DGKH_DROME
ID DGKH_DROME Reviewed; 1895 AA.
AC A8JQ65; Q86NT9;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Diacylglycerol kinase eta {ECO:0000250|UniProtKB:Q86XP1};
DE Short=DAG kinase eta {ECO:0000250|UniProtKB:Q86XP1};
DE EC=2.7.1.107;
GN ORFNames=CG34384;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:ABW08617.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABW08617.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAO39647.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1080-1895.
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates diacylglycerol (DAG) to generate phosphatidic
CC acid (PA). {ECO:0000250|UniProtKB:Q86XP1}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86XP1}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO39647.1; Type=Miscellaneous discrepancy; Note=Frameshift and deletion of residues 1685-1699.; Evidence={ECO:0000305};
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DR EMBL; AE014297; ABW08617.1; -; Genomic_DNA.
DR EMBL; BT003643; AAO39647.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001097704.1; NM_001104234.4.
DR AlphaFoldDB; A8JQ65; -.
DR SMR; A8JQ65; -.
DR BioGRID; 624993; 1.
DR STRING; 7227.FBpp0293459; -.
DR PaxDb; A8JQ65; -.
DR EnsemblMetazoa; FBtr0112625; FBpp0111537; FBgn0085413.
DR GeneID; 5740362; -.
DR KEGG; dme:Dmel_CG34384; -.
DR UCSC; CG34384-RA; d. melanogaster.
DR FlyBase; FBgn0085413; CG34384.
DR VEuPathDB; VectorBase:FBgn0085413; -.
DR eggNOG; KOG1170; Eukaryota.
DR GeneTree; ENSGT00940000167989; -.
DR InParanoid; A8JQ65; -.
DR Reactome; R-DME-114508; Effects of PIP2 hydrolysis.
DR BioGRID-ORCS; 5740362; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 5740362; -.
DR PRO; PR:A8JQ65; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0085413; Expressed in brain and 7 other tissues.
DR ExpressionAtlas; A8JQ65; baseline and differential.
DR Genevisible; A8JQ65; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; ISS:FlyBase.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IBA:GO_Central.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; ISS:FlyBase.
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; 2.
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; PF00536; SAM_1; 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; 2.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1895
FT /note="Diacylglycerol kinase eta"
FT /id="PRO_0000375987"
FT DOMAIN 82..175
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 349..485
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT DOMAIN 1832..1895
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 195..245
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 267..318
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1192..1215
FT /note="Missing (in Ref. 3; AAO39647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1895 AA; 211659 MW; C152645B61070314 CRC64;
MAHLKLDTLH VQRSPRGSRR SSPSSGRSSA CSSGSISPVP IIPIISISHD GDESESESEI
ETEPARLFQR RMSTKCTNNL AAIIKEGFLL KHTWSFQRWR RRYFRLKRNM LFYAKDEKCD
VFDDIDLSDL CYFECGIKNV NHSFQIITPT RSLVLCAESR REMEDWLGSL KTATAPQRPR
GDSFLIEQHD ILSNHHHWYA TSHARPTYCN VCRDALSGVT SHGLSCEVCK CKVHKRCAAK
SIANCKWTTL ASVGKDIIEQ ADGIIMPHQW MEGNLPVSSM CAVCKKTCGS VLRLQDWRCL
WCRATVHVAC RPQMAVACPI GPAKLSVVPP TSVHSISTDD AWDVASPKGN FSPLLVFVNS
KSGDNQGVKF LRRFKQLLNP AQVFDLISTG PSLGLRLFRH FEMFRILVCS GDGSVGWVLS
EIDRFNMHKQ CQVAVMPLGT GNDLARVLGW GSSCDDDTHL PQILERYESA STKMLDRWSI
MVFEKAIPVP KTPKMSISTE QEAMLTGMVT SANHHLRFIV ETNDTQTLIR STRNLCDTVD
DLVCRISEHH KDDEQLAVKC DILRQKLNML LDALQEEEIG AHSGDDLIAT IRSLIARSIP
VTPGSNAYLL NPNISIEKTE KDQINTKERR NSRSLRSSEK EALQCRANSV KRAIYNVVEH
SEPGRPKRYQ RKLSITPFEA LKLPTASGES TPCTSPLPII PPINIISPTM ETSRLTCISP
LPDTRRDSVD ENFFNSINLP APRQFADSRR SSGVEVIQEI EEGANGETVY RKSRMSLTGG
ANIDDAGNRL SPCSDAGENT PTERKVDFLR VPIHTGEPIV DPLCDYRPHE VFERTYYMTR
EMDKGKEKDK EKDKPVEIDK EKDTCVEKEG SMPAEKLVHT CNLQVPGVVV TPNPQNVYSS
ASITIIDTDA QTTTEQSSSD DLGGEASDVL SAISNEECSV ASEIFDKQDA GQTVGDIIQN
MDASNFTHID SPETSDETEA MPGESIMDDI SSVLGHDITY ALQDNTLTDD TTTLCSEHAG
PPKPPRKKSL SALSRTQAHP RRRNSSPPRM ARLARMDSDD NPQQFGFENI VFEIDNRCDD
QKMREPPRYC SLAQFVEGND IARQSFKQLM LEQHRGGDND SDYPEHEQTP TNKGANLLAT
TSEDELSTQT AIKIEIQDID ATVRNLNSSM KPNTILTTST SPTKKSGHGQ DVKRITFDES
CKKESFDDVN PNYPQISVVV RPPTPLRGDC IKPTVSLLPV SSGGAMTVSM TCSGMLGVRA
MNASEIRRHS SHAPGLAVRE FDKDKDRRHS GFNPNQLTLD PEHARFLSSS PAASRRISCG
SLFKPNEALP NLQTLKGSKS SLFMGSTLFG FDHLASAEKD KEEKSGKDKE KTPTDETNRK
LPIINPLVRL PNWPNLANGG GFISKCLLAN ADTLCAAVSP LMDPDETLLA GYHEKCVMNN
YFGIGIDAKI SLDFHNKREE HPEKCRSRAR NYMWYGVLGS KQLLQKTCKN LEQRVQLECD
GQRIPLPELQ GIVILNIPSF MGGTNFWGSS KKDDIFLPPS FDDRVLEVVA VFGSVQMAAS
RLINLQHHRI AQCQSVQINI LGDEEIPIQV DGEAWLQPPG MIRILHKNRV QMLCRNRSLE
LSLKSWQEKQ RQHSISIQRD ASSTASEHAN STDEVISERE CYVLLNFIEA VSSLVKWVKF
LIISHPALQH DLYEVACRAS EALESIHPQG KLLEGPSLRT KLVEVIDSSR QLYDDACTLL
RDRGHSLILR EDLETKLSAA LANMEMELKK CSVQKCIDGK LRAYFNVLAP NEESDGRRKS
RPFWVRLRSG STAGQQAFKP PLTNTREAAN NWSVNEVVTW LETMQLSEYV DSFLKNDIRG
KELLTLGRRD LKDLGVVKVG HVKRILQAIK DLSEN
