VM31_BOTAT
ID VM31_BOTAT Reviewed; 423 AA.
AC C5H5D2;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like batroxstatin-1;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloprotease;
DE Short=SVMP;
DE AltName: Full=Vascular apoptosis-inducing protein-like;
DE Short=VAP-like;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=18926840; DOI=10.1016/j.toxicon.2008.08.022;
RA Tavares N.A.C., Correia J.M., Guarnieri M.C., Lima-Filho J.L.,
RA Prieto-da-Silva A.R.B., Radis-Baptista G.;
RT "Expression of mRNAs coding for VAP1/crotastatin-like metalloproteases in
RT the venom glands of three South American pit vipers assessed by
RT quantitative real-time PCR.";
RL Toxicon 52:897-907(2008).
CC -!- FUNCTION: Snake venom zinc metalloprotease that induces apoptosis in
CC vascular endothelial cells (VEC), without degrading the extracellular
CC matrix (it cannot cleave collagen) or inhibiting adhesion of VEC. Has
CC also fibrinogenolytic and hemorrhagic activities (By similarity).
CC {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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks a Cys at position 176 preventing the formation of a
CC homodimer. {ECO:0000305}.
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DR EMBL; EU733639; ACI02287.1; -; mRNA.
DR AlphaFoldDB; C5H5D2; -.
DR SMR; C5H5D2; -.
DR MEROPS; M12.159; -.
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 CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Calcium; Cell adhesion impairing toxin; Disulfide bond;
KW Fibrinogenolytic toxin; Glycoprotein; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Secreted; Toxin; Zinc.
FT CHAIN 1..423
FT /note="Zinc metalloproteinase-disintegrin-like
FT batroxstatin-1"
FT /id="PRO_0000418198"
FT DOMAIN 10..206
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 214..300
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 278..280
FT /note="D/ECD-tripeptide"
FT ACT_SITE 147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 13
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..201
FT /evidence="ECO:0000250"
FT DISULFID 161..185
FT /evidence="ECO:0000250"
FT DISULFID 163..168
FT /evidence="ECO:0000250"
FT DISULFID 217..246
FT /evidence="ECO:0000250"
FT DISULFID 228..241
FT /evidence="ECO:0000250"
FT DISULFID 230..236
FT /evidence="ECO:0000250"
FT DISULFID 240..263
FT /evidence="ECO:0000250"
FT DISULFID 254..260
FT /evidence="ECO:0000250"
FT DISULFID 259..285
FT /evidence="ECO:0000250"
FT DISULFID 272..292
FT /evidence="ECO:0000250"
FT DISULFID 279..311
FT /evidence="ECO:0000250"
FT DISULFID 304..316
FT /evidence="ECO:0000250"
FT DISULFID 323..373
FT /evidence="ECO:0000250"
FT DISULFID 338..384
FT /evidence="ECO:0000250"
FT DISULFID 351..361
FT /evidence="ECO:0000250"
FT DISULFID 368..410
FT /evidence="ECO:0000250"
FT DISULFID 404..416
FT /evidence="ECO:0000250"
SQ SEQUENCE 423 AA; 46314 MW; 5FBA8B51AF8DB8B5 CRC64;
EQQKYLNARK YIELVIVADN VMVKKYTSNS TAIRTRIYSC VNTLNLIYSA FNTHIALTGV
EIWSNGDKIN VQSNSSVTLD FFGTWRETVL LNRKRHDNAQ LLTAIDLDGP TVGLAYVGSM
CNPKGSTGLI QDHNKLDVMV AITMAHELGH NLGMNHDGNQ CNCGGNPCIM SATLDFEPVY
QFSDCSRDQH WRYLIDNRPP CILNIPLRTD IVSPPVCGNY FVEVGEECDC GLPANCQNQC
CNAATCKLIP GAQCEDGECC ERCQFKGAGT ECRAARSECD IAESCTGQSP ECPTDDFQRN
GQPCLNNQGY CYNGNCPILD HQCHNLFGAG ATVAPNACFD FNRKGQGNSY CRKQNGVTIP
CARKDIKCGR LFCVQGPIGN TISCQSTSSQ DDPDIGMVDL GTKCGDGRVC NSNRECVDVT
TPY
