ID   DIDA_CERVI              Reviewed;         111 AA.
AC   Q3BK16;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Disintegrin CV-11-alpha;
DE            Short=CV11;
DE   Flags: Precursor;
OS   Cerastes vipera (Sahara sand viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Cerastes.
OX   NCBI_TaxID=8698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16411889; DOI=10.1042/bj20051678;
RA   Sanz L., Bazaa A., Marrakchi N., Perez A., Chenik M., Bel Lasfer Z.,
RA   El Ayeb M., Calvete J.J.;
RT   "Molecular cloning of disintegrins from Cerastes vipera and Macrovipera
RT   lebetina transmediterranea venom gland cDNA libraries: insight into the
RT   evolution of the snake venom integrin-inhibition system.";
RL   Biochem. J. 395:385-392(2006).
CC   -!- FUNCTION: Inhibits ADP-induced human platelet aggregation. Antagonist
CC       of alpha-IIb/beta-3 (ITGA2B/ITGB3) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with subunit beta; disulfide-linked.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AM114013; CAJ34937.1; -; mRNA.
DR   AlphaFoldDB; Q3BK16; -.
DR   SMR; Q3BK16; -.
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   2: Evidence at transcript level;
KW   Cell adhesion impairing toxin; Disulfide bond; Hemostasis impairing toxin;
KW   Platelet aggregation inhibiting toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..46
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000318184"
FT   CHAIN           47..111
FT                   /note="Disintegrin CV-11-alpha"
FT                   /id="PRO_5000076854"
FT   DOMAIN          47..111
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           89..91
FT                   /note="Cell attachment site"
FT   DISULFID        53..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        54
FT                   /note="Interchain (with C-7 in beta subunit)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        59
FT                   /note="Interchain (with C-12 in beta subunit)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        67..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        72..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        85..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   111 AA;  12098 MW;  DB50AEEA792680F5 CRC64;
     MIQVLLVIIC LAVFPYQGSS IILESGNVND FELVYPKKVT VLPTGAMNSA HPCCDPVTCK
     PKRGEHCISG PCCRNCKFLS PGTICKKAKG DDMNDYCTGI SSDCPRNPWK D