DID5A_ECHOC
ID DID5A_ECHOC Reviewed; 115 AA.
AC Q3BER4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Disintegrin EO5A;
DE AltName: Full=Eo-12;
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 48-114, 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 the alpha-4/beta-1 (ITGA4/ITGB1) integrin to
CC VCAM-1. Inhibition on alpha-IIb/beta-3 (ITGA2B/ITGB3) is low.
CC {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 show inhibition of inhibition on alpha-1/beta-1
CC (ITGA1/ITGB1), alpha-2/beta-1 (ITGA2/ITGB1) and alpha-6/beta-1
CC (ITGA6/ITGB1). {ECO:0000305|PubMed:12667142}.
CC -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC subfamily. {ECO:0000305}.
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DR EMBL; AM117389; CAJ40966.1; -; mRNA.
DR AlphaFoldDB; Q3BER4; -.
DR SMR; Q3BER4; -.
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_0000319018"
FT CHAIN 48..115
FT /note="Disintegrin EO5A"
FT /id="PRO_5000076909"
FT DOMAIN 26..112
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 89..91
FT /note="Cell attachment site; atypical (MLD)"
FT DISULFID 53..76
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 54
FT /note="Interchain (with C-7 in EO5B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 59
FT /note="Interchain (with C-12 in EO5B)"
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 63
FT /note="Q -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="P -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="G -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 115 AA; 12447 MW; 30A5A274F33EA5BD CRC64;
MIPVLLVTIC LAVFPFQGSS IILESGNIND YEIVYPKKVA VLPTGAMNSA HPCCDPVTCQ
PKQGEHCISG PCCRNCKFLN SGTICKKTML DGLNDYCTGV TSDCPRNPYK GKEDD
