DOK5_MOUSE
ID DOK5_MOUSE Reviewed; 306 AA.
AC Q91ZM9; Q8BRI3; Q9CSM6;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Docking protein 5;
DE AltName: Full=Downstream of tyrosine kinase 5;
GN Name=Dok5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION, AND INTERACTION
RP WITH RET.
RC TISSUE=Embryo;
RX PubMed=11470823; DOI=10.1083/jcb.200102032;
RA Grimm J., Sachs M., Britsch S., Di Cesare S., Schwarz-Romond T.,
RA Alitalo K., Birchmeier W.;
RT "Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret
RT receptor tyrosine kinase and mediate neuronal differentiation.";
RL J. Cell Biol. 154:345-354(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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. DOK5 functions in RET-mediated
CC neurite outgrowth and plays a positive role in activation of the MAP
CC kinase pathway. Putative link with downstream effectors of RET in
CC neuronal differentiation. {ECO:0000269|PubMed:11470823}.
CC -!- SUBUNIT: Interacts with phosphorylated RET. In contrast to other DOK
CC proteins, it does not interact with RASGAP.
CC {ECO:0000269|PubMed:11470823}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the brain, with a high
CC specificity for neurons. {ECO:0000269|PubMed:11470823}.
CC -!- DEVELOPMENTAL STAGE: In 12.5 dpc and 13 dpc embryos, it is expressed in
CC the central nervous system, e.g. in the neural tube, the dorsal root
CC and the cranial ganglion.
CC -!- DOMAIN: PTB domain mediates receptor interaction.
CC -!- PTM: Phosphorylated on tyrosine residues in response to insulin, IGF1
CC and GDNF. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DOK family. Type B subfamily. {ECO:0000305}.
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DR EMBL; AF418208; AAL14627.1; -; mRNA.
DR EMBL; AK012430; BAB28233.1; -; mRNA.
DR EMBL; AK044148; BAC31799.1; -; mRNA.
DR CCDS; CCDS17125.1; -.
DR RefSeq; NP_001157158.1; NM_001163686.1.
DR RefSeq; NP_084037.3; NM_029761.4.
DR AlphaFoldDB; Q91ZM9; -.
DR SMR; Q91ZM9; -.
DR STRING; 10090.ENSMUSP00000029075; -.
DR iPTMnet; Q91ZM9; -.
DR PhosphoSitePlus; Q91ZM9; -.
DR MaxQB; Q91ZM9; -.
DR PaxDb; Q91ZM9; -.
DR PRIDE; Q91ZM9; -.
DR ProteomicsDB; 277589; -.
DR Antibodypedia; 28805; 387 antibodies from 33 providers.
DR DNASU; 76829; -.
DR Ensembl; ENSMUST00000029075; ENSMUSP00000029075; ENSMUSG00000027560.
DR GeneID; 76829; -.
DR KEGG; mmu:76829; -.
DR UCSC; uc008ocg.2; mouse.
DR CTD; 55816; -.
DR MGI; MGI:1924079; Dok5.
DR VEuPathDB; HostDB:ENSMUSG00000027560; -.
DR eggNOG; KOG4047; Eukaryota.
DR GeneTree; ENSGT00940000160725; -.
DR HOGENOM; CLU_057256_1_0_1; -.
DR InParanoid; Q91ZM9; -.
DR OMA; ITYECIC; -.
DR OrthoDB; 1224728at2759; -.
DR PhylomeDB; Q91ZM9; -.
DR TreeFam; TF324994; -.
DR Reactome; R-MMU-8853659; RET signaling.
DR BioGRID-ORCS; 76829; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Dok5; mouse.
DR PRO; PR:Q91ZM9; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91ZM9; protein.
DR Bgee; ENSMUSG00000027560; Expressed in embryonic brain and 73 other tissues.
DR Genevisible; Q91ZM9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; IDA:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0051386; P:regulation of neurotrophin TRK receptor signaling pathway; ISO:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IPI:MGI.
DR CDD; cd14678; PH_DOK4_DOK5_DOK6; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR037816; DOK4/5/6_PH.
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 Reference proteome.
FT CHAIN 1..306
FT /note="Docking protein 5"
FT /id="PRO_0000187278"
FT DOMAIN 8..112
FT /note="PH"
FT DOMAIN 132..237
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT MOTIF 263..273
FT /note="DKFBH motif"
FT CONFLICT 9
FT /note="V -> M (in Ref. 2; BAC31799)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 35453 MW; 7889802FBEAC04A6 CRC64;
MASNFNDIVK QGYVRIRSRR LGIYQRCWLV FKKASSKGPK RLEKFSDERA AYFRCYHKVT
ELNNVKNVAR LPKSTKKHAI GIYFNDDTSK TFACESDLEA DEWCKVLQME CVGTRINDIS
LGEPDLLATG VEREQSERFN VYLMPSPNLD VHGECALQIT YEYICLWDVQ NPRVKLISWP
LSALRRYGRD TTWFTFEAGR MCETGEGLFI FQTRDGEAIY QKVHSAALAI AEQHERLLQS
VKNSMLQMKK SERAASLSTV VPLPRSAYWQ HITRQHSTGQ LYHLQDVTSP LKLHRTETFP
TYRSEH
