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Protein

Diacylglycerol kinase alpha

Gene

DGKA

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity.

Catalytic activityi

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

Enzyme regulationi

Stimulated by calcium and phosphatidylserine. Phosphorylated by protein kinase C.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi122 – 133121CuratedAdd
BLAST
Calcium bindingi167 – 178122CuratedAdd
BLAST
Zinc fingeri204 – 25249Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri268 – 31851Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.1.107. 6170.
ReactomeiREACT_280066. Effects of PIP2 hydrolysis.
SABIO-RKP20192.

Names & Taxonomyi

Protein namesi
Recommended name:
Diacylglycerol kinase alpha (EC:2.7.1.107)
Short name:
DAG kinase alpha
Alternative name(s):
80 kDa diacylglycerol kinase
Diglyceride kinase alpha
Short name:
DGK-alpha
Gene namesi
Name:DGKA
Synonyms:DAGK, DAGK1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Chromosome 5

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi248 – 2481K → R: No decrease in activity. 1 Publication
Mutagenesisi383 – 3831K → N: No decrease in activity. 1 Publication
Mutagenesisi395 – 3951K → N: No decrease in activity. 1 Publication
Mutagenesisi483 – 4831K → N: No decrease in activity. 1 Publication
Mutagenesisi492 – 4921K → R: No decrease in activity. 1 Publication
Mutagenesisi554 – 5541K → N: No decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 734734Diacylglycerol kinase alphaPRO_0000218455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei483 – 4831N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Expressioni

Tissue specificityi

Lymphocytes and oligodendroglial cells.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000000387.

Structurei

3D structure databases

ProteinModelPortaliP20192.
SMRiP20192. Positions 1-117.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 14436EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini154 – 18936EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini371 – 505135DAGKcPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DAGKc domain.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri204 – 25249Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri268 – 31851Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG47311.
GeneTreeiENSGT00760000119050.
HOGENOMiHOG000252931.
HOVERGENiHBG051345.
InParanoidiP20192.
KOiK00901.
OMAiVGLHCVW.
OrthoDBiEOG75XGK8.
TreeFamiTF313104.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.238.110. 1 hit.
InterProiIPR029477. DAG_kinase_typeI_N.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR016064. NAD/diacylglycerol_kinase.
IPR002219. PE/DAG-bd.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF14513. DAG_kinase_N. 2 hits.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 2 hits.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 2 hits.
PROSITEiPS50146. DAGK. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20192-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKERGLISP SDFAQLQKYM EYSTKKVSDV LKLFEDGEMA EYLQGDAIGY
60 70 80 90 100
EGFQQFLKIY LEVDSVPSHL SLALFQSFQT SYCSEETVKR DVVCLSDVSC
110 120 130 140 150
YFSLLEGGRP EDKLEFTFKL YDTDRNGILD SSEVDRIIIQ MMRMAEYLDW
160 170 180 190 200
DVSELRPILQ EMMKEIDYDG SGSVSLAEWL RAGATTVPLL VLLGLEMTLK
210 220 230 240 250
DNGQHMWRPK RFPRPVYCNL CESSIGLGKQ GLSCNLCKYT VHDQCAMKAL
260 270 280 290 300
PCEVSTYAKS RKDIGVQTHV WVRGGCESGR CDRCQKKIRI YHSLVGLHCV
310 320 330 340 350
WCHLEIHDDC LPAMGHECDC GLLRDHILPP SSIYPSVLAS GQERKVSKTS
360 370 380 390 400
QKTTDDLNLS TSEALRIDPV SNTHPLLVFV NPKSGGKQGE RVLWKFQYLL
410 420 430 440 450
NPRQVFNLLK DGPEPGLRFF REVPDYRILV CGGDGTVGWI LETIDKANLP
460 470 480 490 500
FVPPVAVLPL GTGNDLARCL RWGGGYEGQN LGKILKDLEA SKVVHMDRWS
510 520 530 540 550
VEVIPQQTEE KSDPVPFQII NNYFSIGVDA SIAHRFHIMR EKYPEKFNSR
560 570 580 590 600
MKNKLWYFEF ATSESIFSTC KKLEESLTVE ICGKPLDLSN LSLEGIAVLN
610 620 630 640 650
IPSTHGGSNL WGDTKRPHGD IHGINQALGA MAKVITDPDI LKTCVPDLSD
660 670 680 690 700
KRLEVVGLEG AIEMGQIYTK LKNAGHRLAK CSEITFHTTK TLPMQIDGEP
710 720 730
WMQTPCTIKI THRNQMPMLV GPPPRSSNFF GFLC
Length:734
Mass (Da):82,606
Last modified:February 1, 1991 - v1
Checksum:i711C2E66FB4B4E80
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53256 mRNA. Translation: CAA37347.1.
PIRiS09156.
RefSeqiNP_999197.1. NM_214032.2.
XP_005663934.1. XM_005663877.1.
UniGeneiSsc.54911.

Genome annotation databases

EnsembliENSSSCT00000000393; ENSSSCP00000000387; ENSSSCG00000000370.
GeneIDi397097.
KEGGissc:397097.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53256 mRNA. Translation: CAA37347.1.
PIRiS09156.
RefSeqiNP_999197.1. NM_214032.2.
XP_005663934.1. XM_005663877.1.
UniGeneiSsc.54911.

3D structure databases

ProteinModelPortaliP20192.
SMRiP20192. Positions 1-117.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000000387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000000393; ENSSSCP00000000387; ENSSSCG00000000370.
GeneIDi397097.
KEGGissc:397097.

Organism-specific databases

CTDi1606.

Phylogenomic databases

eggNOGiNOG47311.
GeneTreeiENSGT00760000119050.
HOGENOMiHOG000252931.
HOVERGENiHBG051345.
InParanoidiP20192.
KOiK00901.
OMAiVGLHCVW.
OrthoDBiEOG75XGK8.
TreeFamiTF313104.

Enzyme and pathway databases

BRENDAi2.7.1.107. 6170.
ReactomeiREACT_280066. Effects of PIP2 hydrolysis.
SABIO-RKP20192.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.238.110. 1 hit.
InterProiIPR029477. DAG_kinase_typeI_N.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR016064. NAD/diacylglycerol_kinase.
IPR002219. PE/DAG-bd.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF14513. DAG_kinase_N. 2 hits.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 2 hits.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 2 hits.
PROSITEiPS50146. DAGK. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Porcine diacylglycerol kinase sequence has zinc finger and E-F hand motifs."
    Sakane F., Yamada K., Kanoh H., Yokoyama C., Tanabe T.
    Nature 344:345-348(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Lymphocyte.
  2. "The C-terminal part of diacylglycerol kinase alpha lacking zinc fingers serves as a catalytic domain."
    Sakane F., Kai M., Wada I., Imai S., Kanoh H.
    Biochem. J. 318:583-590(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN CATALYTIC, MUTAGENESIS.

Entry informationi

Entry nameiDGKA_PIG
AccessioniPrimary (citable) accession number: P20192
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: April 29, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.