DID5B_ECHOC
ID DID5B_ECHOC Reviewed; 66 AA.
AC P0C6A4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Disintegrin EO5B;
DE AltName: Full=EO4B;
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 PROTEIN SEQUENCE, 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. When it dimerizes
CC with EO4A, it inhibits the adhesion of cells expressing the RGD-
CC dependent integrin alpha-5/beta-1 (ITGA5/ITGB1) to immobilized
CC fibronectin. When it dimerizes with EO5A, it inhibits the adhesion of
CC the alpha-4/beta-1 (ITGA4/ITGB1) integrin to VCAM-1. When it dimerizes
CC either with EO4A or EO5A, the inhibition on alpha-IIb/beta-3
CC (ITGA2B/ITGB3) is low. {ECO:0000269|PubMed:12667142}.
CC -!- SUBUNIT: Heterodimer with EO4A or EO5A; 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: When it dimerizes either with EO4A or EO5A, there is no
CC inhibition on alpha-1/beta-1 (ITGA1/ITGB1), alpha-2/beta-1
CC (ITGA2/ITGB1) and alpha-6/beta-1 (ITGA6/ITGB1).
CC {ECO:0000305|PubMed:12667142}.
CC -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P0C6A4; -.
DR SMR; P0C6A4; -.
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; Toxin.
FT CHAIN 1..66
FT /note="Disintegrin EO5B"
FT /id="PRO_0000319019"
FT DOMAIN 1..65
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 42..44
FT /note="Cell attachment site; atypical (VGD)"
FT DISULFID 6..29
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 7
FT /note="Interchain (with C-54 in EO5A)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 12
FT /note="Interchain (with C-59 in EO5A)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 20..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 25..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 38..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 66 AA; 7142 MW; 406B70045088CC67 CRC64;
NSAHPCCDPV TCQPKKGEHC ISGPCCRNCK FLNSGTVCKR AVGDDMDDYC SGITTDCPRN
PYKGKD
