VM2I_CROBA
ID VM2I_CROBA Reviewed; 72 AA.
AC P31981;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Disintegrin basilicin {ECO:0000303|PubMed:8419314};
DE AltName: Full=Basicilin {ECO:0000305};
DE AltName: Full=Platelet aggregation activation inhibitor;
OS Crotalus basiliscus (Mexican west-coast rattlesnake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX NCBI_TaxID=8744;
RN [1]
RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8419314; DOI=10.1016/s0021-9258(18)54041-2;
RA Scarborough R.M., Rose J.W., Naughton M.A., Phillips D.R., Nannizzi L.,
RA Arfsten A., Campbell A.M., Charo I.F.;
RT "Characterization of the integrin specificities of disintegrins isolated
RT from American pit viper venoms.";
RL J. Biol. Chem. 268:1058-1065(1993).
CC -!- FUNCTION: Inhibits fibrinogen interaction with platelets. Acts by
CC binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and
CC inhibits aggregation induced by ADP, thrombin, platelet-activating
CC factor and collagen.
CC -!- SUBUNIT: Monomer (disintegrin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8419314}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:8419314}.
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}.
CC -!- CAUTION: The term basicilin was erroneously reported in a review. Since
CC such a letter reversal is relatively common, we thought it would be
CC appropriate to indicate it here to facilitate the search for this
CC protein. {ECO:0000305}.
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DR PIR; I43019; I43019.
DR AlphaFoldDB; P31981; -.
DR SMR; P31981; -.
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..72
FT /note="Disintegrin basilicin"
FT /evidence="ECO:0000269|PubMed:8419314"
FT /id="PRO_0000101791"
FT DOMAIN 1..72
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 50..52
FT /note="Cell attachment site"
FT DISULFID 5..14
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 7..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 20..34
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 28..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 33..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 46..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 72 AA; 7704 MW; D584BC894ACC3C1C CRC64;
AGEECDCGSP ANPCCDAATC KLRPGAQCAE GLCCDQCRFI KKGKICRRAR GDNPDDRCTG
QSADCPRNHF HA
