DGKG_RAT
ID DGKG_RAT Reviewed; 788 AA.
AC P49620;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Diacylglycerol kinase gamma;
DE Short=DAG kinase gamma;
DE EC=2.7.1.107 {ECO:0000269|PubMed:7809169};
DE AltName: Full=88 kDa diacylglycerol kinase;
DE AltName: Full=DGK-III {ECO:0000303|PubMed:7809169};
DE AltName: Full=Diglyceride kinase gamma;
DE Short=DGK-gamma;
GN Name=Dgkg; Synonyms=Dagk3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar;
RX PubMed=7809169; DOI=10.1073/pnas.91.26.13042;
RA Goto K., Funayama M., Kondo H.;
RT "Cloning and expression of a cytoskeleton-associated diacylglycerol kinase
RT that is dominantly expressed in cerebellum.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:13042-13046(1994).
CC -!- FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into
CC phosphatidic acid/phosphatidate/PA and regulates the respective levels
CC of these two bioactive lipids (PubMed:7809169). Thereby, acts as a
CC central switch between the signaling pathways activated by these second
CC messengers with different cellular targets and opposite effects in
CC numerous biological processes (By similarity). Has no apparent
CC specificity with regard to the acyl compositions of diacylglycerol (By
CC similarity). Specifically expressed in the cerebellum where it controls
CC the level of diacylglycerol which in turn regulates the activity of
CC protein kinase C gamma. Through protein kinase C gamma, indirectly
CC regulates the dendritic development of Purkinje cells, cerebellar long
CC term depression and ultimately cerebellar motor coordination (By
CC similarity). {ECO:0000250|UniProtKB:P49619,
CC ECO:0000250|UniProtKB:Q91WG7, ECO:0000269|PubMed:7809169}.
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:0000269|PubMed:7809169};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:7809169};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-
CC 3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:7809169};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429;
CC Evidence={ECO:0000305|PubMed:7809169};
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:0000269|PubMed:7809169};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:7809169};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP =
CC 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate +
CC ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:7809169};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340;
CC Evidence={ECO:0000305|PubMed:7809169};
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:0000269|PubMed:7809169};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000305|PubMed:7809169};
CC -!- ACTIVITY REGULATION: The activity is calcium-dependent
CC (PubMed:7809169). Requires phosphatidylserine for maximal activity (By
CC similarity). {ECO:0000250|UniProtKB:P49619,
CC ECO:0000269|PubMed:7809169}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:7809169}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7809169}. Cytoplasm,
CC cytosol {ECO:0000250|UniProtKB:P49619}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:7809169}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in brain (PubMed:7809169).
CC Highly expressed in cerebellar Purkinje cells (at protein level)
CC (PubMed:7809169). {ECO:0000269|PubMed:7809169}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; D38448; BAA07480.1; -; mRNA.
DR RefSeq; NP_037258.1; NM_013126.1.
DR AlphaFoldDB; P49620; -.
DR BioGRID; 247695; 2.
DR STRING; 10116.ENSRNOP00000002452; -.
DR iPTMnet; P49620; -.
DR PhosphoSitePlus; P49620; -.
DR PaxDb; P49620; -.
DR PRIDE; P49620; -.
DR Ensembl; ENSRNOT00000002452; ENSRNOP00000002452; ENSRNOG00000001796.
DR GeneID; 25666; -.
DR KEGG; rno:25666; -.
DR UCSC; RGD:2499; rat.
DR CTD; 1608; -.
DR RGD; 2499; Dgkg.
DR eggNOG; KOG1169; Eukaryota.
DR GeneTree; ENSGT00940000156768; -.
DR HOGENOM; CLU_003770_1_0_1; -.
DR InParanoid; P49620; -.
DR OMA; ALCKYTV; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; P49620; -.
DR TreeFam; TF313104; -.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR PRO; PR:P49620; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001796; Expressed in adult mammalian kidney and 16 other tissues.
DR Genevisible; P49620; RN.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
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; IDA:RGD.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; ISS:UniProtKB.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IEP:RGD.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; TAS:RGD.
DR GO; GO:0050773; P:regulation of dendrite development; ISO:RGD.
DR CDD; cd00029; C1; 1.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.110; -; 2.
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; 1.
DR Pfam; PF14513; DAG_kinase_N; 1.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
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; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Cytoplasm; Cytoskeleton; Kinase; Lipid metabolism;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..788
FT /note="Diacylglycerol kinase gamma"
FT /id="PRO_0000218461"
FT DOMAIN 172..207
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 217..252
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 427..561
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 268..318
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 333..380
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 83..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
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 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 788 AA; 88521 MW; E77BCA40B22C1DA9 CRC64;
MSDGQWVCLS SEEFDQLQKY SEYSSKKIKD VLAEFNEGGS LKQYDPHKPI SYDVFKLFMR
AYLEVDLPQP LSTNLFLAFS QKPRQETPDH PKEGASSSEP NVSDSNAEST AKADAACAPD
TESKPIKTQV PSEELEAAAP WGEPNAPASS SDAPIVYLKD VVCYLSLMET GRPQDKLEFM
FRLYDSDENE LLDQAELDQI VSQMLHVAQY LEWDPTELRP ILKEMLQGMD YNKDGFVSLE
EWVSGGMTTI PLLVLLGMDD SASKGDGRHA WTLKHFKKPT YCNFCHIMLM GVRKQGLCCI
YCKYAVHQRC VSNSIPGCVK TYSKAKRSGE VMQHAWVEGN SSVKCDRCHK SIKCYQSVTA
RHCVWCRMTF HRKCELSTAC DGGELKDHIL LPTSIYPVTR DRQAGKSDSG AAAKGELVMQ
YKIIPSPGTH PLLVLVNPKS GGRQGERILQ KFHYLLNPKQ VFNLDKGGPT PGLNFFQDTP
DFRVLACGGD GTVGWILDCI DKANFTKHPP VAVLPLGTGN DLARCLRWGG GYEGGSLTKI
LKEIEQSPLV MLDRWYLEVM PREEVENGDQ VPYNIMNNYF SIGVDASIAH RFHVMREKHP
EKFNSRMKNK LWYFEFGTSE TFAATCKKLH DHIELECDGV EVDLSNIFLE GIAILNIPSM
YGGTNLWGET KKNRAVIRES RKSVTDPKEL KCCVQDLSDQ LLEVVGLEGA MEMGQIYTGL
KSAGRRLAQC SSVTIRTKKL LPMQVDGEPW MQPPCMIKIT HKNQAPMMMG PPQKSSFFSL
RRKSRSKD
