DGK1_SCHPO
ID DGK1_SCHPO Reviewed; 218 AA.
AC P87170;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=CTP-dependent diacylglycerol kinase 1;
DE EC=2.7.1.174 {ECO:0000250|UniProtKB:Q12382};
DE AltName: Full=Diglyceride kinase 1 {ECO:0000250|UniProtKB:Q12382};
DE Short=DAG kinase 1 {ECO:0000250|UniProtKB:Q12382};
GN Name=ptp4; Synonyms=dgk1 {ECO:0000250|UniProtKB:Q12382};
GN ORFNames=SPBC3D6.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TRANSMEMBRANE DOMAINS.
RX PubMed=11955632; DOI=10.1016/s0167-4781(01)00353-0;
RA Kim M., Hwang K., Lim C.-J., Kim D.;
RT "A potential membrane protein involved in pre-tRNA splicing of
RT Schizosaccharomyces pombe.";
RL Biochim. Biophys. Acta 1574:210-214(2002).
RN [2] {ECO:0000312|EMBL:CAB09125.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=26990381; DOI=10.1111/tra.12394;
RA Meyers A., Del Rio Z.P., Beaver R.A., Morris R.M., Weiskittel T.M.,
RA Alshibli A.K., Mannik J., Morrell-Falvey J., Dalhaimer P.;
RT "Lipid droplets form from distinct regions of the cell in the fission yeast
RT Schizosaccharomyces pombe.";
RL Traffic 17:657-669(2016).
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. Counteracts the activity
CC of PA phosphatase ned1. May be involved in vesicle trafficking between
CC the endoplasmic reticulum and the Golgi apparatus (By similarity).
CC Involved in pre-tRNA splicing (PubMed:11955632).
CC {ECO:0000250|UniProtKB:Q12382, ECO:0000269|PubMed:11955632}.
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:0000269|PubMed:16823372, ECO:0000269|PubMed:26990381}; Multi-pass
CC membrane protein {ECO:0000255}. Nucleus membrane
CC {ECO:0000269|PubMed:26990381}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the DGK1 family. {ECO:0000255}.
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DR EMBL; CU329671; CAB09125.1; -; Genomic_DNA.
DR PIR; T40365; T40365.
DR RefSeq; NP_595517.1; NM_001021426.2.
DR AlphaFoldDB; P87170; -.
DR BioGRID; 277514; 39.
DR STRING; 4896.SPBC3D6.05.1; -.
DR MaxQB; P87170; -.
DR PaxDb; P87170; -.
DR EnsemblFungi; SPBC3D6.05.1; SPBC3D6.05.1:pep; SPBC3D6.05.
DR GeneID; 2540998; -.
DR KEGG; spo:SPBC3D6.05; -.
DR PomBase; SPBC3D6.05; ptp4.
DR VEuPathDB; FungiDB:SPBC3D6.05; -.
DR eggNOG; KOG4453; Eukaryota.
DR HOGENOM; CLU_031477_1_0_1; -.
DR InParanoid; P87170; -.
DR OMA; LPVTEIH; -.
DR PhylomeDB; P87170; -.
DR PRO; PR:P87170; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0004143; F:diacylglycerol kinase activity; ISO:PomBase.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISO:PomBase.
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..218
FT /note="CTP-dependent diacylglycerol kinase 1"
FT /id="PRO_0000371716"
FT TOPO_DOM 1..19
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..88
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..179
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q12382"
SQ SEQUENCE 218 AA; 24397 MW; D934354CE978A667 CRC64;
MSTKLTWSQW SKKHEIPRKA LHTSIGFFAL LLQGCGYHAA QIIPVIEIGF IPAFTGDVIR
FNWPAFSRLY NRVIGPLMRE SEKNAWNGVI FYMIGVWIVL KVFPEEIAVM SVLLLSWCDT
TASTVGRKWG KYTPKIAKNK SLAGSLGAFV CGVFCCYVYW GLFRTGPDSL AAQSRIPFPW
LCLINGFIGA FAEAMDVWGL DDNLVIPVVS ACLLYLIM
