DGKG_HUMAN
ID DGKG_HUMAN Reviewed; 791 AA.
AC P49619; B2RAH4; Q2M1H4; Q5FWG1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Diacylglycerol kinase gamma;
DE Short=DAG kinase gamma;
DE EC=2.7.1.107 {ECO:0000269|PubMed:8034597};
DE AltName: Full=Diglyceride kinase gamma;
DE Short=DGK-gamma;
GN Name=DGKG; Synonyms=DAGK3;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, PATHWAY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND VARIANT LYS-316.
RC TISSUE=Liver;
RX PubMed=8034597; DOI=10.1016/s0021-9258(17)32336-0;
RA Kai M., Sakane F., Imai S., Wada I., Kanoh H.;
RT "Molecular cloning of a diacylglycerol kinase isozyme predominantly
RT expressed in human retina with a truncated and inactive enzyme expression
RT in most other human cells.";
RL J. Biol. Chem. 269:18492-18498(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-316.
RX PubMed=10071200; DOI=10.1007/s004390050917;
RA Stoehr H., Klein J., Gehrig A., Koehler M.R., Jurklies B., Kellner U.,
RA Leo-Kottler B., Schmid M., Weber B.H.F.;
RT "Mapping and genomic characterization of the gene encoding diacylglycerol
RT kinase gamma (DAGK3): assessment of its role in dominant optic atrophy
RT (OPA1).";
RL Hum. Genet. 104:99-105(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-142
RP AND LYS-316.
RC TISSUE=Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP SER-142 AND LYS-316.
RC TISSUE=Lymph;
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 [6]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-706.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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:8034597). Thereby, acts as a
CC central switch between the signaling pathways activated by these second
CC messengers with different cellular targets and opposite effects in
CC numerous biological processes (By similarity). Has no apparent
CC specificity with regard to the acyl compositions of diacylglycerol
CC (PubMed:8034597). Specifically expressed in the cerebellum where it
CC controls the level of diacylglycerol which in turn regulates the
CC activity of protein kinase C gamma. Through protein kinase C gamma,
CC indirectly regulates the dendritic development of Purkinje cells,
CC cerebellar long term depression and ultimately cerebellar motor
CC coordination (By similarity). {ECO:0000250|UniProtKB:Q91WG7,
CC ECO:0000269|PubMed:8034597}.
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:8034597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:8034597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:8034597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000305|PubMed:8034597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:8034597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000305|PubMed:8034597};
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:8034597};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:8034597};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP =
CC 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P49620};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340;
CC Evidence={ECO:0000250|UniProtKB:P49620};
CC -!- ACTIVITY REGULATION: The activity is calcium-dependent (By similarity).
CC Requires phosphatidylserine for maximal activity (PubMed:8034597).
CC {ECO:0000250|UniProtKB:P49620, ECO:0000269|PubMed:8034597}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:8034597}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8034597}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:8034597}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P49620}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=P49619-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P49619-2; Sequence=VSP_001267;
CC Name=3;
CC IsoId=P49619-3; Sequence=VSP_039922;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in retina and in a much
CC lesser extent in the brain. Other tissues contain extremely low levels
CC of DGK-gamma.
CC -!- MISCELLANEOUS: [Isoform 2]: May be inactive. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; D26135; BAA05132.1; -; mRNA.
DR EMBL; AF020945; AAC04686.1; -; Genomic_DNA.
DR EMBL; AF020922; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020923; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020924; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020925; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020926; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020927; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020928; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020929; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020930; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020931; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020932; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020933; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020934; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020935; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020936; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020937; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020938; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020939; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020940; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020941; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020942; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020943; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AF020944; AAC04686.1; JOINED; Genomic_DNA.
DR EMBL; AK314192; BAG36871.1; -; mRNA.
DR EMBL; AC007917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089411; AAH89411.1; -; mRNA.
DR EMBL; BC112363; AAI12364.1; -; mRNA.
DR CCDS; CCDS3274.1; -. [P49619-1]
DR CCDS; CCDS43181.1; -. [P49619-3]
DR CCDS; CCDS43182.1; -. [P49619-2]
DR PIR; A53691; A53691.
DR RefSeq; NP_001074213.1; NM_001080744.1. [P49619-2]
DR RefSeq; NP_001074214.1; NM_001080745.1. [P49619-3]
DR RefSeq; NP_001337.2; NM_001346.2. [P49619-1]
DR AlphaFoldDB; P49619; -.
DR BioGRID; 107978; 24.
DR IntAct; P49619; 3.
DR STRING; 9606.ENSP00000265022; -.
DR BindingDB; P49619; -.
DR ChEMBL; CHEMBL1075157; -.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR DrugBank; DB00144; Phosphatidyl serine.
DR SwissLipids; SLP:000000923; -.
DR SwissLipids; SLP:000000938; -. [P49619-1]
DR iPTMnet; P49619; -.
DR PhosphoSitePlus; P49619; -.
DR BioMuta; DGKG; -.
DR DMDM; 311033457; -.
DR EPD; P49619; -.
DR MassIVE; P49619; -.
DR PaxDb; P49619; -.
DR PeptideAtlas; P49619; -.
DR PRIDE; P49619; -.
DR ProteomicsDB; 56029; -. [P49619-1]
DR ProteomicsDB; 56030; -. [P49619-2]
DR ProteomicsDB; 56031; -. [P49619-3]
DR Antibodypedia; 34852; 126 antibodies from 18 providers.
DR DNASU; 1608; -.
DR Ensembl; ENST00000265022.8; ENSP00000265022.3; ENSG00000058866.15. [P49619-1]
DR Ensembl; ENST00000344484.8; ENSP00000339777.4; ENSG00000058866.15. [P49619-2]
DR Ensembl; ENST00000382164.8; ENSP00000371599.4; ENSG00000058866.15. [P49619-3]
DR GeneID; 1608; -.
DR KEGG; hsa:1608; -.
DR MANE-Select; ENST00000265022.8; ENSP00000265022.3; NM_001346.3; NP_001337.2.
DR UCSC; uc003fqa.4; human. [P49619-1]
DR CTD; 1608; -.
DR DisGeNET; 1608; -.
DR GeneCards; DGKG; -.
DR HGNC; HGNC:2853; DGKG.
DR HPA; ENSG00000058866; Tissue enhanced (brain).
DR MIM; 601854; gene.
DR neXtProt; NX_P49619; -.
DR OpenTargets; ENSG00000058866; -.
DR PharmGKB; PA27314; -.
DR VEuPathDB; HostDB:ENSG00000058866; -.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000156768; -.
DR HOGENOM; CLU_003770_1_0_1; -.
DR InParanoid; P49619; -.
DR OMA; ALCKYTV; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; P49619; -.
DR TreeFam; TF313104; -.
DR BRENDA; 2.7.1.107; 2681.
DR PathwayCommons; P49619; -.
DR Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR SABIO-RK; P49619; -.
DR SignaLink; P49619; -.
DR SIGNOR; P49619; -.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 1608; 11 hits in 1064 CRISPR screens.
DR ChiTaRS; DGKG; human.
DR GeneWiki; DGKG; -.
DR GenomeRNAi; 1608; -.
DR Pharos; P49619; Tbio.
DR PRO; PR:P49619; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P49619; protein.
DR Bgee; ENSG00000058866; Expressed in cerebellar cortex and 106 other tissues.
DR ExpressionAtlas; P49619; baseline and differential.
DR Genevisible; P49619; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IDA:UniProtKB.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0050773; P:regulation of dendrite development; IEA:Ensembl.
DR CDD; cd00029; C1; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.110; -; 2.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_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; PF14513; DAG_kinase_N; 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 SMART; SM00054; EFh; 2.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
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; Calcium; Cytoplasm; Cytoskeleton;
KW Kinase; Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..791
FT /note="Diacylglycerol kinase gamma"
FT /id="PRO_0000218459"
FT DOMAIN 175..210
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 220..255
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 430..564
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 271..321
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 336..385
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 82..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 334..372
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039922"
FT VAR_SEQ 451..475
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001267"
FT VARIANT 142
FT /note="T -> S (in dbSNP:rs1004588)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_020259"
FT VARIANT 316
FT /note="R -> K (in dbSNP:rs2193587)"
FT /evidence="ECO:0000269|PubMed:10071200,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8034597"
FT /id="VAR_024430"
FT VARIANT 370
FT /note="R -> W (in dbSNP:rs3213770)"
FT /id="VAR_020260"
FT VARIANT 706
FT /note="E -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036119"
FT CONFLICT 271
FT /note="R -> G (in Ref. 1; BAA05132 and 2; AAC04686)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 791 AA; 89124 MW; A1382CF1B2CD7362 CRC64;
MGEERWVSLT PEEFDQLQKY SEYSSKKIKD ALTEFNEGGS LKQYDPHEPI SYDVFKLFMR
AYLEVDLPQP LSTHLFLAFS QKPRHETSDH PTEGASNSEA NSADTNIQNA DNATKADEAC
APDTESNMAE KQAPAEDQVA ATPLEPPVPR SSSSESPVVY LKDVVCYLSL LETGRPQDKL
EFMFRLYDSD ENGLLDQAEM DCIVNQMLHI AQYLEWDPTE LRPILKEMLQ GMDYDRDGFV
SLQEWVHGGM TTIPLLVLLG MDDSGSKGDG RHAWTMKHFK KPTYCNFCHI MLMGVRKQGL
CCTYCKYTVH ERCVSRNIPG CVKTYSKAKR SGEVMQHAWV EGNSSVKCDR CHKSIKCYQS
VTARHCVWCR MTFHRKCELS TLCDGGELRD HILLPTSICP ITRDRPGEKS DGCVSAKGEL
VMQYKIIPTP GTHPLLVLVN PKSGGRQGER ILRKFHYLLN PKQVFNLDNG GPTPGLNFFR
DTPDFRVLAC GGDGTVGWIL DCIDKANFAK HPPVAVLPLG TGNDLARCLR WGGGYEGGSL
TKILKDIEQS PLVMLDRWHL EVIPREEVEN GDQVPYSIMN NYFSIGVDAS IAHRFHVMRE
KHPEKFNSRM KNKLWYFEFG TSETFAATCK KLHDHIELEC DGVGVDLSNI FLEGIAILNI
PSMYGGTNLW GENKKNRAVI RESRKGVTDP KELKFCVQDL SDQLLEVVGL EGAMEMGQIY
TGLKSAGRRL AQCASVTIRT NKLLPMQVDG EPWMQPCCTI KITHKNQAPM MMGPPQKSSF
FSLRRKSRSK D
