ID   VM2TI_ERIMA             Reviewed;          51 AA.
AC   P22826;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Disintegrin eristicophin {ECO:0000303|PubMed:2033037};
DE   AltName: Full=Platelet aggregation activation inhibitor;
OS   Eristicophis macmahoni (Leaf-nosed viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Eristicophis.
OX   NCBI_TaxID=110227;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, PYROGLUTAMATE FORMATION AT GLN-1, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=2033037; DOI=10.1016/s0021-9258(18)92826-7;
RA   Scarborough R.M., Rose J.W., Hsu M.A., Phillips D.R., Fried V.A.,
RA   Campbell A.M., Nannizzi L., Charo I.F.;
RT   "Barbourin. A GPIIb-IIIa-specific integrin antagonist from the venom of
RT   Sistrurus m. barbouri.";
RL   J. Biol. Chem. 266:9359-9362(1991).
CC   -!- FUNCTION: Inhibits fibrinogen interaction with platelets. Acts by
CC       binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) on the platelet surface and
CC       inhibits aggregation induced by ADP, thrombin, platelet-activating
CC       factor and collagen. {ECO:0000269|PubMed:2033037}.
CC   -!- SUBUNIT: Monomer (disintegrin). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2033037}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:2033037}.
CC   -!- MISCELLANEOUS: The disintegrin belongs to the short disintegrin
CC       subfamily. {ECO:0000305}.
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; C40003; C40003.
DR   AlphaFoldDB; P22826; -.
DR   SMR; P22826; -.
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   Pyrrolidone carboxylic acid; Secreted; Toxin.
FT   CHAIN           1..51
FT                   /note="Disintegrin eristicophin"
FT                   /evidence="ECO:0000269|PubMed:2033037"
FT                   /id="PRO_0000101805"
FT   DOMAIN          1..51
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           29..31
FT                   /note="Cell attachment site"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:2033037"
FT   DISULFID        7..16
FT                   /evidence="ECO:0000250|UniProtKB:P0C6S4"
FT   DISULFID        12..37
FT                   /evidence="ECO:0000250|UniProtKB:P0C6S4"
FT   DISULFID        13..42
FT                   /evidence="ECO:0000250|UniProtKB:P0C6S4"
FT   DISULFID        25..44
FT                   /evidence="ECO:0000250|UniProtKB:P0C6S4"
SQ   SEQUENCE   51 AA;  5823 MW;  BC9FF45570ADEE5E CRC64;
     QRQEEPCATG PCCRRCKFKR AGKVCRVARG DWNNDYCTGK SCDCPRNPWN G