ID Q58AU5_CAEEL Unreviewed; 796 AA.
AC Q58AU5;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 142.
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=dgk-1 {ECO:0000313|EMBL:CCD63967.1,
GN ECO:0000313|WormBase:C09E10.2d};
GN ORFNames=C09E10.2 {ECO:0000313|WormBase:C09E10.2d}, CELE_C09E10.2
GN {ECO:0000313|EMBL:CCD63967.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD63967.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD63967.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD63967.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:ARBA00001383,
CC ECO:0000256|RuleBase:RU361128};
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000256|ARBA:ARBA00009280, ECO:0000256|RuleBase:RU361128}.
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DR EMBL; BX284606; CCD63967.1; -; Genomic_DNA.
DR RefSeq; NP_001024383.1; NM_001029212.1.
DR AlphaFoldDB; Q58AU5; -.
DR PeptideAtlas; Q58AU5; -.
DR EnsemblMetazoa; C09E10.2d.1; C09E10.2d.1; WBGene00000958.
DR UCSC; C09E10.2e; c. elegans.
DR AGR; WB:WBGene00000958; -.
DR WormBase; C09E10.2d; CE38269; WBGene00000958; dgk-1.
DR OrthoDB; 4642163at2759; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000958; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR ExpressionAtlas; Q58AU5; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0044297; C:cell body; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:ATP-dependent diacylglycerol kinase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IBA:GO_Central.
DR GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:WormBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IDA:WormBase.
DR GO; GO:0040013; P:negative regulation of locomotion; IMP:WormBase.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0046662; P:regulation of egg-laying behavior; IMP:WormBase.
DR GO; GO:0040012; P:regulation of locomotion; IMP:WormBase.
DR GO; GO:0032094; P:response to food; IMP:WormBase.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:WormBase.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:WormBase.
DR CDD; cd20803; C1_DGKtheta_typeV_rpt1; 1.
DR CDD; cd20804; C1_DGKtheta_typeV_rpt2; 1.
DR CDD; cd20854; C1_DGKtheta_typeV_rpt3; 1.
DR Gene3D; 2.60.200.40; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
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; IPR001965; Znf_PHD.
DR PANTHER; PTHR11255; DIACYLGLYCEROL KINASE; 1.
DR PANTHER; PTHR11255:SF54; DIACYLGLYCEROL KINASE THETA; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 3.
DR SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361128};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU361128};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361128};
KW Proteomics identification {ECO:0007829|EPD:Q58AU5,
KW ECO:0007829|PeptideAtlas:Q58AU5};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361128};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 20..70
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 83..131
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 149..200
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 388..526
FT /note="DAGKc"
FT /evidence="ECO:0000259|PROSITE:PS50146"
FT REGION 232..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 88750 MW; 43F4CA2E8FC6EDEB CRC64;
MAAEGHNVDA NLVDMRPNHG HYFVKKTFGK PAYCHHCCDK IWGMLTTGYS CEMCNFVCHE
KCLRTVVSYC SSVALQLIKN PVAHTWSAPC LIKRKYCCVC RKRTDDALSV ECEVCEYYVH
VDCSDLAVSD CKEAATYVAN MESANTVQYH HMREGNLPKE SKCIVCRKTC FSTECLAGMR
CEWCGQTAHA VCYRQMDKEC DFGVLRKIML PPMCLTIPRT ELPMEQLLNI SSHDQPQSRK
VSSPSKIQAD DVSTSGEDVK EREDFEIIRV FDGNNSYRSQ DSLRRYHVVR FYVQEKEDPH
DHAVFVGNLP VSLAQRQYER ILLKLLGAKE KPFTAIGPIY FEYGSLIITF NTPKAATAAV
QKLQSAIYEE KKLIVLCLPN VQPQMIPKDV EPLLVLVNVK SGGCQGTELI QSFRKLLNPF
QVFDVLNGGP LVGLYVFRNI PKYKILACGG DGTIGWVLQC LDIAKQDAAC FSPPCGIVPL
GTGNDLARVL RWGGGYTGEE NPMDILKDVI EADTVKLDRW AVVFHEEERN QPTSSGNQTE
MNEQTMNNPE DQTSMIIMNN YFGIGIDADV CLKFHNKRDA NPEKFQSRLF NKTQYAKIGL
QKMFFERTCK DLWKRIELEV DGRIIELPNI EGIVVLNLLS WGSGANPWGT SKEEGNFSKP
THYDGLLEVV GISDVSRLGL IQSKLAAGIR IAQGGSIRIT THEEWPVQVD GEPHIQPPGT
ITILKSALKA QMLKKAKKSR RGGATNATSL THPHPETSES MSGPLGVPST LGDPNHGKTT
PDNTAADSDE EGDAFL
//
