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 27-MAR-2024, entry version 167. 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; 36. 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 CPTAC; non-CPTAC-5653; -. DR EPD; Q86XP1; -. DR jPOST; Q86XP1; -. DR MassIVE; Q86XP1; -. DR MaxQB; Q86XP1; -. DR PaxDb; 9606-ENSP00000337572; -. DR PeptideAtlas; Q86XP1; -. DR ProteomicsDB; 5568; -. DR ProteomicsDB; 70309; -. [Q86XP1-1] DR ProteomicsDB; 70310; -. [Q86XP1-2] DR ProteomicsDB; 70311; -. [Q86XP1-3] DR Pumba; Q86XP1; -. DR Antibodypedia; 23454; 149 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 AGR; HGNC:2854; -. DR CTD; 160851; -. DR DisGeNET; 160851; -. DR GeneCards; DGKH; -. DR HGNC; HGNC:2854; DGKH. DR HPA; ENSG00000102780; Low tissue specificity. 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; VEGNLAM; -. DR OrthoDB; 4642163at2759; -. 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 1162 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 176 other cell types or tissues. DR ExpressionAtlas; Q86XP1; baseline and differential. 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:ATP-dependent 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: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; cd20848; C1_DGKeta_rpt1; 1. DR CDD; cd20894; C1_DGKeta_rpt2; 1. DR CDD; cd13274; PH_DGK_type2; 1. DR CDD; cd09576; SAM_DGK-eta; 1. DR Gene3D; 2.60.200.40; -; 1. DR Gene3D; 3.30.60.20; -; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR InterPro; IPR017438; ATP-NAD_kinase_N. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR047480; C1_DGKeta_rpt2. 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; DIACYLGLYCEROL KINASE; 1. DR PANTHER; PTHR11255:SF37; DIACYLGLYCEROL KINASE ETA; 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; SSF57889; Cysteine-rich domain; 2. DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. 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. DR Genevisible; Q86XP1; HS. 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 //