ID   DIS_CERVI               Reviewed;          43 AA.
AC   Q3BK17;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Disintegrin CV;
DE   AltName: Full=Disintegrin CV-short;
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: Specifically interacts with the alpha-1/beta-1 integrin
CC       (ITGA1/ITGB1). Exhibits highly inhibitory effects on cell adhesion and
CC       cell migration to collagens I and IV. Also shows in vivo anti-
CC       angiogenic activity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the disintegrin family. Short disintegrin
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AM114012; CAJ34936.1; -; mRNA.
DR   AlphaFoldDB; Q3BK17; -.
DR   BMRB; Q3BK17; -.
DR   SMR; Q3BK17; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SUPFAM; SSF57552; SSF57552; 1.
PE   2: Evidence at transcript level;
KW   Angiogenesis; Cell adhesion impairing toxin; Developmental protein;
KW   Differentiation; Disulfide bond; Secreted; Toxin.
FT   CHAIN           1..43
FT                   /note="Disintegrin CV"
FT                   /id="PRO_5000076853"
FT   DOMAIN          1..43
FT                   /note="Disintegrin"
FT   MOTIF           21..23
FT                   /note="Cell attachment site; atypical (RTS)"
FT   DISULFID        1..10
FT                   /evidence="ECO:0000250"
FT   DISULFID        6..29
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..34
FT                   /evidence="ECO:0000250"
FT   DISULFID        19..36
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   43 AA;  4588 MW;  5869298E900CBC3A CRC64;
     CTTGPCCRQC KLKPAGTTCW RTSVSSHYCT GRSCECPSYP GNG