ID   DID1_ECHOC              Reviewed;         111 AA.
AC   Q3BER2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Disintegrin Eo1 subunit 1;
DE            Short=Eo1-1;
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).
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-IIb/beta-3 (ITGA2B/ITGB3) is low (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC       subfamily. {ECO:0000305}.
CC   -!- CAUTION: This protein has not been reported as being secreted in the
CC       venom. {ECO:0000305}.
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DR   EMBL; AM117391; CAJ40968.1; -; mRNA.
DR   AlphaFoldDB; Q3BER2; -.
DR   SMR; Q3BER2; -.
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; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..46
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000319014"
FT   CHAIN           47..109
FT                   /note="Disintegrin Eo1 subunit 1"
FT                   /id="PRO_5000076911"
FT   PROPEP          110..111
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000319015"
FT   DOMAIN          26..111
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           89..91
FT                   /note="Cell attachment site; atypical (WGD)"
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"
SQ   SEQUENCE   111 AA;  12186 MW;  0E49AEEA79350942 CRC64;
     MIQVLLVIIC LAVFPYQGSS IILESGNVND FELVYPKKVT VLPTGAMNSA HPCCDPVMCK
     PKRGEHCISG PCCRNCKFLS PGTICKKAWG DDMNDYCTGI SSDCPRNPWK D