ID   VM2MU_ECHML             Reviewed;          52 AA.
AC   P0C6R5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Disintegrin multisquamatin;
OS   Echis multisquamatus (Central Asian sand viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=93050;
RN   [1]
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=11275562; DOI=10.1093/oxfordjournals.jbchem.a002898;
RA   Okuda D., Nozaki C., Sekiya F., Morita T.;
RT   "Comparative biochemistry of disintegrins isolated from snake venom:
RT   consideration of the taxonomy and geographical distribution of snakes in
RT   the genus Echis.";
RL   J. Biochem. 129:615-620(2001).
RN   [2]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=8178312; DOI=10.1016/0049-3848(94)90052-3;
RA   Trikha M., Rote W.E., Manley P.J., Lucchesi B.R., Markland F.S.;
RT   "Purification and characterization of platelet aggregation inhibitors from
RT   snake venoms.";
RL   Thromb. Res. 73:39-52(1994).
CC   -!- FUNCTION: Inhibits ADP-induced human, canine and rabbit platelet
CC       aggregation by binding with high affinity to alpha-IIb/beta-3
CC       (ITGA2B/ITGB3). {ECO:0000269|PubMed:11275562,
CC       ECO:0000269|PubMed:8178312}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: The disintegrin belongs to the short 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   AlphaFoldDB; P0C6R5; -.
DR   BMRB; P0C6R5; -.
DR   SMR; P0C6R5; -.
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   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..52
FT                   /note="Disintegrin multisquamatin"
FT                   /id="PRO_0000326265"
FT   DOMAIN          1..50
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           27..29
FT                   /note="Cell attachment site"
FT   DISULFID        5..14
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        10..35
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        11..40
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        23..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   52 AA;  5740 MW;  1FCDBD382660682F CRC64;
     EGEECESGPC CRNCKFLKEG TICKRARGDD MDDYCNGKTC DCPRNPHKGP AT