ID D3Z519_MOUSE Unreviewed; 899 AA.
AC D3Z519;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 106.
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=Dgki {ECO:0000313|Ensembl:ENSMUSP00000047858.8,
GN ECO:0000313|MGI:MGI:2443430};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000047858.8, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000047858.8, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000047858.8,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000047858.8}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000047858.8};
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=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol
CC + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00023400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000256|ARBA:ARBA00023400};
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|ARBA:ARBA00023411};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000256|ARBA:ARBA00023411};
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; D3Z519; -.
DR SMR; D3Z519; -.
DR iPTMnet; D3Z519; -.
DR SwissPalm; D3Z519; -.
DR MaxQB; D3Z519; -.
DR PeptideAtlas; D3Z519; -.
DR ProteomicsDB; 359258; -.
DR Antibodypedia; 32299; 219 antibodies from 29 providers.
DR Ensembl; ENSMUST00000042075.8; ENSMUSP00000047858.8; ENSMUSG00000038665.16.
DR AGR; MGI:2443430; -.
DR MGI; MGI:2443430; Dgki.
DR VEuPathDB; HostDB:ENSMUSG00000038665; -.
DR GeneTree; ENSGT00940000158094; -.
DR HOGENOM; CLU_003770_4_0_1; -.
DR UniPathway; UPA00230; -.
DR ChiTaRS; Dgki; mouse.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000038665; Expressed in lumbar dorsal root ganglion and 56 other cell types or tissues.
DR ExpressionAtlas; D3Z519; baseline and differential.
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; cd20850; C1_DGKiota_rpt1; 1.
DR CDD; cd20896; C1_DGKiota_rpt2; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR047486; C1_DGKiota_rpt1.
DR InterPro; IPR047487; C1_DGKiota_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 PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF92; DIACYLGLYCEROL KINASE IOTA; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50146; DAGK; 1.
PE 1: Evidence at protein level;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
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 Proteomics identification {ECO:0007829|MaxQB:D3Z519,
KW ECO:0007829|PeptideAtlas:D3Z519};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 216..351
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REPEAT 828..860
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 177..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..193
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 101332 MW; 44A21A91CF8678D4 CRC64;
MVKLKVLAGN ATNLENAVNG EHLWLETNVS GDLCYLGEEN CQVRFAKSAL RRKCAVCKIV
VHTACIEQLE KINFRCKPTF REGGSRSPRE NFVRHHWVHR RRQEGKCKQC GKGFQQKFSF
HSKEIVAISC SWCKQAFHNK VTCFMLHHIE EPCSLGAHAA VIVPPTWIIK VKKPQNSLKA
SNRKKKRTSF KRKASKRGTE QETKGRPFVI KPISSPLMKP LLVFVNPKSG GNQGTKVLQM
FMWYLNPRQV FDLSQEGPKD ALEMYRKVPN LRILACGGDG TVGWILSILD ELQLSPQPPV
GVLPLGTGND LARTLNWGGG YTDEPVSKIL CQVEDGTIVQ LDRWNLHVER NPDLPPEELE
DGVCKLPLNV FNNYFSLGFD AHVTLEFHES REANPEKFNS RFRNKMFYAG AAFSDFLQRS
SRDLSKHVKV VCDGTDLTPK IQDLKFQCIV FLNIPRYCAG TMPWGNPGDH HDFEPQRHDD
GYIEVIGFTM ASLAALQVGG HGERLHQCRE VMLLTYKSIP MQVDGEPCRL APAMIRISLR
NQANMVQKSK RRTSMPLLND PQSVPDRLRI RVNKISLQDY EGLHYDKDKL REASIPLGIL
VVRGDCDLET CRMYIDRLQE DLQSVSSGSQ RVHYQDQETS FPRALSAQRL SPRWCFLDAT
SADRFYRIDR SQEHLHFVME ISHDEIFILD PDMVVSQQAG TPPGMPDLVV EQASGLSDWW
NPALRKRMLS DSGMITPHYE DSDLKDFSHS RVLQSPVSSE DHAILQAVLT GDLMKLMESY
KNGGSLLIQG PGHCSLLHYA AKTGNGDIVK YILDHGPAEL LDMADSETGE TALHKAACQR
NRAVCQLLVD AGASLRQTDS KGKTPQERAQ QAGDPDLAAY LESRQNYKII GHEDLETAV
//
