ID A0A2K5E557_AOTNA Unreviewed; 1164 AA.
AC A0A2K5E557;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ENSANAP00000028331.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000028331.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000028331.1}
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 RefSeq; XP_012332204.1; XM_012476781.1.
DR AlphaFoldDB; A0A2K5E557; -.
DR Ensembl; ENSANAT00000046357.1; ENSANAP00000028331.1; ENSANAG00000031866.1.
DR GeneID; 105734077; -.
DR CTD; 160851; -.
DR GeneTree; ENSGT00940000158106; -.
DR OrthoDB; 4642163at2759; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000233020; Unplaced.
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 CDD; cd13274; PH_DGK_type2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; 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; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
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 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:UP000233020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 65..158
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 175..225
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 247..298
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 328..463
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1164 AA; 128183 MW; B961472AEAAF031F CRC64;
MAGAGGQHHP PGAAGGAAAG AGAAVTAAAS SAGPGEDSSD SEAEQEGPQK LIRKVSTSGQ
IRTKTSIKEG QLLKQTSSFQ RWKKRYFKLR GRTLYYAKDS KSLIFDEVDL SDASVAEAST
KNANNSFTII TPFRRLMLCA ENRKEMEDWI SSLKSVQTRE PYEVAQFNVE HFSGMHNWYA
CSHARPTFCN VCRESLSGVT SHGLSCEVCK FKAHKRCAVR ATNNCKWTTL ASIGKDIIED
EDGLAMPHQW LEGNLPVSAK CAVCDKTCGS VLRLQDWKCL WCKTMVHTAC KDLYHPICPL
GQCKVSIIPP IALNSTDSDG FCRATFSFCV SPLLVFVNSK SGDNQGVKFL RRFKQLLNPA
QVFDLMNGGP HLGLRLFQKF DNFRILVCGG DGSVGWVLSE IDKLNLNKQC QLGVLPLGTG
NDLARVLGWG GSYDDDTQLP QILEKLERAS TKMLDRWSIM TYELKLPPKA SLLPGPPEAS
EEFYMTIYED SVATHLTKIL NSDEHAVVIS SAKTLCETVK DFVAKVEKMY DKTLENAVVA
DAVASKCSVL NEKLEQLLQA LHTDSEAAPV LPGLSPLIVE EDAVESSSEE SLGESKEQLV
DDVTKPSSQK AVKPREIMLR ANSLKKAVRQ VIEEAGKVMD DPTVHPCEPA NQSSDYDSTE
TDESKEETKD DGAKESLTVK TTPRSPDARA SHGHSQIDSL PGPAVAASKE NLPVLNTRII
CPGLRAGLAA SIAGSSIINK MLLANIDPFG ATPFIDPDPD SVDGYSEKCV MNNYFGIGLD
AKISLEFNNK REEHPEKCRS RTKNLMWYGV LGTRELLQRS YKNLEQRVQL ECDGQYIPLP
SLQGIAVLNI PSYAGGTNFW GGTKEDDIFA APSFDDKILE VVAIFDSMQM AVSRVIKLQH
HRIAQCRTVK ITIFGDEGVP VQVDGEAWVQ PPGIIKIVHK NRAQMLTRDR AFESTLKSWE
DKQKCDSGKP VLRTHLYIHH AIDLATEEVS QMQLCSQAAE ELITRICDAA TIHCLLEQEL
AHAVNACSHA LNKANPRCPE SLTRDTATEI AINVKALYNE TESLLVGRVP LQLESPHEER
VSNALHSVEV ELQKLTEIPW LYYILHPNED EEPPIDCTKR NNRSTVFRIV PKFKKEKLQK
QKTSSQPGPG DTESGPCEAN SPGN
//
