VM1B1_BOTBA
ID VM1B1_BOTBA Reviewed; 202 AA.
AC P86976;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Zinc metalloproteinase barnettlysin-1 {ECO:0000303|PubMed:26723171};
DE EC=3.4.24.- {ECO:0000269|PubMed:26723171};
DE AltName: Full=Barnettlysin-I {ECO:0000303|PubMed:26723171};
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
OS Bothrops barnetti (Barnett's lancehead) (Trimeresurus barnetti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=1051630;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:26723171};
RX PubMed=26723171; DOI=10.1016/j.bbagen.2015.12.021;
RA Sanchez E.F., Richardson M., Gremski L.H., Veiga S.S., Yarleque A.,
RA Niland S., Lima A.M., Estevao-Costa M.I., Eble J.A.;
RT "A novel fibrinolytic metalloproteinase, barnettlysin-I from Bothrops
RT barnetti (Barnett's pitviper) snake venom with anti-platelet properties.";
RL Biochim. Biophys. Acta 1860:542-556(2016).
CC -!- FUNCTION: Non-hemorrhagic metalloproteinase that hydrolyzes the alpha
CC chains of fibrinogen and fibrin but has no activity on beta- and gamma-
CC chains. Cleaves X-Leu bonds. Inhibits platelet aggregation induced by
CC the von Willebrand factor (VWF) (IC(50) is 1.4 uM) and type I collagen
CC (IC(50) is 3.2 uM). Acts by cleaving the vWF and its receptor GPIb, and
CC by cleaving the collagen-binding Alpha-2A domain of the collagen
CC receptor alpha-2/beta-1 integrin (ITGA2/ITGB1). Also degrades the
CC extracellular matrix protein fibronectin (FN1), but has no effect on
CC laminin and type I collagen. {ECO:0000269|PubMed:26723171}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:26723171};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P60244};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26723171}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:26723171}.
CC -!- MASS SPECTROMETRY: Mass=23386; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:26723171};
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044485; P:envenomation resulting in fibrinogenolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044484; P:envenomation resulting in fibrinolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044477; P:envenomation resulting in negative regulation of platelet aggregation in another organism; IDA:UniProtKB.
DR GO; GO:0044481; P:envenomation resulting in proteolysis in another organism; IDA:UniProtKB.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Fibrinogenolytic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..202
FT /note="Zinc metalloproteinase barnettlysin-1"
FT /id="PRO_0000412998"
FT DOMAIN 6..200
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 143
FT /evidence="ECO:0000250|UniProtKB:P60244,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 9
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P60244,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P60244,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P60244,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT DISULFID 117..197
FT /evidence="ECO:0000250|UniProtKB:P60244,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 157..181
FT /evidence="ECO:0000250|UniProtKB:P60244,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 159..164
FT /evidence="ECO:0000250|UniProtKB:P60244,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 202 AA; 22927 MW; B40376E4FEF2562B CRC64;
TPEQQRYVEL FIVVDHGMFM KXXXXXXXXX XXIHQMVNIM KEAYRYLYID ILLTGVEIWS
NKDLINVQPA APQTLDSFGE WRXXXXXXXK SHDNAQLLTS TDFDGPTIGL AYVGSMCDPK
RSTAVIQDHS EIDLLVAVTM DHELGHNLGI RHDTGSCSCG GYPCVMSPVI SHDISKYFSD
CSYIQCWDFI MKENPQCILN KR
