DOK3_RAT
ID DOK3_RAT Reviewed; 444 AA.
AC B2RYG7;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Docking protein 3;
DE AltName: Full=Downstream of tyrosine kinase 3;
GN Name=Dok3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. DOK3 is a negative regulator of JNK
CC signaling in B-cells through interaction with INPP5D/SHIP1. May
CC modulate ABL1 function (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: On tyrosine phosphorylation, interacts with CSK and
CC INPP5D/SHIP1 via their SH2 domains. Binds ABL1 through the PTB domain
CC and in a kinase-dependent manner. Does not interact with RasGAP (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}.
CC -!- DOMAIN: PTB domain mediates receptor interaction. {ECO:0000250}.
CC -!- PTM: Constitutively tyrosine-phosphorylated. {ECO:0000250}.
CC -!- PTM: On IL2 stimulation, phosphorylated on C-terminal tyrosine residues
CC possibly by Src kinases. Can also be phosphorylated by ABL1 kinase (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DOK family. Type A subfamily. {ECO:0000305}.
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DR EMBL; CH474032; EDL93971.1; -; Genomic_DNA.
DR EMBL; BC166772; AAI66772.1; -; mRNA.
DR RefSeq; NP_001100806.1; NM_001107336.1.
DR RefSeq; XP_006253681.1; XM_006253619.3.
DR AlphaFoldDB; B2RYG7; -.
DR SMR; B2RYG7; -.
DR STRING; 10116.ENSRNOP00000018232; -.
DR iPTMnet; B2RYG7; -.
DR PhosphoSitePlus; B2RYG7; -.
DR PaxDb; B2RYG7; -.
DR PeptideAtlas; B2RYG7; -.
DR Ensembl; ENSRNOT00000018232; ENSRNOP00000018232; ENSRNOG00000013564.
DR GeneID; 306760; -.
DR KEGG; rno:306760; -.
DR UCSC; RGD:1311840; rat.
DR CTD; 79930; -.
DR RGD; 1311840; Dok3.
DR eggNOG; KOG4047; Eukaryota.
DR GeneTree; ENSGT00940000161724; -.
DR HOGENOM; CLU_569310_0_0_1; -.
DR InParanoid; B2RYG7; -.
DR OMA; YENLCML; -.
DR OrthoDB; 378139at2759; -.
DR PhylomeDB; B2RYG7; -.
DR TreeFam; TF324994; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:B2RYG7; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR Bgee; ENSRNOG00000013564; Expressed in spleen and 19 other tissues.
DR Genevisible; B2RYG7; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
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..444
FT /note="Docking protein 3"
FT /id="PRO_0000356281"
FT DOMAIN 7..123
FT /note="PH"
FT DOMAIN 157..261
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L591"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZK7"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZK7"
FT MOD_RES 325
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZK7"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZK7"
SQ SEQUENCE 444 AA; 48190 MW; DF79C5ADB1893046 CRC64;
MESVETPVKD GLLYQQHMKF GKKCWRKVWA LLYAGGPSGV ARLESWDVRD GGLGPGGDRP
AGPGRRGERR IIRLADCVSV LPADGESCPR DTGAFLITTT ERSHLLAAQH RQSWMDPICQ
LAFPSTGECS SGSGQAESPK RGFVPMEENS IYSSWQEVAE FPVVVQRTEA TTRCQLKGPY
LLVLGQDDIQ LRETSKPQAC YSWPYRFLRK FGSDKGVFSF EAGRRCDSGE GLFAFSSPRA
PDICGAVAAA IARQRERLPE LAMSPPCPLP RALSLPSLEP PGELREVAPE YELAPSRKLP
LTDPGPQSLP LLLSPTQDGT ASSLYASVCK QTSKHKATVE HLYENVFMLE ASPGLSNGGP
EAQEGPPGGR SPLGSPIYHN SEELSWPGSA HDSNLEAQYR RLLELELDDA GGAGRPGAQT
GIKAKLVTLL TRERKKGPAP CDRP
