ID   DIDS_ECHCA              Reviewed;          64 AA.
AC   P83658;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Disintegrin schistatin;
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 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DISULFIDE BONDS.
RC   TISSUE=Venom {ECO:0000305};
RA   Bilgrami S., Jabeen T., Kumar J., Yadav S., Sharma S., Kaur P., Singh T.P.;
RL   Submitted (SEP-2003) to UniProtKB.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-19, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC   TISSUE=Venom {ECO:0000269|PubMed:11679739};
RX   PubMed=11679739; DOI=10.1107/s0907444901012082;
RA   Tomar S., Yadav S., Chandra V., Kumar P., Singh T.P.;
RT   "Purification, crystallization and preliminary X-ray diffraction studies of
RT   disintegrin (schistatin) from saw-scaled viper (Echis carinatus).";
RL   Acta Crystallogr. D 57:1669-1670(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=15317139; DOI=10.1016/j.jmb.2004.06.048;
RA   Bilgrami S., Tomar S., Yadav S., Kaur P., Kumar J., Jabeen T., Sharma S.,
RA   Singh T.P.;
RT   "Crystal structure of schistatin, a disintegrin homodimer from saw-scaled
RT   viper (Echis carinatus) at 2.5 A resolution.";
RL   J. Mol. Biol. 341:829-837(2004).
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   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:15317139,
CC       ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1, ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.1,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin
CC       subfamily. {ECO:0000305}.
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DR   PDB; 1RMR; X-ray; 2.50 A; A=1-64.
DR   PDBsum; 1RMR; -.
DR   AlphaFoldDB; P83658; -.
DR   SMR; P83658; -.
DR   EvolutionaryTrace; P83658; -.
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..64
FT                   /note="Disintegrin schistatin"
FT                   /id="PRO_0000101800"
FT   DOMAIN          1..64
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:0000305"
FT   DISULFID        7
FT                   /note="Interchain (with C-12)"
FT   DISULFID        12
FT                   /note="Interchain (with C-7)"
FT   DISULFID        20..26
FT                   /evidence="ECO:0000305"
FT   DISULFID        25..50
FT                   /evidence="ECO:0000305"
FT   DISULFID        38..57
FT                   /evidence="ECO:0000305"
FT   CONFLICT        8
FT                   /note="D -> P (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:1RMR"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:1RMR"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1RMR"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:1RMR"
SQ   SEQUENCE   64 AA;  7083 MW;  FD0CA30A2048EE51 CRC64;
     NSVHPCCDPV ICEPREGEHC ISGPCCENCY FLNSGTICKR ARGDGNQDYC TGITPDCPRN
     RYNV