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Database: UniProt
Entry: Q9R1C6
LinkDB: Q9R1C6
Original site: Q9R1C6 
ID   DGKE_MOUSE              Reviewed;         564 AA.
AC   Q9R1C6; Q5SU69;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   10-APR-2019, entry version 144.
DE   RecName: Full=Diacylglycerol kinase epsilon;
DE            Short=DAG kinase epsilon;
DE            EC=2.7.1.107;
DE   AltName: Full=Diglyceride kinase epsilon;
DE            Short=DGK-epsilon;
GN   Name=Dgke;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11287665; DOI=10.1073/pnas.081536298;
RA   Rodriguez de Turco E.B., Tang W., Topham M.K., Sakane F.,
RA   Marcheselli V.L., Chen C., Taketomi A., Prescott S.M., Bazan N.G.;
RT   "Diacylglycerol kinase epsilon regulates seizure susceptibility and
RT   long-term potentiation through arachidonoyl-inositol lipid
RT   signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4740-4745(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=23542698; DOI=10.1038/ng.2590;
RA   Lemaire M., Fremeaux-Bacchi V., Schaefer F., Choi M., Tang W.H.,
RA   Le Quintrec M., Fakhouri F., Taque S., Nobili F., Martinez F., Ji W.,
RA   Overton J.D., Mane S.M., Nuernberg G., Altmueller J., Thiele H.,
RA   Morin D., Deschenes G., Baudouin V., Llanas B., Collard L.,
RA   Majid M.A., Simkova E., Nuernberg P., Rioux-Leclerc N., Moeckel G.W.,
RA   Gubler M.C., Hwa J., Loirat C., Lifton R.P.;
RT   "Recessive mutations in DGKE cause atypical hemolytic-uremic
RT   syndrome.";
RL   Nat. Genet. 45:531-536(2013).
CC   -!- FUNCTION: Highly selective for arachidonate-containing species of
CC       diacylglycerol (DAG). May terminate signals transmitted through
CC       arachidonoyl-DAG or may contribute to the synthesis of
CC       phospholipids with defined fatty acid composition (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-
CC         3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Cytoplasm {ECO:0000250}. Membrane
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in platelets.
CC       {ECO:0000269|PubMed:23542698}.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC       family. {ECO:0000305}.
DR   EMBL; AF136744; AAD45665.1; -; mRNA.
DR   EMBL; AL646096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS25234.1; -.
DR   RefSeq; NP_062378.1; NM_019505.3.
DR   UniGene; Mm.153695; -.
DR   ProteinModelPortal; Q9R1C6; -.
DR   BioGrid; 207804; 1.
DR   STRING; 10090.ENSMUSP00000103526; -.
DR   iPTMnet; Q9R1C6; -.
DR   PhosphoSitePlus; Q9R1C6; -.
DR   SwissPalm; Q9R1C6; -.
DR   EPD; Q9R1C6; -.
DR   MaxQB; Q9R1C6; -.
DR   PaxDb; Q9R1C6; -.
DR   PeptideAtlas; Q9R1C6; -.
DR   PRIDE; Q9R1C6; -.
DR   DNASU; 56077; -.
DR   Ensembl; ENSMUST00000000285; ENSMUSP00000000285; ENSMUSG00000000276.
DR   Ensembl; ENSMUST00000107894; ENSMUSP00000103526; ENSMUSG00000000276.
DR   GeneID; 56077; -.
DR   KEGG; mmu:56077; -.
DR   UCSC; uc007kwd.1; mouse.
DR   CTD; 8526; -.
DR   MGI; MGI:1889276; Dgke.
DR   eggNOG; KOG1169; Eukaryota.
DR   eggNOG; ENOG410XQVB; LUCA.
DR   GeneTree; ENSGT00940000158604; -.
DR   HOGENOM; HOG000220913; -.
DR   HOVERGEN; HBG051347; -.
DR   InParanoid; Q9R1C6; -.
DR   KO; K00901; -.
DR   OMA; WVLNTIY; -.
DR   OrthoDB; 1275907at2759; -.
DR   PhylomeDB; Q9R1C6; -.
DR   TreeFam; TF313104; -.
DR   BRENDA; 2.7.1.107; 3474.
DR   Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR   PRO; PR:Q9R1C6; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000000276; Expressed in 204 organ(s), highest expression level in retina.
DR   ExpressionAtlas; Q9R1C6; baseline and differential.
DR   Genevisible; Q9R1C6; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; ISO:MGI.
DR   GO; GO:0016301; F:kinase activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0046339; P:diacylglycerol metabolic process; IBA:GO_Central.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0046834; P:lipid phosphorylation; ISO:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR   GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd00029; C1; 2.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR037607; DGK.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   PANTHER; PTHR11255; PTHR11255; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Membrane;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Repeat;
KW   Transferase; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN         1    564       Diacylglycerol kinase epsilon.
FT                                /FTId=PRO_0000218465.
FT   TRANSMEM     20     40       Helical. {ECO:0000255}.
FT   TRANSMEM    433    453       Helical. {ECO:0000255}.
FT   DOMAIN      212    353       DAGKc. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00783}.
FT   ZN_FING      57    106       Phorbol-ester/DAG-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00226}.
FT   ZN_FING     121    174       Phorbol-ester/DAG-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00226}.
SQ   SEQUENCE   564 AA;  63635 MW;  C900BEC2CE9DD109 CRC64;
     MEGDQRSGPP AQSLLPDGHL VLWTLCSVLL PVFITLWCSL QRSRRQLHRR DIFRKSKHCW
     RDTDLFSHPT YCCVCAQHIL QGAFCDCCGL RVDEGCLKKV DKRFPCKEIM LKNDKAADAM
     PHHWIRGNVP LCSYCVFCRQ QCGSQPKLCD YRCIWCQKTV HDECMRGSLR SEKCDFGEFR
     NLIIPPSYLT SINQMRKDKN TNYEGLASKF GKQWTPLIIL ANSRSGTNMG EGLLGEFKIL
     LNPVQVFDVT KTPPIKALQL CTLLPYYSVR VLVCGGDGTV GWVLDAIDEM KIKGQEKYIP
     EVAVLPLGTG NDLSNTLGWG TGYAGEIPVA QVLRNVMEAD GIKLDRWKVQ VTNKGYYNLR
     KPKEFTMNNY FSVGPDALMA LNFHAHREKA PSLFSSRILN KAVYLFYGTK DCLVQECKDL
     NKKIELELDG ERVELPNLEG IIVLNIGYWG GGCRLWEGMG DETYPLARHD DGLLEIVGVY
     GSFHCAQIQV KLANPFRIGQ AHTVRLTLKC SMMPMQVDGE PWAQGPCTVT ITHKTHALML
     YFSGEQSDDD ISSPSDHEDV KEAE
//
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