VM33_BOTAT
ID VM33_BOTAT Reviewed; 414 AA.
AC C5H5D4;
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-3;
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;
DE Flags: Fragment;
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; EU733641; ACI02289.1; -; mRNA.
DR AlphaFoldDB; C5H5D4; -.
DR SMR; C5H5D4; -.
DR MEROPS; M12.315; -.
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..>414
FT /note="Zinc metalloproteinase-disintegrin-like
FT batroxstatin-3"
FT /id="PRO_0000418200"
FT DOMAIN 10..204
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 212..298
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 276..278
FT /note="D/ECD-tripeptide"
FT ACT_SITE 147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
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 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..199
FT /evidence="ECO:0000250"
FT DISULFID 161..183
FT /evidence="ECO:0000250"
FT DISULFID 163..168
FT /evidence="ECO:0000250"
FT DISULFID 215..244
FT /evidence="ECO:0000250"
FT DISULFID 226..239
FT /evidence="ECO:0000250"
FT DISULFID 228..234
FT /evidence="ECO:0000250"
FT DISULFID 238..261
FT /evidence="ECO:0000250"
FT DISULFID 252..258
FT /evidence="ECO:0000250"
FT DISULFID 257..283
FT /evidence="ECO:0000250"
FT DISULFID 270..290
FT /evidence="ECO:0000250"
FT DISULFID 277..309
FT /evidence="ECO:0000250"
FT DISULFID 302..314
FT /evidence="ECO:0000250"
FT DISULFID 321..371
FT /evidence="ECO:0000250"
FT DISULFID 336..381
FT /evidence="ECO:0000250"
FT DISULFID 349..359
FT /evidence="ECO:0000250"
FT DISULFID 366..403
FT /evidence="ECO:0000250"
FT DISULFID 397..408
FT /evidence="ECO:0000250"
FT NON_TER 414
SQ SEQUENCE 414 AA; 46285 MW; 31504D57629979AF CRC64;
EQQRYLNATK YIKLVIVADN VMVRKYTHNL IDIRKRIFEI VNILSLIYLS MNINVALVGV
DIWTNGDKIN VTSAVEPTLA SFGTWRERDL LNRKTHDNAQ LLTGINLNGD TVGYAYIGSM
CMPKQSVGIV QDHGKTYHLV AVTMAHELGH NLGMDHDRDS CTCLANSCIM SATISPSYQF
SDCSQNDHLR YLISHTPQCI LNEPLRTDIV SPEVCGNYLL EEGEECDCGP LWNCQNPCCN
AATCKLTPGA QCAEGLCCYQ CRFIKAGNVC RPPRSECDIA ESCTGQSAHC PTDRFHRNGQ
PCLNNHGYCY NGNCPIMLYQ CIALFGAGTT VAEDVCFNYN LDGQGFFYCR RENDRIFPCA
KEDVKCGRLY CKVYNDNVHP CRYQYLDNGM VDHGTKCAVG KVCSNRQCVD VNTP
