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Q6P5E8 (DGKQ_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diacylglycerol kinase theta

Short name=DAG kinase theta
EC=2.7.1.107
Alternative name(s):
Diglyceride kinase theta
Short name=DGK-theta
Gene names
Name:Dgkq
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length934 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). May regulate the activity of protein kinase C by controlling the balance between these two signaling lipids. Activated in the nucleus in response to alpha-thrombin and nerve growth factor By similarity. May be involved in cAMP-induced activation of NR5A1 and subsequent steroidogenic gene transcription by delivering PA as ligand for NR5A1. Acts synergistically with NR5A1 on CYP17 transcriptional activity By similarity.

Catalytic activity

ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.

Enzyme regulation

Inactivated by binding to RHOA. Not inhibited by phosphatidylserine By similarity.

Subunit structure

Interacts with RHOA (constitutively activated, GTP-bound); the interaction inhibits DGKQ. Interacts with PRKCE. Interacts with PRKCH. Interacts with PLCB1. Interacts with NR5A1 By similarity.

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity. Cytoplasmcytoskeleton By similarity. Nucleus By similarity. Nucleus speckle By similarity. Note: Translocates to the nucleus in response to thrombin stimulation By similarity. Translocates to the plasma membrane in response to steroid hormone receptor stimulation By similarity. Translocation to the plasma membrane is dependent on G-protein coupled receptor stimulation and subsequent activation of PRKCE and probably PRKCH By similarity.

Post-translational modification

Phosphorylated by PRKCE and PRKCH in vitro By similarity.

Sequence similarities

Belongs to the eukaryotic diacylglycerol kinase family.

Contains 1 DAGKc domain.

Contains 3 phorbol-ester/DAG-type zinc fingers.

Contains 1 Ras-associating domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6P5E8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6P5E8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-548: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 934934Diacylglycerol kinase theta
PRO_0000381763

Regions

Domain387 – 486100Ras-associating
Domain576 – 713138DAGKc
Zinc finger54 – 10249Phorbol-ester/DAG-type 1
Zinc finger115 – 16248Phorbol-ester/DAG-type 2
Zinc finger177 – 22852Phorbol-ester/DAG-type 3

Natural variations

Alternative sequence1 – 548548Missing in isoform 2.
VSP_037832

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: C7FA90936443818E

FASTA934102,254
        10         20         30         40         50         60 
MAAAAEPGAR TWPGSGSPRL GSPAGSPVLG ISGRTRPGSG PERTSRAIGS AAPGHSFRKV 

        70         80         90        100        110        120 
TLTKPTFCHL CSDFIWGLAG FLCDVCNFMS HEKCLKQVKT PCTSIAPSLV RVPVAHCFGS 

       130        140        150        160        170        180 
LGLYKRKFCV VCRKSLEVPA FRCEVCELHV HPDCVPFACS DCRQCHQDGQ QDYDTYHHHW 

       190        200        210        220        230        240 
REGNLPSGAR CEVCRKTCGS SDVLAGVRCE WCGVQAHSVC STALAPECTF GRLRSMVLPP 

       250        260        270        280        290        300 
SCVRLLSRNF SKMHCFRIPE TMVLELGDGD DGVDGSAAIG TGREVLTATE STKQTLKIFD 

       310        320        330        340        350        360 
GNDSMRKNQF RLVTVSRLAR NEEVMEAALR AYYISEDPKD FQLQALPLSG NAQALGKAGT 

       370        380        390        400        410        420 
TEEEASKGSC PRDSVPEAWV IRSLPRTQEI LKIYPGWLKV GVAYVSIRVN SQSTARSVVQ 

       430        440        450        460        470        480 
EVLPLFGQQV EDKERFQLIE VLMSSRQVQR TVLADEEPLL DRLWDIRQTS VRQVSQTRFY 

       490        500        510        520        530        540 
VAETRATAPR VSLFVGGLPP GLSPQDYSNL LHEAMATKAA VVSVSHVYSL QGAVILDVTC 

       550        560        570        580        590        600 
FAEAERLYML ARDTAVHGRP LTALVLPDVL HTKLPPDCCP LLVFVNPKSG GLKGRELLCS 

       610        620        630        640        650        660 
FRKLLNPHQV FELTNGGPLP GFHLFSQVPS FRVLVCGGDG TVGWVLAALE ETRRHLACPE 

       670        680        690        700        710        720 
PSVAILPLGT GNDLGRVLRW GAGYSGEDPF SVLVSVDEAD AVLMDRWTIL LDAHEIDSTE 

       730        740        750        760        770        780 
NNVVETEPPK IVQMNNYCGI GIDAELSLDF HQAREEEPGK FTSRFHNKGV YVRVGLQKIS 

       790        800        810        820        830        840 
HSRSLHKEIR LQVEQQEVEL PSIEGLIFIN IPSWGSGADL WGSDNDSRFE KPRIDDGLLE 

       850        860        870        880        890        900 
VVGVTGVVHM GQVQGGLRSG IRIAQGSYFR VTLLKATPVQ VDGEPWVQAP GHMIISATAP 

       910        920        930 
KVHMLRKAKQ KPRKAGANRD TRVDTLPAPE GNPL 

« Hide

Isoform 2 [UniParc].

Checksum: 8430D1C19674B841
Show »

FASTA38642,209

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Medulla oblongata.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK134745 mRNA. Translation: BAE22264.1.
BC062929 mRNA. Translation: AAH62929.1.
CCDSCCDS19515.1. [Q6P5E8-1]
RefSeqNP_950176.1. NM_199011.1. [Q6P5E8-1]
UniGeneMm.260921.

3D structure databases

ProteinModelPortalQ6P5E8.
SMRQ6P5E8. Positions 50-102, 178-229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000057859.

PTM databases

PhosphoSiteQ6P5E8.

Proteomic databases

PaxDbQ6P5E8.
PRIDEQ6P5E8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000053913; ENSMUSP00000057859; ENSMUSG00000004815. [Q6P5E8-1]
GeneID110524.
KEGGmmu:110524.
UCSCuc008yot.1. mouse. [Q6P5E8-1]
uc012eau.1. mouse. [Q6P5E8-2]

Organism-specific databases

CTD1609.
MGIMGI:102918. Dgkq.

Phylogenomic databases

eggNOGNOG47311.
GeneTreeENSGT00750000117493.
HOGENOMHOG000007900.
InParanoidQ6P5E8.
KOK00901.
OMASDFIWGL.
OrthoDBEOG71VSS6.
PhylomeDBQ6P5E8.
TreeFamTF312817.

Gene expression databases

BgeeQ6P5E8.
GenevestigatorQ6P5E8.

Family and domain databases

InterProIPR016064. ATP-NAD_kinase_PpnK-typ.
IPR020454. DAG/PE-bd.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000159. Ras-assoc.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF00130. C1_1. 2 hits.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
PF00788. RA. 2 hits.
[Graphical view]
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 3 hits.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEPS50146. DAGK. 1 hit.
PS50200. RA. 1 hit.
PS00479. ZF_DAG_PE_1. 3 hits.
PS50081. ZF_DAG_PE_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio364149.
PROQ6P5E8.
SOURCESearch...

Entry information

Entry nameDGKQ_MOUSE
AccessionPrimary (citable) accession number: Q6P5E8
Secondary accession number(s): Q3UYE8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot