH GMFTKYNSNI DTIRVHEMVN TVDGFFRSMN VDASIANIEV WSKTITSFGE
WRERDIIPR
