ID A6QPL5_BOVIN Unreviewed; 1215 AA.
AC A6QPL5; F1MDC8;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 112.
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=DGKD {ECO:0000313|Ensembl:ENSBTAP00000027473.6,
GN ECO:0000313|VGNC:VGNC:28026};
GN Synonyms=DGKH {ECO:0000313|EMBL:AAI49378.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI49378.1};
RN [1] {ECO:0000313|EMBL:AAI49378.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hereford {ECO:0000313|EMBL:AAI49378.1};
RC TISSUE=Fetal cerebellum {ECO:0000313|EMBL:AAI49378.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000027473.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000027473.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSBTAP00000027473.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000027473.6};
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; BC149377; AAI49378.1; -; mRNA.
DR RefSeq; NP_001030359.2; NM_001035282.2.
DR PaxDb; 9913-ENSBTAP00000027473; -.
DR Ensembl; ENSBTAT00000027473.6; ENSBTAP00000027473.6; ENSBTAG00000020616.6.
DR GeneID; 513389; -.
DR KEGG; bta:513389; -.
DR CTD; 8527; -.
DR VEuPathDB; HostDB:ENSBTAG00000020616; -.
DR VGNC; VGNC:28026; DGKD.
DR eggNOG; KOG1170; Eukaryota.
DR GeneTree; ENSGT00940000159041; -.
DR HOGENOM; CLU_001799_3_0_1; -.
DR OMA; SKAPCEK; -.
DR TreeFam; TF313104; -.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000020616; Expressed in thymus and 106 other cell types or tissues.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IEA:Ensembl.
DR GO; GO:0046834; P:lipid phosphorylation; IEA:Ensembl.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:Ensembl.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IEA:Ensembl.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd20847; C1_DGKdelta_rpt1; 1.
DR CDD; cd20893; C1_DGKdelta_rpt2; 1.
DR CDD; cd13274; PH_DGK_type2; 1.
DR CDD; cd09575; SAM_DGK-delta; 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; IPR047478; C1_DGKdelta_rpt1.
DR InterPro; IPR047477; C1_DGKdelta_rpt2.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR037606; DGK-delta_SAM.
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:SF30; DIACYLGLYCEROL KINASE DELTA; 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 2: Evidence at transcript level;
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:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 53..146
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 163..213
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 235..286
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 317..451
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT DOMAIN 1146..1209
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 133974 MW; FA0F9F48BFBD67DB CRC64;
MAAAAGAPQP GPPQPPPPPP PEESSDSEPE AEPGSPQKLI RKVSTSGQIR QKTVIKEGML
TKQNNSFQRS KRRYFKLRGR TLYYAKTAKS IIFDEVDLTD ASVAESSTKN VNNSFTVITP
CRKLILCADN RKEMEDWIAA LKTVQSREHF EPTQYSMDHF SGTHNWYACS HARPTYCNVC
REALSGVTSH GLSCEVCKFK AHKRCAVRAT SNCKWTTLAS IGKDIIEDED GIAMPHQWLE
GNLPVSAKCT VCDKTCGSVL RLQDWRCLWC KAMVHTACKD SLVTKCPLGL CKVSVIPPTA
LNSIDSDGFW KATCPPSCTS PLLVFVNSKS GDNQGVKFLR RFKQLLNPAQ VFDLMNGGPH
LGLRLFQKFD TFRILVCGGD GSVGWVLSEI DSLNLHKQCQ LGVLPLGTGN DLARVLGWGS
ACDDDTQLPQ ILEKLERAST KMLDRWSVMA YETKLPRPVS SSTVTEDLSE GSEVQQILFY
EDSVAAHLSK ILTSDQHSVV ISSAKVLCET VKDFVARVGK AYEKTTESSE ESEVMAKKCS
VLKEKLDSLL KTLDDESQAS SSLPTPPPTI AEEAEDGDGA GGGCGSGSTG AHAVGSACPT
RPQIFRPREQ LMLRANSLKK AIRQIIEHTE KAVDEQNAQT QEQEGFILSL SESEKKDLKS
DDRAGHGEGH SASKGRSLRR VSKSPCEKLI SKGSLSPGGS ASLPPQSGSR DGLPALNTKI
LFPNVRAGMS GTLPGGSVIS RLLINADPFN SEPENLEYYT EKCVMNNYFG IGLDAKISLD
FNNKRDEHPE KCRSRTKNMM WYGVLGTREL LHRTYKNLEQ KVLLECDGRP IPLPSLQGIA
VLNIPSYAGG TNFWGGTKED DTFTAPSFDD KILEVVAVFG SMQMAVSRVI KLQHHRIAQC
RTVKISILGD EGVPVQVDGE AWVQPPGYIR IVHKNRAQTL TRDRAFENTL KSWEDKQKCE
LPRAPSFSLH PEILSEEEAT QMDQFGQAAG ALIHSIRELA QSHQDVEQEL AHAVNASSKS
MDRVYGKPRA TEGLSCSLVL EMVNNVRALR SETELLLAGR LALQLDPPQK ERLTAALAEM
DQQLRKLADT PWLCQPMEPG DEENVMLDLS KRSRSGKFRL VTKFKKEKNN KNRAARCSLG
APVHLWGTEE VAAWLEHLSL CEYKDIFTRH DIRGSELLHL ERRDLKDLGV TKVGHMKRIL
CGIKELSRGA AAAEA
//
