VM11_BOTAT
ID VM11_BOTAT Reviewed; 202 AA.
AC P85420;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Snake venom metalloproteinase atroxlysin-1;
DE Short=SVMP;
DE EC=3.4.24.-;
DE AltName: Full=Atroxlysin-I;
OS Bothrops atrox (Barba amarilla) (Fer-de-lance).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8725;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=20102699; DOI=10.1016/j.abb.2010.01.010;
RA Sanchez E.F., Schneider F.S., Yarleque A., Borges M.H., Richardson M.,
RA Figueiredo S.G., Evangelista K.S., Eble J.A.;
RT "The novel metalloproteinase atroxlysin-I from Peruvian Bothrops atrox
RT (Jergon) snake venom acts both on blood vessel ECM and platelets.";
RL Arch. Biochem. Biophys. 496:9-20(2010).
RN [2]
RP PROTEIN SEQUENCE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Venom;
RA Sanchez E.F., Richardson M.;
RT "Complete amino acid sequence of atroxlysin-I, a metalloproteinase from
RT Peruvian Bothrops atrox (Jergon) venom.";
RL Submitted (JUN-2011) to UniProtKB.
CC -!- FUNCTION: Snake venom zinc metalloproteinase that acts on fibrinogen,
CC fibrin, fibronectin (FN1), type I collagen, type IV collagen, integrin
CC alpha-7/beta-1 (ITGA7/ITGB1) and integrin alpha-1/beta-1 (ITGA1/ITGB1).
CC Binds to fibronectin (FN1), fibrinogen and, weakly, to type I collagen
CC and laminin. Cleaves Xaa-Leu bonds. Inhibits ADP- and collagen-induced
CC platelet aggregation both in the presence (IC(50)=1.4 uM for collagen)
CC and in the absence (IC(50)=2.2 uM for collagen) of cofactors. Has
CC hemorrhagic activity. {ECO:0000269|PubMed:20102699}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20102699};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:20102699};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, DTT and high concentrations of
CC zinc ions (>2 mM). Weakly inhibited by TLCK. Not inhibited by PMSF.
CC Activated by calcium ions. {ECO:0000269|PubMed:20102699}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20102699}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20102699}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:20102699}.
CC -!- MISCELLANEOUS: Does not cleave laminin-1 (laminin-111,
CC LAMA1/LAMB1/LAMC1), integrin alpha-2/beta-1 (ITGA2/ITGB1) or integrin
CC alpha-3/beta-1 (ITGA3/ITGB1). {ECO:0000305|PubMed:20102699}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P85420; -.
DR SMR; P85420; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IMP:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0044482; P:envenomation resulting in blood vessel extracellular matrix damage, causing hemorrhagic damage in another organism; IDA:UniProtKB.
DR GO; GO:0044484; P:envenomation resulting in fibrinolysis in another organism; IDA:UniProtKB.
DR GO; GO:0044358; P:envenomation resulting in hemorrhagic damage in another organism; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0035893; P:negative regulation of platelet aggregation 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.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Fibrinolytic toxin;
KW Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Platelet aggregation inhibiting toxin; Protease; Secreted;
KW Toxin; Zinc.
FT CHAIN 1..202
FT /note="Snake venom metalloproteinase atroxlysin-1"
FT /id="PRO_0000341531"
FT DOMAIN 6..202
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT ACT_SITE 143
FT /evidence="ECO:0000250|UniProtKB:P83512,
FT ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-
FT ProRule:PRU10095"
FT BINDING 9
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT DISULFID 117..197
FT /evidence="ECO:0000250|UniProtKB:Q9PW35,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 157..181
FT /evidence="ECO:0000250|UniProtKB:Q9PW35,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 159..164
FT /evidence="ECO:0000250|UniProtKB:Q9PW35,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT CONFLICT 100
FT /note="S -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 104..109
FT /note="NGPTIG -> DQVTIN (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="V -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..121
FT /note="PKR -> LNK (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22918 MW; 61DB77A8AFD27E29 CRC64;
TPEQQRYVDL FIVVDHGMFM KYNGNSDKIR RRIHQMVNIM KEAYSTMYID ILLTGVEIWS
NKDLINVQPA APQTLDSFGE WRKTDLLNRK SHDNAQLLTS TDFNGPTIGL AYVGSMCDPK
RSTGVIQDHS EQDLMVAITM AHELGHNLGI SHDTGSCSCG GYSCIMSPVL SHEPSKYFSD
CSYIQCWDFI MKENPQCILN KR
