ID   VM2EG_ECHPL             Reviewed;          49 AA.
AC   Q7LZK0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Disintegrin echistatin-gamma;
OS   Echis pyramidum leakeyi (Leakey's carpet viper) (Echis carinatus leakeyi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX   NCBI_TaxID=38415;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Venom;
RX   PubMed=7832768; DOI=10.1042/bj3050513;
RA   Chen Y.-L., Huang T.-F., Chen S.-W., Tsai I.-H.;
RT   "Determination of the structure of two novel echistatin variants and
RT   comparison of the ability of echistatin variants to inhibit aggregation of
RT   platelets from different species.";
RL   Biochem. J. 305:513-520(1995).
CC   -!- FUNCTION: Has antiplatelet activities on guinea pig, followed by human,
CC       rabbit and rat platelet-rich plasma. {ECO:0000269|PubMed:7832768}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7832768}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:7832768}.
CC   -!- MISCELLANEOUS: The disintegrin belongs to the short disintegrin
CC       subfamily.
CC   -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC       subfamily. P-IIa 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   PIR; S53432; S53432.
DR   AlphaFoldDB; Q7LZK0; -.
DR   SMR; Q7LZK0; -.
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   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   Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW   Secreted; Toxin.
FT   CHAIN           1..49
FT                   /note="Disintegrin echistatin-gamma"
FT                   /id="PRO_0000329976"
FT   DOMAIN          1..47
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           24..26
FT                   /note="Cell attachment site"
FT   DISULFID        2..11
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        7..32
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        8..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   DISULFID        20..39
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
SQ   SEQUENCE   49 AA;  5441 MW;  0DAF330F593BA9D4 CRC64;
     DCASGPCCRD CKFLEEGTIC NMARGDDMDD YCNGKTCDCP RNPHKWPAP