DGKH_HUMAN
ID DGKH_HUMAN Reviewed; 1220 AA.
AC Q86XP1; A2A2W7; A6NFX7; B4DZ34; Q5VZW0; Q6PI56; Q86XP2; Q8N3N0; Q8N7J9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Diacylglycerol kinase eta {ECO:0000305};
DE Short=DAG kinase eta;
DE EC=2.7.1.107 {ECO:0000269|PubMed:12810723, ECO:0000269|PubMed:23949095};
DE AltName: Full=Diglyceride kinase eta;
DE Short=DGK-eta;
GN Name=DGKH {ECO:0000312|HGNC:HGNC:2854};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, PATHWAY, SUBUNIT (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY (ISOFORMS 1 AND 2), INDUCTION (ISOFORMS 1 AND 2),
RP PHOSPHORYLATION, DOMAIN, AND MUTAGENESIS OF TRP-1151.
RC TISSUE=Testis;
RX PubMed=12810723; DOI=10.1074/jbc.m301542200;
RA Murakami T., Sakane F., Imai S., Houkin K., Kanoh H.;
RT "Identification and characterization of two splice variants of human
RT diacylglycerol kinase eta.";
RL J. Biol. Chem. 278:34364-34372(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 640-1220 (ISOFORM 2).
RC TISSUE=Testis, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 617-1220 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAF1 AND BRAF.
RX PubMed=19710016; DOI=10.1074/jbc.m109.043604;
RA Yasuda S., Kai M., Imai S., Takeishi K., Taketomi A., Toyota M., Kanoh H.,
RA Sakane F.;
RT "Diacylglycerol kinase eta augments C-Raf activity and B-Raf/C-Raf
RT heterodimerization.";
RL J. Biol. Chem. 284:29559-29570(2009).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23949095; DOI=10.1159/000351849;
RA Sato M., Liu K., Sasaki S., Kunii N., Sakai H., Mizuno H., Saga H.,
RA Sakane F.;
RT "Evaluations of the selectivities of the diacylglycerol kinase inhibitors
RT R59022 and R59949 among diacylglycerol kinase isozymes using a new non-
RT radioactive assay method.";
RL Pharmacology 92:99-107(2013).
CC -!- FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into
CC phosphatidic acid/phosphatidate/PA and regulates the respective levels
CC of these two bioactive lipids (PubMed:12810723, PubMed:23949095).
CC Thereby, acts as a central switch between the signaling pathways
CC activated by these second messengers with different cellular targets
CC and opposite effects in numerous biological processes (Probable)
CC (PubMed:12810723, PubMed:23949095). Plays a key role in promoting cell
CC growth (PubMed:19710016). Activates the Ras/B-Raf/C-Raf/MEK/ERK
CC signaling pathway induced by EGF (PubMed:19710016). Regulates the
CC recruitment of RAF1 and BRAF from cytoplasm to membranes and their
CC heterodimerization (PubMed:19710016). {ECO:0000269|PubMed:12810723,
CC ECO:0000269|PubMed:19710016, ECO:0000269|PubMed:23949095, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608,
CC ChEBI:CHEBI:456216; EC=2.7.1.107;
CC Evidence={ECO:0000269|PubMed:12810723};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:12810723};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:12810723, ECO:0000269|PubMed:23949095};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:12810723};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:12810723}.
CC -!- SUBUNIT: Interacts with RAF1 and BRAF. {ECO:0000269|PubMed:19710016}.
CC -!- SUBUNIT: [Isoform 1]: Homooligomers (PubMed:12810723). Heterooligomers
CC (PubMed:12810723). Oligomerization through the SAM domain inhibits the
CC diacylglycerol kinase activity (PubMed:12810723). Heterooligomerizes
CC with SAM domain-containing isoforms of DGKD (PubMed:12810723).
CC {ECO:0000269|PubMed:12810723}.
CC -!- SUBUNIT: [Isoform 2]: Does not form homooligomers.
CC {ECO:0000269|PubMed:12810723}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12810723,
CC ECO:0000269|PubMed:19710016}. Cell membrane
CC {ECO:0000269|PubMed:12810723, ECO:0000269|PubMed:19710016}.
CC Note=Translocated from the cytoplasm to endosomes in response to stress
CC stimuli (PubMed:12810723). Isoform 2 is rapidly relocated back to the
CC cytoplasm upon removal of stress stimuli, whereas isoform 1 exhibits
CC sustained endosomal association (PubMed:12810723). Translocates from
CC the cytoplasm to the cell membrane in the presence of active GTP-bound
CC form of HRAS (PubMed:19710016).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=DAG kinase eta-2, DGKH-2;
CC IsoId=Q86XP1-1; Sequence=Displayed;
CC Name=2; Synonyms=DAG kinase eta-1, DGKH-1;
CC IsoId=Q86XP1-2; Sequence=VSP_019185;
CC Name=3;
CC IsoId=Q86XP1-3; Sequence=VSP_019183, VSP_019186;
CC Name=4;
CC IsoId=Q86XP1-5; Sequence=VSP_019183;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed only in testis, kidney and
CC colon. {ECO:0000269|PubMed:12810723}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12810723}.
CC -!- INDUCTION: [Isoform 1]: Down-regulated by glucocorticoid.
CC {ECO:0000269|PubMed:12810723}.
CC -!- INDUCTION: [Isoform 2]: Up-regulated by glucocorticoid.
CC {ECO:0000269|PubMed:12810723}.
CC -!- DOMAIN: The SAM domain mediates homooligomerization.
CC {ECO:0000269|PubMed:12810723}.
CC -!- PTM: Phosphorylated. Phosphorylation does not inhibit catalytic
CC activity. {ECO:0000269|PubMed:12810723}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC05280.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AB078967; BAC66960.1; -; mRNA.
DR EMBL; AB078968; BAC66961.1; -; mRNA.
DR EMBL; AK302727; BAG63946.1; -; mRNA.
DR EMBL; AL136527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043292; AAH43292.1; -; mRNA.
DR EMBL; AL833883; CAD38739.1; -; mRNA.
DR EMBL; AK098302; BAC05280.1; ALT_INIT; mRNA.
DR CCDS; CCDS55898.1; -. [Q86XP1-3]
DR CCDS; CCDS55899.1; -. [Q86XP1-5]
DR CCDS; CCDS9381.1; -. [Q86XP1-1]
DR CCDS; CCDS9382.1; -. [Q86XP1-2]
DR RefSeq; NP_001191433.1; NM_001204504.2. [Q86XP1-2]
DR RefSeq; NP_001191434.1; NM_001204505.2. [Q86XP1-3]
DR RefSeq; NP_001191435.1; NM_001204506.2. [Q86XP1-5]
DR RefSeq; NP_001284358.1; NM_001297429.1.
DR RefSeq; NP_690874.2; NM_152910.5. [Q86XP1-2]
DR RefSeq; NP_821077.1; NM_178009.4. [Q86XP1-1]
DR AlphaFoldDB; Q86XP1; -.
DR SMR; Q86XP1; -.
DR BioGRID; 127768; 35.
DR IntAct; Q86XP1; 7.
DR STRING; 9606.ENSP00000337572; -.
DR ChEMBL; CHEMBL4105940; -.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR SwissLipids; SLP:000000928; -. [Q86XP1-2]
DR iPTMnet; Q86XP1; -.
DR PhosphoSitePlus; Q86XP1; -.
DR BioMuta; DGKH; -.
DR DMDM; 74762463; -.
DR EPD; Q86XP1; -.
DR jPOST; Q86XP1; -.
DR MassIVE; Q86XP1; -.
DR MaxQB; Q86XP1; -.
DR PaxDb; Q86XP1; -.
DR PeptideAtlas; Q86XP1; -.
DR PRIDE; Q86XP1; -.
DR ProteomicsDB; 5568; -.
DR ProteomicsDB; 70309; -. [Q86XP1-1]
DR ProteomicsDB; 70310; -. [Q86XP1-2]
DR ProteomicsDB; 70311; -. [Q86XP1-3]
DR Antibodypedia; 23454; 129 antibodies from 26 providers.
DR DNASU; 160851; -.
DR Ensembl; ENST00000261491.9; ENSP00000261491.4; ENSG00000102780.17. [Q86XP1-2]
DR Ensembl; ENST00000337343.9; ENSP00000337572.4; ENSG00000102780.17. [Q86XP1-1]
DR Ensembl; ENST00000379274.6; ENSP00000368576.3; ENSG00000102780.17. [Q86XP1-2]
DR Ensembl; ENST00000536612.3; ENSP00000445114.2; ENSG00000102780.17. [Q86XP1-3]
DR Ensembl; ENST00000628433.2; ENSP00000485809.1; ENSG00000102780.17. [Q86XP1-5]
DR GeneID; 160851; -.
DR KEGG; hsa:160851; -.
DR MANE-Select; ENST00000337343.9; ENSP00000337572.4; NM_178009.5; NP_821077.1.
DR UCSC; uc001uyl.3; human. [Q86XP1-1]
DR CTD; 160851; -.
DR DisGeNET; 160851; -.
DR GeneCards; DGKH; -.
DR HGNC; HGNC:2854; DGKH.
DR HPA; ENSG00000102780; Tissue enhanced (brain).
DR MIM; 604071; gene.
DR neXtProt; NX_Q86XP1; -.
DR OpenTargets; ENSG00000102780; -.
DR PharmGKB; PA27315; -.
DR VEuPathDB; HostDB:ENSG00000102780; -.
DR eggNOG; KOG1170; Eukaryota.
DR GeneTree; ENSGT00940000158106; -.
DR HOGENOM; CLU_001799_3_0_1; -.
DR InParanoid; Q86XP1; -.
DR OMA; FERAHTR; -.
DR OrthoDB; 43384at2759; -.
DR PhylomeDB; Q86XP1; -.
DR TreeFam; TF313104; -.
DR BRENDA; 2.7.1.107; 2681.
DR PathwayCommons; Q86XP1; -.
DR Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR SignaLink; Q86XP1; -.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 160851; 15 hits in 1081 CRISPR screens.
DR ChiTaRS; DGKH; human.
DR GenomeRNAi; 160851; -.
DR Pharos; Q86XP1; Tbio.
DR PRO; PR:Q86XP1; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q86XP1; protein.
DR Bgee; ENSG00000102780; Expressed in dorsal root ganglion and 174 other tissues.
DR ExpressionAtlas; Q86XP1; baseline and differential.
DR Genevisible; Q86XP1; HS.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0032093; F:SAM domain binding; IDA:UniProtKB.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; ISS:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IMP:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; IDA:BHF-UCL.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR CDD; cd00029; C1; 2.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Kinase;
KW Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1220
FT /note="Diacylglycerol kinase eta"
FT /id="PRO_0000239367"
FT DOMAIN 65..158
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 328..463
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT DOMAIN 1151..1214
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 175..225
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 247..298
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1218..1220
FT /note="PDZ-binding"
FT COMPBIAS 589..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019183"
FT VAR_SEQ 1148..1220
FT /note="VQKWGTEEVAAWLDLLNLGEYKDIFIRHDIRGAELLHLERRDLKDLGIPKVG
FT HVKRILQGIKELGRSTPQSEV -> GSGDTESGSCEANSPGN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12810723,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_019185"
FT VAR_SEQ 1191
FT /note="K -> KNTVGEKRDTKENGKHM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019186"
FT VARIANT 1201
FT /note="V -> A (in dbSNP:rs17646069)"
FT /id="VAR_033867"
FT MUTAGEN 1151
FT /note="W->G: Loss of homoligomerization and
FT heterooligomerization but not diacylglycerol kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:12810723"
FT CONFLICT 677
FT /note="I -> M (in Ref. 2; BAC05280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1220 AA; 134866 MW; F1BBF5B7FA582C97 CRC64;
MAGAGGQHHP PGAAGGAAAG AGAAVTSAAA SAGPGEDSSD SEAEQEGPQK LIRKVSTSGQ
IRTKTSIKEG QLLKQTSSFQ RWKKRYFKLR GRTLYYAKDS KSLIFDEVDL SDASVAEAST
KNANNSFTII TPFRRLMLCA ENRKEMEDWI SSLKSVQTRE PYEVAQFNVE HFSGMHNWYA
CSHARPTFCN VCRESLSGVT SHGLSCEVCK FKAHKRCAVR ATNNCKWTTL ASIGKDIIED
EDGVAMPHQW LEGNLPVSAK CAVCDKTCGS VLRLQDWKCL WCKTMVHTAC KDLYHPICPL
GQCKVSIIPP IALNSTDSDG FCRATFSFCV SPLLVFVNSK SGDNQGVKFL RRFKQLLNPA
QVFDLMNGGP HLGLRLFQKF DNFRILVCGG DGSVGWVLSE IDKLNLNKQC QLGVLPLGTG
NDLARVLGWG GSYDDDTQLP QILEKLERAS TKMLDRWSIM TYELKLPPKA SLLPGPPEAS
EEFYMTIYED SVATHLTKIL NSDEHAVVIS SAKTLCETVK DFVAKVEKTY DKTLENAVVA
DAVASKCSVL NEKLEQLLQA LHTDSQAAPV LPGLSPLIVE EDAVESSSEE SLGESKEQLG
DDVTKPSSQK AVKPREIMLR ANSLKKAVRQ VIEEAGKVMD DPTVHPCEPA NQSSDYDSTE
TDESKEEAKD DGAKESITVK TAPRSPDARA SYGHSQTDSV PGPAVAASKE NLPVLNTRII
CPGLRAGLAA SIAGSSIINK MLLANIDPFG ATPFIDPDLD SVDGYSEKCV MNNYFGIGLD
AKISLEFNNK REEHPEKCRS RTKNLMWYGV LGTRELLQRS YKNLEQRVQL ECDGQYIPLP
SLQGIAVLNI PSYAGGTNFW GGTKEDDIFA APSFDDKILE VVAIFDSMQM AVSRVIKLQH
HRIAQCRTVK ITIFGDEGVP VQVDGEAWVQ PPGIIKIVHK NRAQMLTRDR AFESTLKSWE
DKQKCDSGKP VLRTHLYIHH AIDLATEEVS QMQLCSQAAE ELITRICDAA TIHCLLEQEL
AHAVNACSHA LNKANPRCPE SLTRDTATEI AINVKALYNE TESLLVGRVP LQLESPHEER
VSNALHSVEV ELQKLTEIPW LYYILHPNED EEPPMDCTKR NNRSTVFRIV PKFKKEKVQK
QKTSSQPVQK WGTEEVAAWL DLLNLGEYKD IFIRHDIRGA ELLHLERRDL KDLGIPKVGH
VKRILQGIKE LGRSTPQSEV
