ID   DID4A_ECHOC             Reviewed;         128 AA.
AC   Q3BER3; Q3BER5; Q3BER6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Disintegrin EO4A;
DE   AltName: Full=Dim-3 SP6;
DE   AltName: Full=Eo-10;
DE   AltName: Full=Eo-10c1;
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 48-115, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=12667142; DOI=10.1042/bj20021739;
RA   Calvete J.J., Moreno-Murciano M.P., Theakston R.D.G., Kisiel D.G.,
RA   Marcinkiewicz C.;
RT   "Snake venom disintegrins: novel dimeric disintegrins and structural
RT   diversification by disulphide bond engineering.";
RL   Biochem. J. 372:725-734(2003).
CC   -!- FUNCTION: Poor inhibitor of platelet aggregation. The disintegrin
CC       inhibits the adhesion of cells expressing the RGD-dependent integrin
CC       alpha-5/beta-1 (ITGA5/ITGB1) to immobilized fibronectin. Inhibition on
CC       alpha-2b/beta-3 (ITGA2B/ITGB3) is low. {ECO:0000269|PubMed:12667142}.
CC   -!- SUBUNIT: Heterodimer with EO5B; disulfide-linked.
CC       {ECO:0000269|PubMed:12667142}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12667142}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: Does not inhibit alpha-1/beta-1 (ITGA1/ITGB1), alpha-
CC       2/beta-1 (ITGA2/ITGB1) and alpha-6/beta-1 (ITGA6/ITGB1) integrins.
CC       {ECO:0000305|PubMed:12667142}.
CC   -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AM117387; CAJ40964.1; -; mRNA.
DR   EMBL; AM117388; CAJ40965.1; -; mRNA.
DR   EMBL; AM117390; CAJ40967.1; -; mRNA.
DR   AlphaFoldDB; Q3BER3; -.
DR   SMR; Q3BER3; -.
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..47
FT                   /evidence="ECO:0000269|PubMed:12667142"
FT                   /id="PRO_0000319016"
FT   CHAIN           48..114
FT                   /note="Disintegrin EO4A"
FT                   /id="PRO_5000076907"
FT   PROPEP          115..128
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000319017"
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..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        54
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        59
FT                   /note="Interchain"
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"
FT   CONFLICT        89
FT                   /note="R -> K (in Ref. 1; CAJ40967)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="H -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="S -> P (in Ref. 1; CAJ40965)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111..115
FT                   /note="GKYDP -> SEEED (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   128 AA;  13925 MW;  D12BF9AE8EA540DD CRC64;
     MIPVLLVTIC LAVFPFQGSS IILESGNIND YEIVYPKKVN VLPTGAMNSA HPCCDPVTCQ
     PKQGEHCISG PCCRNCKFLN SGTICKRARG DNLHDYCTGI SSDCPRNPYK GKYDPMKWPA
     AAKGSVLM