DGK1_ASHGO
ID DGK1_ASHGO Reviewed; 317 AA.
AC Q753I3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=CTP-dependent diacylglycerol kinase 1;
DE EC=2.7.1.174 {ECO:0000250|UniProtKB:Q12382};
DE AltName: Full=Diglyceride kinase 1;
DE Short=DAG kinase 1;
GN Name=DGK1; Synonyms=HSD1; OrderedLocusNames=AFR329C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: CTP-dependent diacylglycerol kinase that catalyzes the
CC phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls
CC phosphatidate levels at the nuclear envelope. May be involved in
CC vesicle trafficking between the endoplasmic reticulum and the Golgi
CC apparatus. {ECO:0000250|UniProtKB:Q12382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + CTP = a 1,2-diacyl-sn-glycero-3-
CC phosphate + CDP + H(+); Xref=Rhea:RHEA:25948, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:37563, ChEBI:CHEBI:58069,
CC ChEBI:CHEBI:58608; EC=2.7.1.174;
CC Evidence={ECO:0000250|UniProtKB:Q12382};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q12382};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q12382};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q12382}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12382}. Nucleus membrane
CC {ECO:0000250|UniProtKB:Q12382}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12382}.
CC -!- SIMILARITY: Belongs to the DGK1 family. {ECO:0000305}.
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DR EMBL; AE016819; AAS53700.1; -; Genomic_DNA.
DR RefSeq; NP_985876.1; NM_211231.1.
DR AlphaFoldDB; Q753I3; -.
DR STRING; 33169.AAS53700; -.
DR EnsemblFungi; AAS53700; AAS53700; AGOS_AFR329C.
DR GeneID; 4622141; -.
DR KEGG; ago:AGOS_AFR329C; -.
DR eggNOG; KOG4453; Eukaryota.
DR HOGENOM; CLU_031477_0_1_1; -.
DR InParanoid; Q753I3; -.
DR OMA; LPVTEIH; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004143; F:diacylglycerol kinase activity; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR037997; Dgk1-like.
DR PANTHER; PTHR31303; PTHR31303; 1.
PE 3: Inferred from homology;
KW Calcium; Endoplasmic reticulum; ER-Golgi transport; Kinase; Magnesium;
KW Membrane; Nucleus; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..317
FT /note="CTP-dependent diacylglycerol kinase 1"
FT /id="PRO_0000240381"
FT TOPO_DOM 1..130
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..190
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..271
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..317
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 35399 MW; 9F9EC99A12DE022E CRC64;
MANEEELQTA ESAFVTGARR YSNDYSESES SSKHSGCSTP VEGTPAEAAT TIGARASGGS
TTWQRLRQLL MERGSDVHLP VTEIHLKSQE WFGDFITKHE VPRKVFHSSI GFFTLALYVR
DVDYRNVRLP LIVGFVHVLL LDVIRLHWPA FNTLYCQVTG LLMRKKEVHT YNGVLWYLLG
LIFAFSFFSK DVALVSLFLL SWCDTAASTV GRLYGHLTPR ISRNKSLAGS LAAFVVGVIS
CAVFYGYFVP AYSHVNHPGE IMWNPETSRL SLVQLSLLGG FVASLSEGID LFNWDDNFTI
PVLSAIFMHT IIAFSQR
