ID W5PBJ7_SHEEP Unreviewed; 1154 AA.
AC W5PBJ7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:ENSOARP00000007808.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000007808.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000007808.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000007808.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000007808.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AMGL01013580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01013581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5PBJ7; -.
DR SMR; W5PBJ7; -.
DR STRING; 9940.ENSOARP00000007808; -.
DR PaxDb; 9940-ENSOARP00000007808; -.
DR Ensembl; ENSOART00000007925.1; ENSOARP00000007808.1; ENSOARG00000007286.1.
DR eggNOG; KOG1170; Eukaryota.
DR HOGENOM; CLU_001799_3_0_1; -.
DR OMA; VEGNLAM; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000002356; Chromosome 10.
DR Bgee; ENSOARG00000007286; Expressed in testis and 49 other cell types or tissues.
DR ExpressionAtlas; W5PBJ7; baseline.
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: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 CDD; cd09576; SAM_DGK-eta; 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 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; IPR011993; PH-like_dom_sf.
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; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 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; 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; 1.
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:UP000002356};
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..94
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 111..161
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 183..234
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 264..399
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT DOMAIN 1085..1148
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 518..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 128958 MW; 1061F2C489E5E51A CRC64;
TSIKEGQLLK QTSSFQRWKK RYFKLRGRTL YYAKDSKSLI FDEVDLSDAS VAEASTKNAN
NSFTIITPFR RLMLCAENRK EMEDWISSLK SVQTREPYEV AQFNVEHFSG MHNWYACSHA
RPTFCNVCRE SLSGVTSHGL SCEVCKFKAH KRCAVRATNN CKWTTLASVG KDIIENEDGV
AMPHQWLEGN LPVSAKCAVC DKTCGSVLRL QDWRCLWCRA MVHTACKDLY HPICPLGQCK
VSVIPPIALN STDSDGFCRA TFSFCVSPLL VFVNSKSGDN QGVKFLRRFK QLLNPAQVFD
LMNGGPHLGL RLFQKFDNFR ILVCGGDGSV GWVLSEIDKL NLNKQCQLGV LPLGTGNDLA
RVLGWGGSYD DDTQLPQILE KLERASTKML DRWSIMTYEL KLPPKASLLP EPPEASEEFY
MTIYEDSVAA HLTKILNSDE HAVVISSAKI LCETVKDFVA KVEKAHEKTL EKAVAADAVA
SKCSILNEKL EQLLQALHTE SQAGPVLPGI SPLMVEEDAV ESSSEESLCE SKEHLLDDTT
KPSSQKAVKP REIMLRANSL KKAVRQVIEE AGKVMDDQPV HSSELVNQSF DYDSTETDDS
KDELKEDDVK ESLTVKGALR SPDGRAGRSQ TDSGPGAPVA ASKENLPVLN TRIICPGLRA
GLAASIAGSS IINKMLLANI DPFGATPFID PDPDSVDGYS EKCVMNNYFG IGLDAKISLE
FNNKREEHPE KCRSRTKNLM WYGVLGTREL LQRSYKNLEQ RVQLECDGQY IPLPSLQGIA
VLNIPSYAGG TNFWGGTKED DIFAAPSFDD KILEVVAIFD SVQMAVSRVI KLQHHRIAQC
RTVKITIFGD EGVPVQVDGE AWVQPPGIIK IVHKNRAQML TRDRAFESTL KSWEDKQKCD
SGKPVLRTHL YIQHAADLAT EEVSQMQLCS QAAEELITRI CDAATIHCLL EQELAHAVNA
CSHALNKANP RFPESLTRDT ATEIAINVKA LYNETESLLV GRVPLQLESP HEERVSNALH
SVEVELQKLT EIPWLYYILH PNEDEEPPMD CTKRNSKSTV FRIVPKFKKE KVQKQKTSSQ
PVQKWGTEEV AAWLDLLNLG EYREIFIRHD IRGAELLHLE RRDLKDLGIP KVGHVKRILQ
GIKELERGTL QPEV
//
