ID   VM26B_ECHCS             Reviewed;          69 AA.
AC   P82466;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2000, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Disintegrin EC6 subunit beta;
DE            Short=EC6B;
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   PROTEIN SEQUENCE, FUNCTION, AND 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 alpha; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC       subfamily.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC       subfamily. P-IIe sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P82466; -.
DR   SMR; P82466; -.
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; Toxin.
FT   CHAIN           1..69
FT                   /note="Disintegrin EC6 subunit beta"
FT                   /id="PRO_0000101802"
FT   DOMAIN          1..65
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           42..44
FT                   /note="Cell attachment site"
FT   DISULFID        6..29
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        7
FT                   /note="Interchain (with C-59 in subunit alpha)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        12
FT                   /note="Interchain (with C-54 in subunit alpha)"
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   69 AA;  7279 MW;  6916F2CA0821E1E8 CRC64;
     NSVHPCCDPV TCKPKRGKHC ASGPCCENCY IVGVGTVCNP ARGDWNDDNC TGVSSDCPPN
     PWNGKPSDN