DIDLA_ECHCA
ID DIDLA_ECHCA Reviewed; 62 AA.
AC P0C6B4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Disintegrin schistatin-like subunit A;
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, SUBUNIT, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND
RP DISULFIDE BONDS.
RC TISSUE=Venom;
RX PubMed=16101289; DOI=10.1021/bi050849y;
RA Bilgrami S., Yadav S., Kaur P., Sharma S., Perbandt M., Betzel C.,
RA Singh T.P.;
RT "Crystal structure of the disintegrin heterodimer from saw-scaled viper
RT (Echis carinatus) at 1.9 A resolution.";
RL Biochemistry 44:11058-11066(2005).
CC -!- FUNCTION: May bind to both alpha-IIb/beta-3 (ITGA2B/ITGB3) and alpha-
CC V/beta-3 (ITGAV/ITGB3) integrins, and may inhibit platelet aggregation.
CC {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with subunit B; disulfide-linked.
CC {ECO:0000269|PubMed:16101289}.
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 PDB; 1TEJ; X-ray; 1.90 A; A=1-62.
DR PDBsum; 1TEJ; -.
DR AlphaFoldDB; P0C6B4; -.
DR SMR; P0C6B4; -.
DR EvolutionaryTrace; P0C6B4; -.
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 3D-structure; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Hemostasis impairing toxin;
KW Platelet aggregation inhibiting toxin; Secreted; Toxin.
FT CHAIN 1..62
FT /note="Disintegrin schistatin-like subunit A"
FT /id="PRO_0000319469"
FT DOMAIN 1..62
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 41..43
FT /note="Cell attachment site"
FT DISULFID 5..28
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:16101289"
FT DISULFID 6
FT /note="Interchain (with C-12 in subunit B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:16101289"
FT DISULFID 11
FT /note="Interchain (with C-7 in subunit B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:16101289"
FT DISULFID 19..25
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:16101289"
FT DISULFID 24..49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:16101289"
FT DISULFID 37..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000269|PubMed:16101289"
FT TURN 8..11
FT /evidence="ECO:0007829|PDB:1TEJ"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1TEJ"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1TEJ"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1TEJ"
SQ SEQUENCE 62 AA; 6795 MW; 56078548214143F1 CRC64;
SVNPCCDPVI CKPRDGEHCI SGPCCNNCKF LNSGTICQRA RGDGNHDYCT GITTDCPRNR
YN
