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Database: UniProt
Entry: P18618
LinkDB: P18618
Original site: P18618 
ID   VM2_BOTAT               Reviewed;          72 AA.
AC   P18618;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 2.
DT   22-FEB-2023, entry version 86.
DE   RecName: Full=Disintegrin batroxostatin;
DE   AltName: Full=Disintegrin colombistatin;
DE   AltName: Full=Platelet aggregation activation inhibitor;
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   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=18830584; DOI=10.1007/s00204-008-0358-y;
RA   Sanchez E.E., Rodriguez-Acosta A., Palomar R., Lucena S.E., Bashir S.,
RA   Soto J.G., Perez J.C.;
RT   "Colombistatin: a disintegrin isolated from the venom of the South American
RT   snake (Bothrops colombiensis) that effectively inhibits platelet
RT   aggregation and SK-Mel-28 cell adhesion.";
RL   Arch. Toxicol. 83:271-279(2009).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-71, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=2207176; DOI=10.1016/0167-4889(90)90096-v;
RA   Rucinski B., Niewiarowski S., Holt J.C., Soszka T., Knudsen K.A.;
RT   "Batroxostatin, an Arg-Gly-Asp-containing peptide from Bothrops atrox, is a
RT   potent inhibitor of platelet aggregation and cell interaction with
RT   fibronectin.";
RL   Biochim. Biophys. Acta 1054:257-262(1990).
CC   -!- FUNCTION: Inhibits fibrinogen interaction with platelets. Acts by
CC       binding to the glycoprotein IIb-IIIa receptor (ITGA2B/ITGB3) on the
CC       platelet surface and inhibits aggregation induced by ADP, thrombin,
CC       platelet-activating factor and collagen. Also inhibits T24 and SK-Mel-
CC       28 cell adhesion to fibronectin with IC(50) of 4.4 uM and 33 nM,
CC       respectively. {ECO:0000269|PubMed:18830584,
CC       ECO:0000269|PubMed:2207176}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18830584,
CC       ECO:0000269|PubMed:2207176}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:18830584, ECO:0000305|PubMed:2207176}.
CC   -!- MASS SPECTROMETRY: Mass=7778.65; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18830584};
CC   -!- MISCELLANEOUS: The name colombistatin has been given to this protein
CC       due to its source species B.colombiensis, which is a synonym of
CC       B.atrox.
CC   -!- MISCELLANEOUS: The disintegrin belongs to the medium disintegrin
CC       subfamily.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC       subfamily. P-IIa sub-subfamily. {ECO:0000305}.
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DR   PIR; S13168; S13168.
DR   AlphaFoldDB; P18618; -.
DR   SMR; P18618; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF32; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 28; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW   Secreted; Toxin.
FT   CHAIN           1..72
FT                   /note="Disintegrin batroxostatin"
FT                   /evidence="ECO:0000269|PubMed:18830584"
FT                   /id="PRO_0000101785"
FT   DOMAIN          1..72
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   REGION          52..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           51..53
FT                   /note="Cell attachment site"
FT   DISULFID        6..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        8..16
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        21..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        29..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        34..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        47..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   CONFLICT        10
FT                   /note="A -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   72 AA;  7736 MW;  85B0D18ED932A2DC CRC64;
     EAGEECDCGA PENPCCDAAT CKLRPGAQCA EGLCCDQCRF KGAGKICRRA RGDNPDDRCT
     GQSADCPRNR FY
//
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