ID   VM2_CRORU               Reviewed;          61 AA.
AC   H9M5U4;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Disintegrin rubistatin;
DE   Flags: Fragment;
OS   Crotalus ruber ruber (Red diamond rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION OF RECOMBINANT PROTEIN.
RC   TISSUE=Venom gland;
RX   PubMed=22192732; DOI=10.1016/j.toxicon.2011.12.002;
RA   Carey C.M., Bueno R., Gutierrez D.A., Petro C., Lucena S.E., Sanchez E.E.,
RA   Soto J.G.;
RT   "Recombinant rubistatin (r-Rub), an MVD disintegrin, inhibits cell
RT   migration and proliferation, and is a strong apoptotic inducer of the human
RT   melanoma cell line SK-Mel-28.";
RL   Toxicon 59:241-248(2012).
CC   -!- FUNCTION: Recombinant disintegrin rubistatin inhibits ADP-induced
CC       platelet aggregation. In addition, it strongly induces apoptosis, and
CC       inhibits cell migration and proliferation of the human cancer cell line
CC       SK-Mel-28. {ECO:0000269|PubMed:22192732}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not induce chromatin fragmentation (apoptosis) in
CC       T24 and HeLa cells. {ECO:0000305|PubMed:22192732}.
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   EMBL; JN227479; AER36087.1; -; mRNA.
DR   AlphaFoldDB; H9M5U4; -.
DR   SMR; H9M5U4; -.
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; Toxin.
FT   CHAIN           <1..61
FT                   /note="Disintegrin rubistatin"
FT                   /id="PRO_0000424616"
FT   DOMAIN          <1..61
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           39..41
FT                   /note="Cell attachment site; atypical (MVD)"
FT   DISULFID        ?..3
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        ?..4
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        9..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        17..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        22..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        35..54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   NON_TER         1
SQ   SEQUENCE   61 AA;  6558 MW;  37B421D6B0C7C8DC CRC64;
     NPCCDAATCK MRPGSQCAEG LCCDQCRFMK KGTVCRVSMV DRNDDTCTGL SADCPRNGLY
     G