DGK3_CAEEL
ID DGK3_CAEEL Reviewed; 795 AA.
AC Q03603;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Probable diacylglycerol kinase 3;
DE Short=DAG kinase 3;
DE EC=2.7.1.107;
DE AltName: Full=Diglyceride kinase 3;
DE Short=DGK-3;
GN Name=dgk-3; ORFNames=F54G8.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17086178; DOI=10.1038/nn1796;
RA Biron D., Shibuya M., Gabel C., Wasserman S.M., Clark D.A., Brown A.,
RA Sengupta P., Samuel A.D.;
RT "A diacylglycerol kinase modulates long-term thermotactic behavioral
RT plasticity in C. elegans.";
RL Nat. Neurosci. 9:1499-1505(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16418272; DOI=10.1073/pnas.0506954103;
RA Matsuki M., Kunitomo H., Iino Y.;
RT "Goalpha regulates olfactory adaptation by antagonizing Gqalpha-DAG
RT signaling in Caenorhabditis elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:1112-1117(2006).
CC -!- FUNCTION: Involved in AFD-neuron mediated thermotaxis. Regulates
CC behavior to environmental temperature. Thought to have a role in
CC olfactory adaptation by affecting diacylglycerol levels.
CC {ECO:0000269|PubMed:16418272, ECO:0000269|PubMed:17086178}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Slow to adapt to new temperature levels. Dgk-3
CC and dgk-1 double mutant shows defects in olfactory adaptation.
CC {ECO:0000269|PubMed:16418272, ECO:0000269|PubMed:17086178}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z19155; CAA79558.3; -; Genomic_DNA.
DR PIR; S28273; S28273.
DR RefSeq; NP_499031.3; NM_066630.3.
DR AlphaFoldDB; Q03603; -.
DR STRING; 6239.F54G8.2; -.
DR PaxDb; Q03603; -.
DR EnsemblMetazoa; F54G8.2.1; F54G8.2.1; WBGene00000960.
DR GeneID; 186262; -.
DR KEGG; cel:CELE_F54G8.2; -.
DR UCSC; F54G8.2; c. elegans.
DR CTD; 186262; -.
DR WormBase; F54G8.2; CE46230; WBGene00000960; dgk-3.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000168305; -.
DR HOGENOM; CLU_003770_1_0_1; -.
DR InParanoid; Q03603; -.
DR OMA; YNPEGAQ; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; Q03603; -.
DR Reactome; R-CEL-114508; Effects of PIP2 hydrolysis.
DR PRO; PR:Q03603; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000960; Expressed in larva and 3 other tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IBA:GO_Central.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IBA:GO_Central.
DR GO; GO:0042048; P:olfactory behavior; IMP:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:WormBase.
DR GO; GO:0043052; P:thermotaxis; IMP:WormBase.
DR CDD; cd00029; C1; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.110; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR029477; DAG_kinase_typeI_N.
DR InterPro; IPR037607; DGK.
DR InterPro; IPR038199; DGK_typeI_N_sf.
DR InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR PANTHER; PTHR11255; PTHR11255; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF14513; DAG_kinase_N; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR SMART; SM00109; C1; 2.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Calcium; Kinase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..795
FT /note="Probable diacylglycerol kinase 3"
FT /id="PRO_0000218471"
FT DOMAIN 170..205
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 215..250
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 423..558
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 265..316
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 329..375
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 795 AA; 89315 MW; A1427D2F9837616A CRC64;
MLLSPEQFSR LSEYAAYSRR KLKDMLSDFQ QDGKFYSYLS VDGQTINIDG FRAFLIDYFG
ADLPSDLVDQ LFLSFSKPPI KERRTSLFED AISTVRAKFS ESLSGRMAGL NIAGGSGQQT
DRSQSSEPQA LVCIPEDDVM GPRVANNDSQ EPRIPLKPLI CTLSLLEADT PENKLDVVFH
VYDSDGNGFL DKSEIDGIIE QMMNVARYQQ WDTIELEQVI RQMMVDIDYD NDGIVSFDEW
RRGGLTNIPL LVLLGFDTEM KEDGSHVWRL RHFTKPTYCN ACCSILVGWG GKQGLSCSLC
KYTVHERCVR SAATNCIRTY SSRQQDKLYH HWQDANATAK CVKCKATVGV FQGKGCRWCH
NYVHHRCMSA LAQECDLGAL VHHILPPTHI FPAFLERKTS TSLKNHNFSS HSASLLQAVS
PSNDCRPLLV LVNPKSGGKQ GVKILQKFEY LLNPRQVYDL SKTGPEPGLQ LFSTLKNCNI
LVCGGDGTIG WVLESMDKMT FPHGRPPVAV LPLGTGNDLA RCLRWGGGYE NENLHKILEQ
IEKSSLIDMD RWQIKIEITE NKSARRASEK GDTPPYSIIN NYFSIGVDAS IAHRFHVMRE
KFPEKFNSRM RNKLWYFELG TSETLSSSCK NLHEQIDILC DGESIDLGQD ASLEGIALLN
IPSIYGGSNL WGRSRKSKGR MPGLFPMKNA EKMQLQTRVQ DIGDGLIELV GLESAMQMGQ
IKAGVRGARR LSQCSTVVIQ THKSFPMQID GEPWMQPPCI IQITHKNQAK MLVAAAPRKR
SSWMLLKRQS TNDDN
