CDSH_SCHPO
ID CDSH_SCHPO Reviewed; 439 AA.
AC Q9P381;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putative phosphatidate cytidylyltransferase;
DE EC=2.7.7.41;
DE AltName: Full=CDP-DAG synthase;
DE AltName: Full=CDP-DG synthase;
DE AltName: Full=CDP-diacylglycerol synthase;
DE Short=CDS;
DE AltName: Full=CDP-diglyceride pyrophosphorylase;
DE AltName: Full=CDP-diglyceride synthase;
DE AltName: Full=CTP:phosphatidate cytidylyltransferase;
GN ORFNames=SPBC13A2.03;
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]
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 [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Supplies CDP-diacylglycerol, which may play an important role
CC as both a precursor to phosphoinositide biosynthesis in the plasma
CC membrane and as a negative effector of phosphatidylinositol 4-kinase
CC activity, thereby exerting an effect on cell proliferation via a lipid-
CC dependent signal transduction cascade. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR EMBL; CU329671; CAB99396.1; -; Genomic_DNA.
DR RefSeq; NP_596416.1; NM_001022335.2.
DR AlphaFoldDB; Q9P381; -.
DR STRING; 4896.SPBC13A2.03.1; -.
DR iPTMnet; Q9P381; -.
DR MaxQB; Q9P381; -.
DR PaxDb; Q9P381; -.
DR PRIDE; Q9P381; -.
DR EnsemblFungi; SPBC13A2.03.1; SPBC13A2.03.1:pep; SPBC13A2.03.
DR GeneID; 2540017; -.
DR KEGG; spo:SPBC13A2.03; -.
DR PomBase; SPBC13A2.03; -.
DR VEuPathDB; FungiDB:SPBC13A2.03; -.
DR eggNOG; KOG1440; Eukaryota.
DR HOGENOM; CLU_023471_1_1_1; -.
DR InParanoid; Q9P381; -.
DR OMA; FIMNNIF; -.
DR PhylomeDB; Q9P381; -.
DR BRENDA; 2.7.7.41; 5613.
DR Reactome; R-SPO-1483148; Synthesis of PG.
DR Reactome; R-SPO-1483226; Synthesis of PI.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:Q9P381; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISM:PomBase.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IDA:PomBase.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IDA:PomBase.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; ISS:PomBase.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; ISS:PomBase.
DR InterPro; IPR000374; PC_trans.
DR InterPro; IPR016720; PC_Trfase_euk.
DR PANTHER; PTHR13773; PTHR13773; 1.
DR PIRSF; PIRSF018269; PC_trans_euk; 1.
DR PROSITE; PS01315; CDS; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Membrane; Nucleotidyltransferase; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..439
FT /note="Putative phosphatidate cytidylyltransferase"
FT /id="PRO_0000316216"
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 439 AA; 49937 MW; 8285DA1826049BB7 CRC64;
MARKRTNKRN NSDKENGNVG VVQNKDSASS KTTEPARLTK HKSLARKPSQ NFITRTIWTF
LLLGIFFTAL AMGHFWVVLL VTIVQIGVYK EVIAIASVPS REKDLPWTRF INWYFLMTTL
YYAYGESIYA YFHHLFIMDS FMLPLVLHHR FISFMLYIIG FVLFVASLKK GNYKFQFSQF
CWTHMTLLLV VGQSHFMINN LFEGLFWFFV PVCYVVCNDV FAYLCGKMFG KHPLIQVSPK
KTVEGFLGGW ICTVVIGSLI SYVLMHFKYF ICPTRDLSTS AFSGLNCTPN SVFLPHTYTI
PAVFVDTFRL PETITLAPIY FHLAIFATFS SLIAPFGGFF ASGLKRAFKI KDFGASIPGH
GGLTDRMDCQ FLNGVFVYMY FQSFIAEKST SVADLLDTAV YSLTTTQQVQ LVEDLQNYLI
SHGKTSVQAI CSKLLQNSK
