ID   DIRK_BUTOC              Reviewed;          17 AA.
AC   P0DQU8;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 1.
DT   03-AUG-2022, entry version 1.
DE   RecName: Full=RK peptide {ECO:0000303|PubMed:30287364};
DE   AltName: Full=Disintegrin-like peptide {ECO:0000303|PubMed:30287364};
OS   Buthus occitanus tunetanus (Common European scorpion) (Buthus tunetanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Buthus.
OX   NCBI_TaxID=6871;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SYNTHESIS, MASS SPECTROMETRY, DISULFIDE BOND,
RP   AND 3D-STRUCTURE MODELING.
RC   TISSUE=Venom;
RX   PubMed=30287364; DOI=10.1016/j.ijbiomac.2018.09.180;
RA   Khamessi O., Ben Mabrouk H., Othman H., ElFessi-Magouri R., De Waard M.,
RA   Hafedh M., Marrakchi N., Srairi-Abid N., Kharrat R.;
RT   "RK, the first scorpion peptide with dual disintegrin activity on
RT   alpha1/beta1 and alphav/beta3 integrins.";
RL   Int. J. Biol. Macromol. 120:1777-1788(2018).
CC   -!- FUNCTION: Venom protein with no toxicity on mice (ICV injection) and
CC       tumor cell lines. Inhibits the cell adhesion of three cell lines to
CC       fibrinogen, fibronectin and type IV collagen. Interacts with both
CC       alpha-1/beta-1 (ITGA1/ITGB1) and alpha-v/beta-3 (ITGAV/ITGB3) with a
CC       more pronounced effect for alpha-1/beta-1 (ITGA1/ITGB1).
CC       {ECO:0000269|PubMed:30287364}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30287364}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:30287364}.
CC   -!- MASS SPECTROMETRY: Mass=1780.03; Method=MALDI; Note=Average mass.;
CC       Evidence={ECO:0000269|PubMed:30287364};
CC   -!- SIMILARITY: Belongs to the disintegrin-like family. {ECO:0000305}.
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PE   1: Evidence at protein level;
KW   Cell adhesion impairing toxin; Direct protein sequencing; Disulfide bond;
KW   Secreted; Toxin.
FT   PEPTIDE         1..17
FT                   /note="RK peptide"
FT                   /evidence="ECO:0000269|PubMed:30287364"
FT                   /id="PRO_0000455820"
FT   MOTIF           11..13
FT                   /note="D/ECD-tripeptide"
FT                   /evidence="ECO:0000305|PubMed:30287364"
FT   DISULFID        3..12
FT                   /evidence="ECO:0000269|PubMed:30287364"
SQ   SEQUENCE   17 AA;  1782 MW;  97F3315CA4FD72DE CRC64;
     IDCGTVMIPS ECDPKSS