DIDBA_ECHML
ID DIDBA_ECHML Reviewed; 68 AA.
AC P0C6A3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Disintegrin EMS11A;
OS Echis multisquamatus (Central Asian sand viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX NCBI_TaxID=93050;
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. The disintegrin
CC inhibits the adhesion of both the alpha-4/beta-1 (ITGA4/ITGB1) and the
CC alpha-5/beta-1 (ITGA5/ITGB1) integrins to VCAM-1 and fibronectin
CC respectively with almost the same degree of specificity. Inhibition on
CC alpha-IIb/beta-3 (ITGA2B/ITGB3) is low. {ECO:0000269|PubMed:12667142}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked. {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).
CC {ECO:0000305|PubMed:12667142}.
CC -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0C6A3; -.
DR SMR; P0C6A3; -.
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..68
FT /note="Disintegrin EMS11A"
FT /id="PRO_0000319013"
FT DOMAIN 1..65
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 42..44
FT /note="Cell attachment site; atypical (MLD)"
FT DISULFID 6..29
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 7
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 12
FT /note="Interchain"
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 68 AA; 7469 MW; 15B4B9724852F550 CRC64;
NSAHPCCDPV KCEPREGEHC ISGPCCRNCK FLNAGTICKK AMLDGLNDYC TGISSDCPRN
RYKGKEDD
