DGKH_MESAU
ID DGKH_MESAU Reviewed; 1154 AA.
AC Q64398;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Diacylglycerol kinase eta {ECO:0000305};
DE Short=DAG kinase eta;
DE EC=2.7.1.107 {ECO:0000269|PubMed:8702685};
DE AltName: Full=130 kDa diacylglycerol kinase;
DE AltName: Full=Diglyceride kinase eta;
DE Short=DGK-eta;
GN Name=DGKH;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Smooth muscle;
RX PubMed=8702685; DOI=10.1074/jbc.271.33.19781;
RA Klauck T.M., Xu X., Mousseau B., Jaken S.;
RT "Cloning and characterization of a glucocorticoid-induced diacylglycerol
RT kinase.";
RL J. Biol. Chem. 271:19781-19788(1996).
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:8702685). 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 (Probable). Plays a key role in promoting
CC cell growth (By similarity). Activates the Ras/B-Raf/C-Raf/MEK/ERK
CC signaling pathway induced by EGF. Regulates the recruitment of RAF1 and
CC BRAF from cytoplasm to membranes and their heterodimerization (By
CC similarity). {ECO:0000250|UniProtKB:Q86XP1, ECO:0000269|PubMed:8702685,
CC 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:8702685};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:8702685};
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:8702685};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:8702685};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:8702685}.
CC -!- SUBUNIT: Interacts with RAF1 and BRAF. {ECO:0000250|UniProtKB:Q86XP1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86XP1}. Cell
CC membrane {ECO:0000250|UniProtKB:Q86XP1}. Note=Translocated from the
CC cytoplasm to endosomes in response to stress stimuli.
CC {ECO:0000250|UniProtKB:Q86XP1}.
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues
CC (PubMed:8702685). Most abundant in the brain and testis; also found in
CC lung, spleen, and prostate (at protein level) (PubMed:8702685).
CC {ECO:0000269|PubMed:8702685}.
CC -!- INDUCTION: By glucocorticoids. {ECO:0000269|PubMed:8702685}.
CC -!- PTM: Phosphorylated. Phosphorylation does not inhibit catalytic
CC activity. {ECO:0000250|UniProtKB:Q86XP1}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; U59429; AAC52714.1; -; mRNA.
DR AlphaFoldDB; Q64398; -.
DR SMR; Q64398; -.
DR STRING; 10036.XP_005070993.1; -.
DR eggNOG; KOG1170; Eukaryota.
DR BRENDA; 2.7.1.107; 3239.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA: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:0046339; P:diacylglycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0046834; P:lipid phosphorylation; IDA:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00029; C1; 2.
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 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 SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS50003; PH_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 ATP-binding; Cell membrane; Cytoplasm; Kinase; Lipid metabolism; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1154
FT /note="Diacylglycerol kinase eta"
FT /id="PRO_0000218463"
FT DOMAIN 59..152
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 322..457
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 169..219
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 241..292
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 126818 MW; 0507DEECF64BC5CB CRC64;
MAGAGYQHHP PGGAAVGTSA VSPTAAGPGE DSSDSEAEQG GPQKLIRKVS TSGQIRTKTS
IKEGQLLKQT SSFQRWKKRY FKLRGRTLYY AKDSKSLIFD EVDLSDASVA EASTKNANNS
FTIITPFRRL MLCAENRKEM EDWISSLKSV QSREPYEVAQ FNVEHFSGMH NWYACSHARP
TFCNVCRESL SGVTSHGLSC EVCKFKAHKR CAVRATNNCK WTTLASIGKD IIEDEDGVAM
PHQWLEGNLP VSAKCAVCDK TCGSVLRLQD WKCLWCKAMV HTACKDLYHP VCPLGQCKVS
IIPPIALNST DSDGFCRATF SFCVSPLLVF VNSKSGDNQG VKFLRRFKQL LNPAQVFDLM
NGGPHLGLRL FQKFDNFRIL VCGGDGSVGW VLSEIDKLNL NKQCQLGVLP LGTGNDLARV
LGWGGSYDDD TQLPQILEKL ERASTKMLDR WSIMTYELKL PAKASLLPEP PEASGGFYMT
IYEDSVANHL TKILNSDEHA VVISSAKILC ETVKDFVAKV EKAQDKTLEN TVVAEAVANK
CSVLNEKLEQ LLQALHADAQ ASRVPPGVGP AIPEEDAVES SSEESLGESK DQLVNDIAKP
SSQKAVKPRE IMLRANSLKK AVRQVIEEAG KVMDEQTVQP CEPVSPSCDY DSPEADDSKD
NDTKESPAAK STSQAPEAQA IRGHFQTDSV AGSAMATTKE NLPVLNTRII CPGLRAGLAA
SIAGSSIINK MLLANIDPFG ATPFIDPDLD SLDGYSEKCV MNNYFGIGLD AKISLEFNNK
REEHPEKCRS RTKNLMWYGV LGTRELLQRS YKNLEQRVQL ECDGQYIPLP SLQGIAVLNI
PSYAGGTNFW GGTKEDDIFA APSFDDKILE VVAVFDSVQM AVSRVIKLQH HRIAQCRTVK
ITIFGDEGVP VQVDGEAWVQ PPGIIKIVHK NRAQMLTRDR AFESTLKSWE DKQKCDSGKP
VLRTNLYIHP AADLATEEVS QMRLCSQAAE ELITRICDAA TIHCLLGAGT GSSVNACSHA
LNKANPRFPE SLTRDTATEI AINVKALYNE TESLLVGRVP LQLESPHEER VSSALHSVEV
ELQKLTEIPW LYYILRPNED EEPPMDCTKR NSKSTVFRIV PKFKMEKAQK QKTSSQPGPG
DTESGSYEAN SPGN
