DGKA_DICDI
ID DGKA_DICDI Reviewed; 887 AA.
AC P34125; Q54ZZ0; Q86AQ4; Q8I8F4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Diacylglycerol kinase A;
DE EC=2.7.1.107;
DE AltName: Full=Myosin heavy chain kinase;
DE Short=MHCK;
GN Name=dgkA; Synonyms=mhcK; ORFNames=DDB_G0277223;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=12296770; DOI=10.1042/bj20021027;
RA De La Roche M.A., Smith J.L., Rico M., Carrasco S., Merida I., Licate L.,
RA Cote G.P., Egelhoff T.T.;
RT "Dictyostelium discoideum has a single diacylglycerol kinase gene with
RT similarity to mammalian theta isoforms.";
RL Biochem. J. 368:809-815(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=AX3;
RX PubMed=1321427; DOI=10.1073/pnas.89.13.5877;
RA Ravid S., Spudich J.A.;
RT "Membrane-bound Dictyostelium myosin heavy chain kinase: a developmentally
RT regulated substrate-specific member of the protein kinase C family.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5877-5881(1992).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16042397; DOI=10.1021/bi0507276;
RA Ostroski M., Tu-Sekine B., Raben D.M.;
RT "Analysis of a novel diacylglycerol kinase from Dictyostelium discoideum:
RT DGKA.";
RL Biochemistry 44:10199-10207(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16854454; DOI=10.1016/j.advenzreg.2006.01.018;
RA Tu-Sekine B., Ostroski M., Raben D.M.;
RT "Analysis of two diacylglycerol kinase activities in mixed micelles.";
RL Adv. Enzyme Regul. 46:12-24(2006).
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. Thereby, acts as a central switch
CC between the signaling pathways activated by these second messengers
CC with different cellular targets and opposite effects in numerous
CC biological processes. Also plays an important role in the biosynthesis
CC of complex lipids. {ECO:0000269|PubMed:12296770,
CC ECO:0000269|PubMed:16042397, ECO:0000269|PubMed:16854454}.
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:12296770, ECO:0000269|PubMed:16042397,
CC ECO:0000269|PubMed:16854454};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273;
CC Evidence={ECO:0000305|PubMed:12296770};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=148 uM for ATP (in the presence of 1,2-dioctanoyl-sn-glycerol)
CC {ECO:0000269|PubMed:16042397, ECO:0000269|PubMed:16854454};
CC KM=336 uM for ATP (in the presence of 1,2-dihexanoyl-sn-glycerol)
CC {ECO:0000269|PubMed:16042397, ECO:0000269|PubMed:16854454};
CC Vmax=40 nmol/min/mg enzyme towards ATP (in the presence of 1,2-
CC dioctanoyl-sn-glycerol) {ECO:0000269|PubMed:16042397,
CC ECO:0000269|PubMed:16854454};
CC Vmax=100 nmol/min/mg enzyme towards ATP (in the presence of 1,2-
CC dihexanoyl-sn-glycerol) {ECO:0000269|PubMed:16042397,
CC ECO:0000269|PubMed:16854454};
CC pH dependence:
CC Optimum pH is 7.0 with 1,2-dioctanoyl-sn-glycerol as a substrate, and
CC 7.4 with 1,2-dihexanoyl-sn-glycerol as a substrate.
CC {ECO:0000269|PubMed:16042397, ECO:0000269|PubMed:16854454};
CC -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC {ECO:0000305|PubMed:12296770}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P23743}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:1321427}; Peripheral
CC membrane protein {ECO:0000269|PubMed:1321427}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low level during vegetative growth
CC and during early development. Higher levels of expression are detected
CC later during development (12-24 hours). {ECO:0000269|PubMed:12296770,
CC ECO:0000269|PubMed:1321427}.
CC -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
CC {ECO:0000305}.
CC -!- CAUTION: The initially described myosin heavy chain kinase activity is
CC probably artifactual due to numerous errors in the sequence used for
CC characterization. {ECO:0000305|PubMed:1321427}.
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DR EMBL; AY152858; AAN39880.1; -; Genomic_DNA.
DR EMBL; AAFI02000019; EAL68797.1; -; Genomic_DNA.
DR EMBL; M93393; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A46136; A46136.
DR RefSeq; XP_642726.1; XM_637634.1.
DR AlphaFoldDB; P34125; -.
DR STRING; 44689.DDB0185037; -.
DR PaxDb; P34125; -.
DR PRIDE; P34125; -.
DR EnsemblProtists; EAL68797; EAL68797; DDB_G0277223.
DR GeneID; 8620920; -.
DR KEGG; ddi:DDB_G0277223; -.
DR dictyBase; DDB_G0277223; dgkA.
DR eggNOG; KOG0694; Eukaryota.
DR eggNOG; KOG1169; Eukaryota.
DR HOGENOM; CLU_325282_0_0_1; -.
DR InParanoid; P34125; -.
DR OMA; HCAMKAQ; -.
DR PhylomeDB; P34125; -.
DR BRENDA; 2.7.11.7; 1939.
DR Reactome; R-DDI-114508; Effects of PIP2 hydrolysis.
DR SABIO-RK; P34125; -.
DR UniPathway; UPA00230; -.
DR PRO; PR:P34125; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0019992; F:diacylglycerol binding; IDA:UniProtKB.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IDA:dictyBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IMP:dictyBase.
DR GO; GO:0071398; P:cellular response to fatty acid; IMP:dictyBase.
DR GO; GO:0071285; P:cellular response to lithium ion; IMP:dictyBase.
DR GO; GO:0046339; P:diacylglycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0046834; P:lipid phosphorylation; ISS:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:dictyBase.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0050926; P:regulation of positive chemotaxis; IMP:dictyBase.
DR CDD; cd00029; C1; 3.
DR Gene3D; 3.40.50.10330; -; 1.
DR InterPro; IPR017438; ATP-NAD_kinase_N.
DR InterPro; IPR046349; C1-like_sf.
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; PF00130; C1_1; 3.
DR Pfam; PF00609; DAGK_acc; 1.
DR Pfam; PF00781; DAGK_cat; 1.
DR SMART; SM00109; C1; 3.
DR SMART; SM00045; DAGKa; 1.
DR SMART; SM00046; DAGKc; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
DR SUPFAM; SSF57889; SSF57889; 3.
DR PROSITE; PS50146; DAGK; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Lipid metabolism; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..887
FT /note="Diacylglycerol kinase A"
FT /id="PRO_0000218476"
FT DOMAIN 330..473
FT /note="DAGKc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00783"
FT ZN_FING 7..57
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 140..190
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 208..259
FT /note="Phorbol-ester/DAG-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 64..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..743
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 828
FT /note="D -> E (in Ref. 1; AAN39880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 887 AA; 99177 MW; B93209A9876B6132 CRC64;
MNQLNISHNW KIKSFTSITF CDHCGSMLWG ICTQGFQCSD CNFSAHSHCT NLVTLHCNNN
KNNSKPNEKP ATITAAAASS STTTTTTTET STNTAASTTT TTNNIDIKNK DKTPTTSPFS
SPILSSYNNN SGNEFCSNRQ HKFHKTSKSI TKFCNYCRET TFTISGEPVM CSECRYIAHG
HCQTKVPLNC IIPYSSPINT INDGGNVRHH WVEGNLKKSK KCIHCMEPCE KSFSLAHYKC
LWCHKYLHSS CFDKHNPICD FGSLSDMILP PSSIRLLSTT ATTTNKIEKL IIEEQQPQLS
SSPSSPRLNI NNNNNNNEII EWELIENSNM PEKVLFVFVN SKSGGQFGST LIRKLSSLLN
PLQIIDLIKC GGPDSTLQMI NRYLAKHPEQ TNRFRILVCG GDGTVGWLFK QMTKHLVPST
IPIGIIPLGT GNDLARSLGW GIGYDGEKLI EILKSINEAK TIQMDTWSIE MWDDDKPEDR
RVIEMNNYFS IGLDAMVALG FHLARNANPQ LFTGRTVNKL WYTKIGLEEF VTKNFVSLAR
IVKINVGTRE IRVDRSIEGI IILNLGSYAG GVDLWGANRK DNQTHSDGTG NQFIDDQTLE
IVGVTSLPHL GSCLSSISSP IKMGQADEIR IQVSMPSIIL KDKSNEIETA FQVDGEPEPI
EVRNCTFKIS FFKKVSMLSN RSFKPRIENH DSDLSTFQIS QSPNLYSPPS FKNPPPNLNQ
YQQPHQPPQS QPQPQPQPQQ SLQSPQSPEP INNNTNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNNNNSNN NNNNISNDLT NNSEVNPEKS TNNEKTNDNN NNNNNNINTP
FEPISLPDEN NNNNNNNNNN NNNNNNNNNN NETNSEKSYT NNCDEVD
