DGKG_MOUSE
ID DGKG_MOUSE Reviewed; 788 AA.
AC Q91WG7;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Diacylglycerol kinase gamma;
DE Short=DAG kinase gamma;
DE EC=2.7.1.107 {ECO:0000269|PubMed:32033984};
DE AltName: Full=88 kDa diacylglycerol kinase;
DE AltName: Full=Diglyceride kinase gamma;
DE Short=DGK-gamma;
GN Name=Dgkg; Synonyms=Dagk3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=32033984; DOI=10.1523/eneuro.0319-19.2020;
RA Tsumagari R., Kakizawa S., Kikunaga S., Fujihara Y., Ueda S., Yamanoue M.,
RA Saito N., Ikawa M., Shirai Y.;
RT "DGKgamma Knock-Out Mice Show Impairments in Cerebellar Motor Coordination,
RT LTD, and the Dendritic Development of Purkinje Cells through the Activation
RT of PKCgamma.";
RL ENeuro 7:0-0(2020).
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:32033984). 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 (PubMed:32033984). Has no apparent
CC specificity with regard to the acyl compositions of diacylglycerol (By
CC similarity). Specifically expressed in the cerebellum where it controls
CC the level of diacylglycerol which in turn regulates the activity of
CC protein kinase C gamma (PubMed:32033984). Through protein kinase C
CC gamma, indirectly regulates the dendritic development of Purkinje
CC cells, cerebellar long term depression and ultimately cerebellar motor
CC coordination (PubMed:32033984). {ECO:0000250|UniProtKB:P49619,
CC ECO:0000269|PubMed:32033984}.
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:32033984};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000269|PubMed:32033984};
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:0000250|UniProtKB:P49620};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000250|UniProtKB:P49620};
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:0000250|UniProtKB:P49620};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000250|UniProtKB:P49620};
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 -!- 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:0000250|UniProtKB:P49620};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000250|UniProtKB:P49620};
CC -!- ACTIVITY REGULATION: The activity is calcium-dependent (By similarity).
CC Requires phosphatidylserine for maximal activity (By similarity).
CC {ECO:0000250|UniProtKB:P49619, ECO:0000250|UniProtKB:P49620}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000269|PubMed:32033984}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P49620}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49619}. Cytoplasm,
CC cytoskeleton {ECO:0000250|UniProtKB:P49620}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus and cerebellar Purkinje
CC cells and weakly and diffusely expressed in the granule cells.
CC {ECO:0000269|PubMed:32033984}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice show impairments in
CC motor coordination, long-term depression/LTD and development of
CC Purkinje cells (PubMed:32033984). The level of phosphatidic acid in
CC synaptosomal membranes is significantly decreased (PubMed:32033984).
CC The number of branches, the total length of the dendrites and the
CC membrane capacitance of the distal dendritic region are significantly
CC lower (PubMed:32033984). {ECO:0000269|PubMed:32033984}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; BC015278; AAH15278.1; -; mRNA.
DR CCDS; CCDS28068.1; -.
DR RefSeq; NP_619591.1; NM_138650.2.
DR AlphaFoldDB; Q91WG7; -.
DR IntAct; Q91WG7; 1.
DR MINT; Q91WG7; -.
DR STRING; 10090.ENSMUSP00000087371; -.
DR iPTMnet; Q91WG7; -.
DR PhosphoSitePlus; Q91WG7; -.
DR EPD; Q91WG7; -.
DR MaxQB; Q91WG7; -.
DR PaxDb; Q91WG7; -.
DR PRIDE; Q91WG7; -.
DR ProteomicsDB; 277325; -.
DR Antibodypedia; 34852; 126 antibodies from 18 providers.
DR DNASU; 110197; -.
DR Ensembl; ENSMUST00000089925; ENSMUSP00000087371; ENSMUSG00000022861.
DR GeneID; 110197; -.
DR KEGG; mmu:110197; -.
DR UCSC; uc007ysg.2; mouse.
DR CTD; 1608; -.
DR MGI; MGI:105060; Dgkg.
DR VEuPathDB; HostDB:ENSMUSG00000022861; -.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000156768; -.
DR InParanoid; Q91WG7; -.
DR OMA; ALCKYTV; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; Q91WG7; -.
DR TreeFam; TF313104; -.
DR Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR BioGRID-ORCS; 110197; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Dgkg; mouse.
DR PRO; PR:Q91WG7; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q91WG7; protein.
DR Bgee; ENSMUSG00000022861; Expressed in subiculum and 109 other tissues.
DR ExpressionAtlas; Q91WG7; baseline and differential.
DR Genevisible; Q91WG7; MM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS: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; IMP:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISO:MGI.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IMP:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IMP:UniProtKB.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; IMP:UniProtKB.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP:UniProtKB.
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; IMP:UniProtKB.
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 ATP-binding; Calcium; Cytoplasm; Cytoskeleton; Kinase; Lipid metabolism;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..788
FT /note="Diacylglycerol kinase gamma"
FT /id="PRO_0000218460"
FT DOMAIN 172..207
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 217..252
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 427..561
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 268..318
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 333..380
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 83..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 788 AA; 88523 MW; 969298DFD144F5DF CRC64;
MSEEQWVSLS SEEFDQLQKY SEYSSKKIKD VLAEFNEGGS LRQYDPHKPI SYDVFKLFMR
AYLEVDLPQP LSTHLFLAFS QKPRQETPDH PKEGASSSEP NVSDYNSDNA AKADEACAPD
TESKTTKTQA PSKELEAAAP WEDPGALASS SDAPVVYLKD VVCYLSLMET GRPQDKLEFM
FRLYDSDENG LLDQAEMDQI VSQMLHVAQY LEWDPTELRP ILKEMLQGMD YDKDGFVSLQ
EWINGGMTTI PLLVLLGMDD SGSKGDGRHA WTLKHFKKPT YCNFCRAMLM GVGKQGLCCI
YCKYTVHQRC VSKTIHGCVK TNSKAKRSGE VMQHAWVEGN SSVKCDRCHK SIKCYQSVTA
RHCVWCRMTF HRKCELSTVC DGGELKDHIL LPTSICPVSG DRQGGKSDGS VAAKGELVTQ
YKIIPSPGTH PLLVLVNPKS GGRQGERILR KFHYLLNPEQ VFNLDNGGPT PGLNFFHDTP
DFRVLACGGD GTVGWILDCI DKANFTKHPP VAVLPLGTGN DLARCLRWGG GYEGGSLTKI
LKEIEQSPLV MLDRWYLEVM PREEVENGDQ VPYNIMNNYF SIGVDASIAH RFHMMREKHP
EKFNSRMKNK LWYFEFGTSE TFAATCKKLH DHIELECDGV EVDLSNIFLE GIAILNIPSM
YGGTNLWGET KKNRAVIRES RKSVTDPKEL KCCVQDLSDQ LLEVVGLEGA MEMGQIYTGL
KSAGRRLAQC SSVTIRTNKL LPMQVDGEPW MQPQCTIKIT HKNQAPMMMG PPQKSSFFSL
RRKSRSKD
