DGKI_RAT
ID DGKI_RAT Reviewed; 1050 AA.
AC F1MAB7; Q810C3; Q810C4; Q810C5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Diacylglycerol kinase iota {ECO:0000303|PubMed:15024004};
DE Short=DAG kinase iota {ECO:0000305|PubMed:15024004};
DE EC=2.7.1.107 {ECO:0000269|PubMed:15024004};
GN Name=Dgki {ECO:0000312|RGD:735049};
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] (ISOFORMS 1; 2 AND 3), FUNCTION (ISOFORMS 2 AND
RP 3), CATALYTIC ACTIVITY (ISOFORM 2), ACTIVITY REGULATION, PATHWAY,
RP SUBCELLULAR LOCATION (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY (ISOFORMS
RP 1; 2 AND 3).
RC TISSUE=Brain;
RX PubMed=15024004; DOI=10.1074/jbc.m312976200;
RA Ito T., Hozumi Y., Sakane F., Saino-Saito S., Kanoh H., Aoyagi M.,
RA Kondo H., Goto K.;
RT "Cloning and characterization of diacylglycerol kinase iota splice variants
RT in rat brain.";
RL J. Biol. Chem. 279:23317-23326(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP INTERACTION WITH DLG1; DLG2; DLG3 AND DLG4, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MOTIF.
RX PubMed=21119615; DOI=10.1038/emboj.2010.286;
RA Yang J., Seo J., Nair R., Han S., Jang S., Kim K., Han K., Paik S.K.,
RA Choi J., Lee S., Bae Y.C., Topham M.K., Prescott S.M., Rhee J.S.,
RA Choi S.Y., Kim E.;
RT "DGKiota regulates presynaptic release during mGluR-dependent LTD.";
RL EMBO J. 30:165-180(2011).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:15024004). 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 (Probable). Has probably no preference
CC for any of the diacylglycerols in terms of the acyl chain composition,
CC especially for the acyl chain at the sn-2 position (PubMed:15024004).
CC By controlling the diacylglycerol/DAG-mediated activation of RASGRP3,
CC negatively regulates the Rap1 signaling pathway. May play a role in
CC presynaptic diacylglycerol/DAG signaling and control neurotransmitter
CC release during metabotropic glutamate receptor-dependent long-term
CC depression (By similarity). {ECO:0000250|UniProtKB:D3YWQ0,
CC ECO:0000269|PubMed:15024004, ECO:0000305}.
CC -!- FUNCTION: [Isoform 2]: Has a decreased affinity for ATP and a reduced
CC diacylglycerol kinase activity. Has no preference for any of the
CC diacylglycerols in terms of the acyl chain composition.
CC {ECO:0000269|PubMed:15024004}.
CC -!- FUNCTION: [Isoform 3]: Has no diacylglycerol kinase activity.
CC {ECO:0000269|PubMed:15024004}.
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:15024004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:15024004};
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:15024004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:15024004};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:15024004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328;
CC Evidence={ECO:0000305|PubMed:15024004};
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:15024004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340;
CC Evidence={ECO:0000305|PubMed:15024004};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:15024004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340;
CC Evidence={ECO:0000305|PubMed:15024004};
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:15024004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000305|PubMed:15024004};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
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:15024004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324;
CC Evidence={ECO:0000305|PubMed:15024004};
CC -!- ACTIVITY REGULATION: Activated by phosphatidylserine.
CC {ECO:0000269|PubMed:15024004}.
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000269|PubMed:15024004}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with DLG4; controls the
CC localization of DGKI to the synapse (PubMed:21119615). Interacts (via
CC PDZ-binding motif) with DLG1 (PubMed:21119615). Interacts (via PDZ-
CC binding motif) with DLG2 (PubMed:21119615). Interacts (via PDZ-binding
CC motif) with DLG3 (PubMed:21119615). May interact with RASGRP3; involved
CC in the regulation of RASGRP3 activity (By similarity).
CC {ECO:0000250|UniProtKB:D3YWQ0, ECO:0000269|PubMed:21119615}.
CC -!- INTERACTION:
CC F1MAB7; Q62696: Dlg1; NbExp=3; IntAct=EBI-8523614, EBI-389325;
CC F1MAB7; Q63622: Dlg2; NbExp=3; IntAct=EBI-8523614, EBI-396947;
CC F1MAB7; Q62936: Dlg3; NbExp=2; IntAct=EBI-8523614, EBI-349596;
CC F1MAB7; P31016: Dlg4; NbExp=5; IntAct=EBI-8523614, EBI-375655;
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:21119615}. Cell projection, dendrite
CC {ECO:0000269|PubMed:21119615}. Presynapse
CC {ECO:0000269|PubMed:21119615}. Postsynapse
CC {ECO:0000269|PubMed:21119615}. Postsynaptic density
CC {ECO:0000269|PubMed:21119615}. Synaptic cell membrane
CC {ECO:0000269|PubMed:21119615}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000269|PubMed:21119615}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:15024004, ECO:0000269|PubMed:21119615}.
CC Nucleus {ECO:0000250|UniProtKB:O75912}. Note=Excluded from inhibitory
CC synapses (PubMed:21119615). Localization between cytoplasm and nucleus
CC is regulated by protein kinase C (By similarity). Both in the detergent
CC soluble and particulate fractions (PubMed:15024004).
CC {ECO:0000250|UniProtKB:O75912, ECO:0000269|PubMed:15024004,
CC ECO:0000269|PubMed:21119615}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:15024004}. Note=Not detected in detergent soluble
CC fraction. {ECO:0000269|PubMed:15024004}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:15024004}. Note=Not detected in detergent soluble
CC fraction. {ECO:0000269|PubMed:15024004}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=rDGKi-1 {ECO:0000303|PubMed:15024004};
CC IsoId=F1MAB7-1; Sequence=Displayed;
CC Name=2; Synonyms=rDGKi-2 {ECO:0000303|PubMed:15024004};
CC IsoId=F1MAB7-2; Sequence=VSP_060835, VSP_060836;
CC Name=3; Synonyms=rDGKi-3 {ECO:0000303|PubMed:15024004};
CC IsoId=F1MAB7-3; Sequence=VSP_060833, VSP_060834;
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain (at protein level)
CC (PubMed:15024004, PubMed:21119615). Expressed in hippocampus,
CC cerebellum, brain stem and spinal cord (at protein level)
CC (PubMed:21119615). Highly expressed in hippocampus, cerebellar cortex,
CC olfactory bulb, and olfactory tubercle and to lower extent in the
CC cerebral cortex, caudate putamen, and thalamus. Not detected in the
CC white matter (PubMed:15024004). Also expressed in eye
CC (PubMed:15024004). {ECO:0000269|PubMed:15024004,
CC ECO:0000269|PubMed:21119615}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Major isoform in brain (at protein
CC level). {ECO:0000269|PubMed:15024004}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Minor isoform in brain (at protein
CC level). {ECO:0000269|PubMed:15024004}.
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:15024004}.
CC -!- DEVELOPMENTAL STAGE: Expression gradually increases in the first weeks
CC after birth (at protein level). {ECO:0000269|PubMed:21119615}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
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DR EMBL; AB058962; BAC66854.1; -; mRNA.
DR EMBL; AB058963; BAC66855.1; -; mRNA.
DR EMBL; AB058964; BAC66856.1; -; mRNA.
DR EMBL; AABR07060249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07060250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07060251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07060252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07060253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07060254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07060255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_942077.2; NM_198782.2. [F1MAB7-1]
DR AlphaFoldDB; F1MAB7; -.
DR SMR; F1MAB7; -.
DR IntAct; F1MAB7; 8.
DR MINT; F1MAB7; -.
DR STRING; 10116.ENSRNOP00000034571; -.
DR iPTMnet; Q810C4; -.
DR PaxDb; F1MAB7; -.
DR Ensembl; ENSRNOT00000033268; ENSRNOP00000034571; ENSRNOG00000026705. [F1MAB7-1]
DR GeneID; 688705; -.
DR KEGG; rno:688705; -.
DR CTD; 9162; -.
DR RGD; 735049; Dgki.
DR eggNOG; KOG0782; Eukaryota.
DR GeneTree; ENSGT00940000158094; -.
DR HOGENOM; CLU_003770_4_0_1; -.
DR InParanoid; F1MAB7; -.
DR OMA; CFLDSCT; -.
DR OrthoDB; 274339at2759; -.
DR TreeFam; TF312817; -.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR UniPathway; UPA00230; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000026705; Expressed in frontal cortex and 9 other tissues.
DR ExpressionAtlas; F1MAB7; baseline and differential.
DR Genevisible; F1MAB7; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:MGI.
DR GO; GO:0099147; C:extrinsic component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0098891; C:extrinsic component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:RGD.
DR GO; GO:0005095; F:GTPase inhibitor activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0046339; P:diacylglycerol metabolic process; IDA:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0046959; P:habituation; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046834; P:lipid phosphorylation; IDA:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0043087; P:regulation of GTPase activity; ISO:RGD.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; ISO:RGD.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
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; PTHR11255; 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; SSF111331; SSF111331; 1.
DR SUPFAM; SSF48403; SSF48403; 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 Alternative splicing; ANK repeat; ATP-binding; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Kinase;
KW Lipid metabolism; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat; Synapse; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1050
FT /note="Diacylglycerol kinase iota"
FT /id="PRO_0000451699"
FT DOMAIN 367..502
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT REPEAT 943..972
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 979..1008
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT ZN_FING 172..227
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 245..304
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 52..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1048..1050
FT /note="PDZ-binding"
FT /evidence="ECO:0000269|PubMed:21119615"
FT COMPBIAS 57..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..344
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 583..591
FT /note="CDGTDLTPK -> LSWMRLSDS (in isoform 3)"
FT /id="VSP_060833"
FT VAR_SEQ 592..1050
FT /note="Missing (in isoform 3)"
FT /id="VSP_060834"
FT VAR_SEQ 824..840
FT /note="EHLHFVMEISHDEIFIL -> ACFSPLGTFALCDGDFS (in isoform
FT 2)"
FT /id="VSP_060835"
FT VAR_SEQ 841..1050
FT /note="Missing (in isoform 2)"
FT /id="VSP_060836"
FT CONFLICT 156
FT /note="K -> I (in Ref. 1; BAC66854/BAC66856/BAC66855)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="N -> I (in Ref. 1; BAC66854/BAC66856/BAC66855)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="F -> L (in Ref. 1; BAC66854/BAC66856/BAC66855)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="D -> E (in Ref. 1; BAC66854/BAC66855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1050 AA; 115894 MW; AD2B51EB74838255 CRC64;
MDAAGRGCHL LPLPAARGPA RAPAASSALS PAGLCSGTAS ASSAAAGAVA MNPSSSAGEE
RGATGGSSSS GSGAGSCCLG AEGGVDPRGA GAAAAAALEE PAAAGQKEKE EALEEKLRDL
TFRKQVSYRK AISRTGLQHL APAHPLGLPV ANGPAKEPRA TLDWSENAVN GEHLWLETNV
SGDLCYLGEE NCQVRFAKSA LRRKCAVCKI VVHTACIEQL EKINFRCKPT FREGGSRSPR
ENFVRHHWVH RRRQEGKCKQ CGKGFQQKFS FHSKEIVAIS CSWCKQAFHN KVTCFMLHHI
EEPCSLGAHA AVIVPPTWII KVKKPQNSLK ASNRKKKRTS FKRKASKRGT EQENKGRPFV
IKPISSPLMK PLLVFVNPKS GGNQGTKVLQ MFMWYLNPRQ VFDLSQEGPK DALELYRKVP
NLRILACGGD GTVGWILSIL DELQLSPQPP VGVLPLGTGN DLARTLNWGG GYTDEPVSKI
LCQVEDGTIV QLDRWNLHVE RNPDLPPEEL EDGVCKLPLN VFNNYFSLGF DAHVTLEFHE
SREANPEKFN SRFRNKMFYA GAAFSDFLQR SSRDLSKHVK VVCDGTDLTP KIQDLKFQCI
VFLNIPRYCA GTMPWGNPGD HHDFEPQRHD DGYIEVIGFT MASLAALQVG GHGERLHQCR
EVMLLTYKSI PMQVDGEPCR LAPAMIRISL RNQANMVQKS KRRTSMPLLN DPQSVPDRLR
IRVNKISLQD YEGLHYDKEK LREASIPLGI LVVRGDCDLE TCRMYIDRLQ EDLQSVSSGS
QRVHYQDQET SFPRAISAQR LSPRWCFLDA TSADRFYRID RSQEHLHFVM EISHDEIFIL
DPDMVVSQQA GTPPGMPDLV VEQASGLSDW WNPALRKRML SDSGMITPHY EDSDLKDFSH
SRVLQSPVSS EDHAILQAVI TGDLMKLMES YKNGGSLLIQ GPGHCSLLHY AAKTGNGEIV
KYILDHGPAE LLDMADSETG ETALHKAACQ RNRAVCQLLV DAGASLRQTD SKGKTPQERA
QQAGDPDLAA YLESRQNYKI IGHEDLETAV
