ID   DOK3_CHICK              Reviewed;         426 AA.
AC   A3R064;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Docking protein 3;
DE   AltName: Full=Downstream of tyrosine kinase 3;
GN   Name=DOK3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP   PHOSPHORYLATION AT TYR-331, IDENTIFICATION BY MASS SPECTROMETRY,
RP   MUTAGENESIS OF TYR-331, VARIANT ALA-122, AND INTERACTION WITH GRB2 AND
RP   INPP5D.
RX   PubMed=17290227; DOI=10.1038/sj.emboj.7601557;
RA   Stork B., Neumann K., Goldbeck I., Alers S., Kaehne T., Naumann M.,
RA   Engelke M., Wienands J.;
RT   "Subcellular localization of Grb2 by the adaptor protein Dok-3 restricts
RT   the intensity of Ca2+ signaling in B cells.";
RL   EMBO J. 26:1140-1149(2007).
CC   -!- FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding
CC       proteins. They provide a docking platform for the assembly of
CC       multimolecular signaling complexes. Plays a role as negative regulator
CC       of the mobilization of calcium ions and of calcium signaling.
CC       {ECO:0000269|PubMed:17290227}.
CC   -!- SUBUNIT: Homooligomer. Interacts with GRB2 and INPP5D/SHIP.
CC       {ECO:0000269|PubMed:17290227}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17290227}. Cell
CC       membrane {ECO:0000269|PubMed:17290227}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:17290227}; Cytoplasmic side
CC       {ECO:0000269|PubMed:17290227}.
CC   -!- DOMAIN: PTB domain mediates receptor interaction.
CC   -!- PTM: Tyrosine-phosphorylated in the presence of GRB2.
CC       {ECO:0000269|PubMed:17290227}.
CC   -!- SIMILARITY: Belongs to the DOK family. Type A subfamily. {ECO:0000305}.
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DR   EMBL; EF051736; ABM91434.1; -; mRNA.
DR   RefSeq; NP_001076832.1; NM_001083363.1.
DR   AlphaFoldDB; A3R064; -.
DR   SMR; A3R064; -.
DR   STRING; 9031.ENSGALP00000041481; -.
DR   iPTMnet; A3R064; -.
DR   GeneID; 429960; -.
DR   KEGG; gga:429960; -.
DR   CTD; 79930; -.
DR   VEuPathDB; HostDB:geneid_429960; -.
DR   eggNOG; KOG4047; Eukaryota.
DR   InParanoid; A3R064; -.
DR   OrthoDB; 378139at2759; -.
DR   PhylomeDB; A3R064; -.
DR   PRO; PR:A3R064; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   CDD; cd01203; PTB_DOK1_DOK2_DOK3; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR037751; Dok1/2/3_PTB.
DR   InterPro; IPR002404; IRS_PTB.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   Pfam; PF02174; IRS; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00310; PTBI; 1.
DR   PROSITE; PS51064; IRS_PTB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..426
FT                   /note="Docking protein 3"
FT                   /id="PRO_0000356282"
FT   DOMAIN          4..115
FT                   /note="PH"
FT   DOMAIN          145..249
FT                   /note="IRS-type PTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT   REGION          243..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         331
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:17290227"
FT   VARIANT         122
FT                   /note="E -> A"
FT                   /evidence="ECO:0000269|PubMed:17290227"
FT   MUTAGEN         197
FT                   /note="R->A: Abolishes interaction with INPP5D/SHIP."
FT   MUTAGEN         331
FT                   /note="Y->F: Strongly reduced tyrosine phosphorylation.
FT                   Abolishes interaction with GRB2 and INPP5D/SHIP."
FT                   /evidence="ECO:0000269|PubMed:17290227"
SQ   SEQUENCE   426 AA;  47167 MW;  F955FB76D699BD80 CRC64;
     MERPVKDGII YVQHCKFGKR TWRKIRAQLF AASPFGVARM EKFDARDHGT VSDISLQRCA
     RRVIRLSDCV SVGPMGTESC PKATAAFYLT TTEKNYVLAA EQRDEWIEQL CQLAFQGKKE
     AEQSSSTGLQ PIPMEENCLY SSWQDLTEFP VLVLRTEAAA RCELHGHYVL AALPHSLTLK
     DAQSQQPLLT WPYPFLRKFG QDQNIFSFEA GRRSDSGEGT FTFSTPRAAE LCRAVAAAIA
     CQQQGQESPQ PSAQGLSNQP WGAEAEDPQC SPTLGRAHSG SHSASYPSLN LLRFPPVEPE
     APAPIVYASI ARGQQPHFRP CPGQPLPEHL YENIFTAQPR PLAEEEAEEE EGRWELGCRQ
     APEGHSSEAA VPYPARSAPQ PHTQRWAPGG SRGGAEEPSR PKPQRTLRAK LVRLLSRDGP
     GARDWS