DOK4_PONAB
ID DOK4_PONAB Reviewed; 339 AA.
AC Q5RA30;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Docking protein 4;
DE AltName: Full=Downstream of tyrosine kinase 4;
GN Name=DOK4;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. DOK4 functions in RET-mediated
CC neurite outgrowth and plays a positive role in activation of the MAP
CC kinase pathway (By similarity). Putative link with downstream effectors
CC of RET in neuronal differentiation. May be involved in the regulation
CC of the immune response induced by T-cells (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RET and TEK/TIE2. Interaction with RET is
CC mediated through the PTB domain and requires phosphorylation of RET (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: PTB domain mediates receptor interaction. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues in response to insulin, IGF1
CC or RET stimulation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DOK family. Type B subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR859193; CAH91380.1; -; mRNA.
DR RefSeq; NP_001125815.1; NM_001132343.1.
DR AlphaFoldDB; Q5RA30; -.
DR SMR; Q5RA30; -.
DR STRING; 9601.ENSPPYP00000008351; -.
DR GeneID; 100172743; -.
DR KEGG; pon:100172743; -.
DR CTD; 55715; -.
DR eggNOG; KOG4047; Eukaryota.
DR InParanoid; Q5RA30; -.
DR Proteomes; UP000001595; Unplaced.
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 2: Evidence at transcript level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..339
FT /note="Docking protein 4"
FT /id="PRO_0000187276"
FT DOMAIN 7..112
FT /note="PH"
FT DOMAIN 132..237
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT MOTIF 265..275
FT /note="DKFBH motif"
SQ SEQUENCE 339 AA; 38621 MW; E465BD320AE17A80 CRC64;
MATNFSDIVK QGYVKMKSRK LGIYRRCWLV FRKSSSKGPQ RLEKYPDEKS VCLRGCPKVT
EISNVKCVTR LPKETKRQAV AIIFTDDSAR TFTCDSELEA EEWYKTLSVE CLGSRLNDIS
LGEPDLLAPG VQCEQTDRFN VFLLPCPNLD VYGECKLQIT HENIYLWDIH NPRVKLVSWP
LCSLRRYGRD AARFTFEAGR MCDAGEGLYT FQTQEGEQIY QRVHSATLAI AEQHKRVLLE
MEKNVRLLNK GTEHYSYPCT PTTMLPRSAY WHHITGSQNI AEASSYAAQG PEQQVASQFL
WAWSDTGRIC ASTVLLASLA VGVLSRGDIW LTPQVKIWF