VM23A_ECHCA
ID VM23A_ECHCA Reviewed; 67 AA.
AC P81630;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Disintegrin EC3A;
OS Echis carinatus (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=40353;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=10212222; DOI=10.1074/jbc.274.18.12468;
RA Marcinkiewicz C., Calvete J.J., Marcinkiewicz M.M., Raida M.,
RA Vijay-Kumar S., Huang Z., Lobb R.R., Niewiarowski S.;
RT "EC3, a novel heterodimeric disintegrin from Echis carinatus venom,
RT inhibits alpha4 and alpha5 integrins in an RGD-independent manner.";
RL J. Biol. Chem. 274:12468-12473(1999).
CC -!- FUNCTION: Inhibits adhesion of cells expressing alpha-4/beta-1
CC (ITGA4/ITGB1) and alpha-4/beta-7 (ITGA4/ITGB7) integrins to the natural
CC ligands vascular cell adhesion molecule 1 (VCAM-1) and mucosal
CC addressin cell adhesion molecule 1 (MADCAM-1). It is also a weaker
CC inhibitor of alpha-5/beta-1 (ITGA5/ITGB1) and alpha-2b/beta-3
CC (ITGA2B/ITGB3) integrins. The inhibitory activity of EC3 towards alpha-
CC 4 integrins is associated with the MLD sequence of EC3B subunit. The
CC ability of EC3 to inhibit ITGA5/ITGB1 resides in both subunits A and B.
CC {ECO:0000269|PubMed:10212222}.
CC -!- SUBUNIT: Heterodimer with EC3B; disulfide-linked.
CC {ECO:0000269|PubMed:10212222}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not inhibit alpha-V/beta-3 (ITGAV/ITGB3) integrin.
CC {ECO:0000305|PubMed:10212222}.
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}.
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; P81630; -.
DR SMR; P81630; -.
DR PRIDE; P81630; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; 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; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Secreted; Toxin.
FT CHAIN 1..67
FT /note="Disintegrin EC3A"
FT /id="PRO_0000101798"
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-12 in EC3B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 12
FT /note="Interchain (with C-7 in EC3B)"
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"
FT VARIANT 33
FT /note="R -> N"
FT VARIANT 37
FT /note="V -> I"
SQ SEQUENCE 67 AA; 7440 MW; 578C29A1D681CA3C CRC64;
NSVHPCCDPV KCEPREGEHC ISGPCCRNCY FLRAGTVCKR AVGDDVDDYC SGITPDCPRN
RYKGKED
