ID   DIDLB_ECHCA             Reviewed;          63 AA.
AC   P0C6B5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Disintegrin schistatin-like subunit B;
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 A; 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; B=1-63.
DR   PDBsum; 1TEJ; -.
DR   AlphaFoldDB; P0C6B5; -.
DR   SMR; P0C6B5; -.
DR   EvolutionaryTrace; P0C6B5; -.
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..63
FT                   /note="Disintegrin schistatin-like subunit B"
FT                   /id="PRO_0000319470"
FT   DOMAIN          1..63
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                   ECO:0000269|PubMed:16101289"
FT   DISULFID        7
FT                   /note="Interchain (with C-11 in subunit A)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:16101289"
FT   DISULFID        12
FT                   /note="Interchain (with C-6 in subunit A)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:16101289"
FT   DISULFID        20..26
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:16101289"
FT   DISULFID        25..50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:16101289"
FT   DISULFID        38..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:16101289"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:1TEJ"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:1TEJ"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:1TEJ"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1TEJ"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:1TEJ"
SQ   SEQUENCE   63 AA;  6961 MW;  15996A964A6A0CE0 CRC64;
     NSVNPCCDPQ TCKPIEGKHC ISGPCCENCY FLRSGTICQR ARGDGNNDYC TGITPDCPRN
     RYN