ID   DOK7_TAKRU              Reviewed;         502 AA.
AC   Q18PD9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Protein Dok-7;
DE   AltName: Full=Downstream of tyrosine kinase 7;
GN   Name=dok7;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16794080; DOI=10.1126/science.1127142;
RA   Okada K., Inoue A., Okada M., Murata Y., Kakuta S., Jigami T., Kubo S.,
RA   Shiraishi H., Eguchi K., Motomura M., Akiyama T., Iwakura Y., Higuchi O.,
RA   Yamanashi Y.;
RT   "The muscle protein Dok-7 is essential for neuromuscular synaptogenesis.";
RL   Science 312:1802-1805(2006).
CC   -!- FUNCTION: Probable muscle-intrinsic activator of MUSK that plays an
CC       essential role in neuromuscular synaptogenesis. Acts in aneural
CC       activation of MUSK and subsequent acetylcholine receptor (AchR)
CC       clustering in myotubes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Synapse {ECO:0000250}. Note=Accumulates at
CC       neuromuscular junctions. {ECO:0000250}.
CC   -!- DOMAIN: The PH domain mediated binding to phospholipids with
CC       phosphoinositol headgroups. Affinity is highest for phosphatidyl 3,4,5-
CC       trisphosphate, followed by phosphatidylinositol 3,4-bisphosphate and
CC       phosphatidylinositol 4,5-bisphosphate (By similarity). {ECO:0000250}.
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DR   EMBL; AB220920; BAE96741.1; -; mRNA.
DR   RefSeq; NP_001037837.1; NM_001044372.1.
DR   AlphaFoldDB; Q18PD9; -.
DR   SMR; Q18PD9; -.
DR   GeneID; 724073; -.
DR   KEGG; tru:724073; -.
DR   CTD; 285489; -.
DR   HOGENOM; CLU_024931_0_0_1; -.
DR   InParanoid; Q18PD9; -.
DR   OrthoDB; 317220at2759; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IEA:InterPro.
DR   CDD; cd14677; PH_DOK7; 1.
DR   CDD; cd13165; PTB_DOK7; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   InterPro; IPR037746; Dok-7.
DR   InterPro; IPR037747; Dok-7_PH.
DR   InterPro; IPR037748; Dok-7_PTB.
DR   InterPro; IPR002404; IRS_PTB.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR21636; PTHR21636; 1.
DR   Pfam; PF02174; IRS; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Lipid-binding; Membrane; Reference proteome; Synapse.
FT   CHAIN           1..502
FT                   /note="Protein Dok-7"
FT                   /id="PRO_0000250373"
FT   DOMAIN          4..109
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          105..210
FT                   /note="IRS-type PTB"
FT   REGION          210..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  53658 MW;  D6282260FB47CBA0 CRC64;
     MTDSVVVEGY ARLRDGKKWK TRWLVLRKPS PVADCLLLLV FKDKSDKVQG NKERLSATLE
     ELCGLEVGPW YEGVAFTLAI LCLTQTTLLG FDSKEALLAW DARLRYSLGE VHRFSVGVLP
     GTKLESGPAT LHLCNNLLAL ARDVPPVIVG HWNLPDLRRY GPVPNGFVFE GGTRCGYWAG
     VFLLASVESE QISFLFDCIV RGISPTRGPF GLRPVLPDPS TSETSSEERL NHETLELEKR
     LSMLSHRSST ASYCPSAGGD DRSISGSSDT SDTSHSDCSV GSRLTIWTEP TSIQPENLGN
     AGAKAAAQSA EKPLPSGQGG GSQPPTKPPR QLQEIGRQSS SDSGIATGSH SSYSGSFSSY
     TGSLDSNTGE DYGSVFSLPP HLGQDVRPCT CLNVPGHEYQ IPTSLRYLYD TPRSVLQEVG
     GDTKDNQPPA ALGPTTEPAE GDKRSPGEGH LATADGDSPN EHFRSPSESK KSSEAPSGGH
     PGSCCFKTIV TICAVCGGFK VS