ID   DIS_ECHOC               Reviewed;         128 AA.
AC   Q3BER1;
DT   26-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 ocellatusin {ECO:0000303|PubMed:11852062, ECO:0000303|PubMed:16830094};
DE   AltName: Full=Short ocellatusion precursor Eo10c-10 {ECO:0000303|PubMed:16830094};
DE   Flags: Precursor;
OS   Echis ocellatus (Ocellated saw-scaled viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=99586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=16830094; DOI=10.1007/s00239-005-0269-y;
RA   Juarez P., Wagstaff S.C., Sanz L., Harrison R.A., Calvete J.J.;
RT   "Molecular cloning of Echis ocellatus disintegrins reveals non-venom-
RT   secreted proteins and a pathway for the evolution of ocellatusin.";
RL   J. Mol. Evol. 63:183-193(2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 66-115, FUNCTION, SUBUNIT, MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=11852062; DOI=10.1016/s0014-5793(02)02233-0;
RA   Smith J.B., Theakston R.D., Coelho A.L., Barja-Fidalgo C., Calvete J.J.,
RA   Marcinkiewicz C.;
RT   "Characterization of a monomeric disintegrin, ocellatusin, present in the
RT   venom of the Nigerian carpet viper, Echis ocellatus.";
RL   FEBS Lett. 512:111-115(2002).
CC   -!- FUNCTION: The disintegrin ocellatusin-10c1 is a poor inhibitor of
CC       platelet aggregation. The disintegrin inhibits the adhesion of cells
CC       expressing the RGD-dependent integrin alpha-5/beta-1 (ITGA5/ITGB1) to
CC       immobilized fibronectin. Inhibition on alpha-2b/beta-3 (ITGA2B/ITGB3)
CC       is low, and there is no inhibition on alpha-1/beta-1 (ITGA1/ITGB1),
CC       alpha-2/beta-1 (ITGA2/ITGB1) and alpha-6/beta-1 (ITGA6/ITGB1) (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: The short monomeric disintegrin ocellatusin inhibits ADP-
CC       induced platelet aggregation (IC(50)=168 nM). Inhibits alpha-5/beta-1
CC       (ITGA5/ITGB1) integrin and induces the expression of a ligand-induced
CC       binding site epitope on beta-1 integrin subunit. Has a direct
CC       chemotactic stimulus on human neutrophils in vitro.
CC       {ECO:0000269|PubMed:11852062}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11852062}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11852062}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:11852062}.
CC   -!- MASS SPECTROMETRY: Mass=5598; Mass_error=2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:11852062};
CC   -!- SIMILARITY: Belongs to the disintegrin family. Short disintegrin
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: The disintegrin is also encoded by another precursor (AC
CC       Q14FJ4). {ECO:0000305}.
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DR   EMBL; AM117392; CAJ40969.1; -; mRNA.
DR   AlphaFoldDB; Q3BER1; -.
DR   SMR; Q3BER1; -.
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   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; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..65
FT                   /evidence="ECO:0000269|PubMed:11852062"
FT                   /id="PRO_0000319042"
FT   CHAIN           66..115
FT                   /note="Disintegrin ocellatusin"
FT                   /id="PRO_5000076912"
FT   PROPEP          116..128
FT                   /id="PRO_0000319043"
FT   DOMAIN          26..112
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           89..91
FT                   /note="Cell attachment site"
FT   DISULFID        53..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        67..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        72..97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        73..102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        85..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   CONFLICT        115
FT                   /note="P -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   128 AA;  14076 MW;  0BE6AB6E856A0C68 CRC64;
     MIPVLLVTIC LAVFPFQGSS IILESGNIND YEIVYPKKVA VLPTGAMNSA HPCYDPVTCQ
     PKEKEDCESG PCCDNCKFLK EGTICKMARG DNMHDYCNGK TCDCPRNPYK GEHDPMEWPA
     PAKGSVLM