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Database: UniProt
Entry: DOK6_MOUSE
LinkDB: DOK6_MOUSE
Original site: DOK6_MOUSE 
ID   DOK6_MOUSE              Reviewed;         331 AA.
AC   Q2MHE5; B2RSP9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   RecName: Full=Docking protein 6;
DE   AltName: Full=Downstream of tyrosine kinase 6;
GN   Name=Dok6;
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].
RA   Okada K., Higuchi O., Yamanashi Y.;
RT   "Roles of Dok family proteins in neuromuscular synaptogenesis.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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. DOK6 promotes Ret-mediated neurite
CC       growth. May have a role in brain development and/or maintenance (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts via its PTB domain with phosphorylated RET.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q2MHE5; Q6VNS1: Ntrk3; NbExp=3; IntAct=EBI-20585476, EBI-16744951;
CC   -!- DOMAIN: PTB domain mediates receptor interaction. {ECO:0000250}.
CC   -!- PTM: On Ret activation, phosphorylated on one or more C-terminal
CC       tyrosine residues by an Src family kinase. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DOK family. Type B subfamily. {ECO:0000305}.
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DR   EMBL; AB221044; BAE75920.1; -; mRNA.
DR   EMBL; BC138955; AAI38956.1; -; mRNA.
DR   EMBL; BC138957; AAI38958.1; -; mRNA.
DR   CCDS; CCDS37878.1; -.
DR   RefSeq; NP_001034262.1; NM_001039173.1.
DR   AlphaFoldDB; Q2MHE5; -.
DR   SMR; Q2MHE5; -.
DR   BioGRID; 549975; 1.
DR   IntAct; Q2MHE5; 2.
DR   STRING; 10090.ENSMUSP00000095103; -.
DR   iPTMnet; Q2MHE5; -.
DR   PhosphoSitePlus; Q2MHE5; -.
DR   MaxQB; Q2MHE5; -.
DR   PaxDb; 10090-ENSMUSP00000095103; -.
DR   ProteomicsDB; 277371; -.
DR   Antibodypedia; 23216; 193 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000097495.5; ENSMUSP00000095103.4; ENSMUSG00000073514.5.
DR   GeneID; 623279; -.
DR   KEGG; mmu:623279; -.
DR   UCSC; uc008fvr.1; mouse.
DR   AGR; MGI:3639495; -.
DR   CTD; 220164; -.
DR   MGI; MGI:3639495; Dok6.
DR   VEuPathDB; HostDB:ENSMUSG00000073514; -.
DR   eggNOG; KOG4047; Eukaryota.
DR   GeneTree; ENSGT00940000158760; -.
DR   HOGENOM; CLU_057256_0_0_1; -.
DR   InParanoid; Q2MHE5; -.
DR   OMA; NIFRRCW; -.
DR   OrthoDB; 2996885at2759; -.
DR   PhylomeDB; Q2MHE5; -.
DR   TreeFam; TF324994; -.
DR   Reactome; R-MMU-8853659; RET signaling.
DR   BioGRID-ORCS; 623279; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Dok6; mouse.
DR   PRO; PR:Q2MHE5; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q2MHE5; Protein.
DR   Bgee; ENSMUSG00000073514; Expressed in dentate gyrus of hippocampal formation granule cell and 24 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
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; cd14678; PH_DOK4_DOK5_DOK6; 1.
DR   CDD; cd13164; PTB_DOK4_DOK5_DOK6; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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   PANTHER; PTHR21258:SF43; DOCKING PROTEIN 6; 1.
DR   PANTHER; PTHR21258; DOCKING PROTEIN RELATED; 1.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM01244; IRS; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00310; PTBI; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS51064; IRS_PTB; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..331
FT                   /note="Docking protein 6"
FT                   /id="PRO_0000322637"
FT   DOMAIN          8..112
FT                   /note="PH"
FT   DOMAIN          132..237
FT                   /note="IRS-type PTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT   REGION          293..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           263..273
FT                   /note="DKFBH motif"
SQ   SEQUENCE   331 AA;  38287 MW;  0C5EF364547091C1 CRC64;
     MASNFNDIVK QGYVKIRSRK LGIFRRCWLV FKKASSKGPR RLEKFPDEKA AYFRNFHKVT
     ELHNIKNITR LPRETKKHAV AIIFHDETSK TFACESELEA EEWCKHLCME CLGTRLNDIS
     LGEPDLLAAG VQREQNERFN VYLMPTPNLD IYGECTMQIT HENIYLWDIH NAKVKLVMWP
     LSSLRRYGRD STWFTFESGR MCDTGEGLFT FQTREGEMIY QKVHSATLAI AEQHERLMLE
     MEQKARLQTS LTEPMTLSKS ISLPRSAYWH HITRQNSVGE IYSLQGHGFG SSKMSRAQTF
     PSYAPEQSEE AQPPLSRSSS YGFSYSSSLI Q
//
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