ID A0A2K6D0Y9_MACNE Unreviewed; 1100 AA.
AC A0A2K6D0Y9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Diacylglycerol kinase {ECO:0000256|RuleBase:RU361128};
DE Short=DAG kinase {ECO:0000256|RuleBase:RU361128};
DE EC=2.7.1.107 {ECO:0000256|RuleBase:RU361128};
GN Name=DGKH {ECO:0000313|Ensembl:ENSMNEP00000029579.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000029579.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000029579.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023371};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000256|ARBA:ARBA00023371};
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:0000256|RuleBase:RU361128};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000256|ARBA:ARBA00005175}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR AlphaFoldDB; A0A2K6D0Y9; -.
DR Ensembl; ENSMNET00000053984.1; ENSMNEP00000029579.1; ENSMNEG00000038131.1.
DR GeneTree; ENSGT00940000158106; -.
DR OMA; VEGNLAM; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000038131; Expressed in lung and 12 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0030168; P:platelet activation; IEA:UniProt.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd20848; C1_DGKeta_rpt1; 1.
DR CDD; cd20894; C1_DGKeta_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
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; 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; PF07647; SAM_2; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..22
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 39..89
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 111..162
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 192..327
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT DOMAIN 1015..1094
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 445..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 122436 MW; CEE27A58EFBC4392 CRC64;
MLCAENRKEM EDWISSLKSV QTREPYEVAQ FNVEHFSGMH NWYACSHARP TFCNVCRESL
SGVTSHGLSC EVCKFKAHKR CAVRATNNCK WTTLASIGKD IIEDEDGVAM PHQWLEGNLP
VSAKCAVCDK TCGSVLRLQD WKCLWCKTMV HTACKDLYHP ICPLGQCKVS IIPPIALNST
DSDGFCRATF SFCVSPLLVF VNSKSGDNQG VKFLRRFKQL LNPAQVFDLM NGGPHLGLRL
FQKFDNFRIL VCGGDGSVGW VLSEIDKLNL NKQCQLGVLP LGTGNDLARV LGWGGSYDDD
TQLPQILEKL ERASTKMLDR WSIMTYELKL PPKASLLPGP PEASEEFYMT IYEDSVATHL
TKILNSDEHA VVISSAKTLC ETVKDFVAKV EKTYDKTLEN AVVADAVASK CSVLNEKLEQ
LLQALHTDSQ AAPVLPGLSP LIVEEDAVES SSEESLGESK EQLVDDVTKP SSQKAVKPRE
IMLRANSLKK AVRQVIEEAG KVMDDPTVHP CEPANQSSDY DSTETDESKE EAKDDGSKES
LTVKTAPRSP DARASHGHSQ TDSVPGPAVA ASKENLPVLN TRIICPGLRA GLAASIAGSS
IINKMLLANI DPFGATPFID PDPDSVDGYS EKCVMNNYFG IGLDAKISLE FNNKREEHPE
KCRSRTKNLM WYGVLGTREL LQRSYKNLEQ RVQLECDGQY IPLPSLQGIA VLNIPSYAGG
TNFWGGTKED DIFAAPSFDD KILEVVAIFD SMQMAVSRVI KLQHHRIAQC RTVKITIFGD
EGVPVQVDGE AWVQPPGIIK IVHKNRAQML TRDRAFESTL KSWEDKQKCD SGKPVLRTHL
YIHHAIDLAT EEVSQMQLCS QAAEELITRI CDAATIHCLL EQELAHAVNA CSHALNKANP
RCPESLTRDT ATEIAINVKA LYNETESLLV GRVPLQLESP HEERVSNALH SVEVELQKLT
EIPWLYYILH PNEDEEPPMD CTKRNNRSTV FRIVPKFKKE KVQKQKTSSQ PVQKWGTEEV
AAWLDLLNLG EYKDIFIRHD IRGAELLHLE RRDLKNTVGE RRDTKENGKH MDLGIPKVGH
VKRILQGIKE LGRSTPQSEV
//
