DOK1_RAT
ID DOK1_RAT Reviewed; 480 AA.
AC Q4QQV2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Docking protein 1;
DE AltName: Full=Downstream of tyrosine kinase 1;
GN Name=Dok1;
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 MRNA].
RC TISSUE=Placenta;
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).
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. DOK1 appears to be a negative
CC regulator of the insulin signaling pathway. Modulates integrin
CC activation by competing with talin for the same binding site on ITGB3
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RasGAP and INPP5D/SHIP1. Interacts directly
CC with phosphorylated ITGB3 (By similarity). Interacts with SRMS (via the
CC SH2 and SH3 domains) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- DOMAIN: The PTB domain mediates receptor interaction. {ECO:0000250}.
CC -!- PTM: Constitutively tyrosine-phosphorylated (By similarity).
CC Phosphorylated by TEC. Phosphorylated by LYN (By similarity).
CC Phosphorylated on tyrosine residues by the insulin receptor kinase.
CC Results in the negative regulation of the insulin signaling pathway (By
CC similarity). Phosphorylated on tyrosine residues by SRMS (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DOK family. Type A subfamily. {ECO:0000305}.
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DR EMBL; BC097972; AAH97972.1; -; mRNA.
DR RefSeq; NP_001020587.1; NM_001025416.1.
DR AlphaFoldDB; Q4QQV2; -.
DR SMR; Q4QQV2; -.
DR BioGRID; 260183; 4.
DR IntAct; Q4QQV2; 3.
DR MINT; Q4QQV2; -.
DR STRING; 10116.ENSRNOP00000010020; -.
DR iPTMnet; Q4QQV2; -.
DR PhosphoSitePlus; Q4QQV2; -.
DR jPOST; Q4QQV2; -.
DR PaxDb; Q4QQV2; -.
DR GeneID; 312477; -.
DR KEGG; rno:312477; -.
DR UCSC; RGD:1309499; rat.
DR CTD; 1796; -.
DR RGD; 1309499; Dok1.
DR VEuPathDB; HostDB:ENSRNOG00000007412; -.
DR eggNOG; KOG4047; Eukaryota.
DR HOGENOM; CLU_030101_3_1_1; -.
DR InParanoid; Q4QQV2; -.
DR OMA; ALYSQVH; -.
DR OrthoDB; 378139at2759; -.
DR PhylomeDB; Q4QQV2; -.
DR TreeFam; TF324994; -.
DR Reactome; R-RNO-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR Reactome; R-RNO-8853659; RET signaling.
DR PRO; PR:Q4QQV2; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007412; Expressed in spleen and 18 other tissues.
DR Genevisible; Q4QQV2; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0038145; P:macrophage colony-stimulating factor signaling pathway; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:RGD.
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 Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00310; PTBI; 1.
DR PROSITE; PS51064; IRS_PTB; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..480
FT /note="Docking protein 1"
FT /id="PRO_0000356279"
FT DOMAIN 3..119
FT /note="PH"
FT DOMAIN 151..259
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 253..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 295
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 336
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 340
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 361
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 376
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 397
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 408
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99704"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
FT MOD_RES 448
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97465"
SQ SEQUENCE 480 AA; 52170 MW; B276AC33DDA9F194 CRC64;
MDGALMEGPL FLQSQRFGTK RWKKTWAVLY PASPHGVARL EFFDHKGSSS GGGRGGSRRL
DCKMIRLAEC VSVVPVTVES PPEPGASAFR LDTAQRSHLL AADAASSTAW VQILCRTAFP
KGGWALAQTE NPPKFSALEM LENSLYSPTW EGSQFWVTSQ KTEASERCGL QGSYVLRVEA
EKLTLLTLGA QSQILEPLLF WPYTLLRRYG RDKVMFSFEA GRRCPSGPGT FTFQTAQGND
IFQAVEAAIQ QQKAQGKVGQ GQDITRTDSH DGETEGKMAP TPVPQEPLGS PPALYAEPLD
SLRIPPGPSQ DSLYSDPLGS TPAGAGEGVQ RKKPLYWDLY GHVQQQLLKT KLIDSKEDPI
YDEPEGLAPA PLRGLYDLPQ EPKDAWWCQA RLKEEGYELP YNPATDDYAV PPPRSSKPTP
APKPQGLILP ESGTTAGSGS KGSDTALYSQ VQKSGTPGRW DCGLSRVGND RVGVKSEGST
