VM2I_SISMB
ID VM2I_SISMB Reviewed; 73 AA.
AC P22827;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Disintegrin barbourin;
DE AltName: Full=Platelet aggregation activation inhibitor;
OS Sistrurus miliarius barbouri (Dusky pigmy rattlesnake) (Sistrurus
OS barbouri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Sistrurus.
OX NCBI_TaxID=8759;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Venom;
RX PubMed=2033037; DOI=10.1016/s0021-9258(18)92826-7;
RA Scarborough R.M., Rose J.W., Hsu M.A., Phillips D.R., Fried V.A.,
RA Campbell A.M., Nannizzi L., Charo I.F.;
RT "Barbourin. A GPIIb-IIIa-specific integrin antagonist from the venom of
RT Sistrurus m. barbouri.";
RL J. Biol. Chem. 266:9359-9362(1991).
RN [2]
RP REVIEW.
RX PubMed=21447352; DOI=10.1016/j.toxicon.2011.03.017;
RA Koh C.Y., Kini R.M.;
RT "From snake venom toxins to therapeutics - Cardiovascular examples.";
RL Toxicon 59:497-506(2012).
CC -!- FUNCTION: Inhibitor of ligand binding to the integrins alpha-IIb/beta-3
CC (ITGA2B/ITGB3). Competition with fibrinogen for the RGD recognition
CC sites on the alpha-IIb/beta-3 integrin results in the inhibition of
CC platelet aggregation induced by ADP, thrombin, platelet-activating
CC factor and collagen.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: This peptide has served as a model to produce
CC eptifibatide (Integrilin), a cyclic heptapeptide available in the
CC market as antiplatelet agent. {ECO:0000305|PubMed:21447352}.
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; A40003; A40003.
DR AlphaFoldDB; P22827; -.
DR SMR; P22827; -.
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; -; 1.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR Pfam; PF00200; Disintegrin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 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..73
FT /note="Disintegrin barbourin"
FT /id="PRO_0000101807"
FT DOMAIN 1..73
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 51..53
FT /note="Cell attachment site; atypical (KGD)"
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"
SQ SEQUENCE 73 AA; 7701 MW; D370EB1F2322C5AC CRC64;
EAGEECDCGS PENPCCDAAT CKLRPGAQCA DGLCCDQCRF MKKGTVCRVA KGDWNDDTCT
GQSADCPRNG LYG
