ID   DID6A_ECHCS             Reviewed;         115 AA.
AC   P82465; E9JGH5;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 2.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Disintegrin EC6 subunit alpha;
DE            Short=EC6A;
DE   Flags: Precursor;
OS   Echis carinatus sochureki (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=124223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=21062752; DOI=10.1093/molbev/msq302;
RA   Casewell N.R., Wagstaff S.C., Harrison R.A., Wuster W.;
RT   "Gene tree parsimony of multilocus snake venom protein families reveals
RT   species tree conflict as a result of multiple parallel gene loss.";
RL   Mol. Biol. Evol. 28:1157-1172(2011).
RN   [2]
RP   PROTEIN SEQUENCE OF 48-115, FUNCTION, MOTIF MET-89--91-ASP, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=10926928; DOI=10.1074/jbc.m003209200;
RA   Marcinkiewicz C., Taooka Y., Yokosaki Y., Calvete J.J., Marcinkiewicz M.M.,
RA   Lobb R.R., Niewiarowski S., Sheppard D.;
RT   "Inhibitory effects of MLDG-containing heterodimeric disintegrins reveal
RT   distinct structural requirements for interaction of the integrin alpha
RT   9beta 1 with VCAM-1, tenascin-C, and osteopontin.";
RL   J. Biol. Chem. 275:31930-31937(2000).
CC   -!- FUNCTION: Potently inhibits adhesion of alpha-4/beta-1 (ITGA4/ITGB1)
CC       and alpha-9/beta-1 (ITGA9/ITGB1) integrins to VCAM1, and adhesion of
CC       alpha-5/beta-1 (ITGA5/ITGB1) integrin to fibronectin. Has a much less
CC       effect on alpha-IIb/beta-3 (ITGA2B/ITGB3) integrin. Also potently
CC       inhibits neutrophil migration across TNF-alpha-activated human
CC       umbilical endothelial cells. {ECO:0000269|PubMed:10926928}.
CC   -!- SUBUNIT: Heterodimer with subunit beta; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC       subfamily. {ECO:0000305}.
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DR   EMBL; GU012272; ADI47726.1; -; mRNA.
DR   AlphaFoldDB; P82465; -.
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   Secreted; Signal; Toxin.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..47
FT                   /evidence="ECO:0000269|PubMed:10926928"
FT                   /id="PRO_0000423376"
FT   CHAIN           48..115
FT                   /note="Disintegrin EC6 subunit alpha"
FT                   /id="PRO_0000101801"
FT   DOMAIN          48..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-12 in subunit beta)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        59
FT                   /note="Interchain (with C-7 in subunit beta)"
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   115 AA;  12578 MW;  B827670DD93D70A9 CRC64;
     MIQVLLVIIC LAVFPYQGSS IILESGNIND YEIVYPKKVA VLPTGAMNSV HPCCDPVTCE
     PREGEHCISG PCCRNCKFLN AGTICKKAML DGLNDYCTGI SSDCPRNRYK GKEDD