ID   VM2T_PROFL              Reviewed;          70 AA.
AC   P21859;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Disintegrin triflavin;
DE   AltName: Full=Platelet aggregation activation inhibitor;
DE   AltName: Full=RGD-containing peptide;
DE   AltName: Full=Trimestatin;
OS   Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=88087;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Venom;
RX   PubMed=1864844;
RA   Huang T.-F., Sheu J.-R., Teng C.-M., Chen S.-W., Liu C.-S.;
RT   "Triflavin, an antiplatelet Arg-Gly-Asp-containing peptide, is a specific
RT   antagonist of platelet membrane glycoprotein IIb-IIIa complex.";
RL   J. Biochem. 109:328-334(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-17.
RC   TISSUE=Venom;
RX   PubMed=1859363; DOI=10.1042/bj2770351;
RA   Huang T.-F., Sheu J.-R., Teng C.-M.;
RT   "A potent antiplatelet peptide, triflavin, from Trimeresurus flavoviridis
RT   snake venom.";
RL   Biochem. J. 277:351-357(1991).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=14499613; DOI=10.1016/s0022-2836(03)00991-4;
RA   Fujii Y., Okuda D., Fujimoto Z., Horii K., Morita T., Mizuno H.;
RT   "Crystal structure of trimestatin, a disintegrin containing a cell adhesion
RT   recognition motif RGD.";
RL   J. Mol. Biol. 332:1115-1122(2003).
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.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC   -!- MISCELLANEOUS: The disintegrin belongs to the medium 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; A58649; A58649.
DR   PDB; 1J2L; X-ray; 1.70 A; A=1-70.
DR   PDBsum; 1J2L; -.
DR   AlphaFoldDB; P21859; -.
DR   SMR; P21859; -.
DR   EvolutionaryTrace; P21859; -.
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; Disintegrin domain; 1.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 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..70
FT                   /note="Disintegrin triflavin"
FT                   /id="PRO_0000101810"
FT   DOMAIN          1..70
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT   MOTIF           49..51
FT                   /note="Cell attachment site"
FT   DISULFID        4..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:14499613"
FT   DISULFID        6..14
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:14499613"
FT   DISULFID        13..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:14499613"
FT   DISULFID        27..33
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:14499613"
FT   DISULFID        32..57
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:14499613"
FT   DISULFID        45..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT                   ECO:0000269|PubMed:14499613"
FT   TURN            16..18
FT                   /evidence="ECO:0007829|PDB:1J2L"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:1J2L"
FT   STRAND          28..30
FT                   /evidence="ECO:0007829|PDB:1J2L"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:1J2L"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:1J2L"
SQ   SEQUENCE   70 AA;  7576 MW;  D8D256789E903415 CRC64;
     GEECDCGSPS NPCCDAATCK LRPGAQCADG LCCDQCRFKK KRTICRIARG DFPDDRCTGQ
     SADCPRWNGL
//