ID   VM2I_LACMU              Reviewed;          73 AA.
AC   P31990;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Disintegrin lachesin {ECO:0000303|PubMed:8419314};
DE   AltName: Full=Platelet aggregation activation inhibitor;
OS   Lachesis muta muta (Bushmaster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Lachesis.
OX   NCBI_TaxID=8753;
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}.
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DR   PIR; E43019; E43019.
DR   AlphaFoldDB; P31990; -.
DR   SMR; P31990; -.
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 lachesin"
FT                   /evidence="ECO:0000269|PubMed:8419314"
FT                   /id="PRO_0000101806"
FT   DOMAIN          1..73
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   REGION          51..73
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"
SQ   SEQUENCE   73 AA;  7765 MW;  9D1A173DFEDD3C0E CRC64;
     EAGEECDCGA PANPCCDAAT CKLRPGAQCA EGLCCDQCRF IKKGKICRRA RGDNPDDRCT
     GQSADCPRNG YYG