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UniProtKB/Swiss-Prot entry Q9P381


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CDSH_SCHPO
Primary accession number Q9P381
Secondary accession numbers None
Integrated into Swiss-Prot on February 5, 2008
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 38)
Name and origin of the protein
Protein name Putative phosphatidate cytidylyltransferase
Synonyms EC 2.7.7.41
CDP-diglyceride pyrophosphorylase
CDP-diglyceride synthetase
CDP-diacylglycerol synthase
CDS
CTP:phosphatidate cytidylyltransferase
CDP-DG synthetase
CDP-DAG synthase
Gene name
ORFNames: SPBC13A2.03
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CU329671; CAB99396.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_596416.1; -.
3D structure databases
ModBase Q9P381.
Organism-specific databases
GeneDB_Spombe SPBC13A2.03; -.
Gene expression databases
ArrayExpress Q9P381; -.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031966; Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004605; Molecular function: phosphatidate cytidylyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008654; Biological process: phospholipid biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000374; PC_trans.
IPR016720; PC_Trfase_euk.
Graphical view of domain structure.
Pfam PF01148; CTP_transf_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF018269; PC_trans_euk; 1.
PROSITE PS01315; CDS; 1.
ProtoNet Q9P381.
Genome annotation databases
GeneID 2540017; -.
KEGG spo:SPBC13A2.03; -.
NMPDR fig|4896.1.peg.2282; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Endoplasmic reticulum; Membrane; Mitochondrion; Nucleotidyltransferase; Phospholipid biosynthesis; Phosphoprotein; Transferase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   439  439     Putative phosphatidate cytidylyltransferase. PRO_0000316216
TRANSMEM   52    71  20     Potential. 
TRANSMEM   76    98  23     Potential. 
TRANSMEM   110   130  21     Potential. 
TRANSMEM   145   165  21     Potential. 
TRANSMEM   180   199  20     Potential. 
TRANSMEM   245   265  21     Potential. 
TRANSMEM   321   341  21     Potential. 
MOD_RES   12    12        Phosphoserine. 
Sequence information
Length: 439 AA [This is the length of the unprocessed precursor] Molecular weight: 49937 Da [This is the MW of the unprocessed precursor] CRC64: 8285DA1826049BB7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MARKRTNKRN NSDKENGNVG VVQNKDSASS KTTEPARLTK HKSLARKPSQ NFITRTIWTF 

        70         80         90        100        110        120 
LLLGIFFTAL AMGHFWVVLL VTIVQIGVYK EVIAIASVPS REKDLPWTRF INWYFLMTTL 

       130        140        150        160        170        180 
YYAYGESIYA YFHHLFIMDS FMLPLVLHHR FISFMLYIIG FVLFVASLKK GNYKFQFSQF 

       190        200        210        220        230        240 
CWTHMTLLLV VGQSHFMINN LFEGLFWFFV PVCYVVCNDV FAYLCGKMFG KHPLIQVSPK 

       250        260        270        280        290        300 
KTVEGFLGGW ICTVVIGSLI SYVLMHFKYF ICPTRDLSTS AFSGLNCTPN SVFLPHTYTI 

       310        320        330        340        350        360 
PAVFVDTFRL PETITLAPIY FHLAIFATFS SLIAPFGGFF ASGLKRAFKI KDFGASIPGH 

       370        380        390        400        410        420 
GGLTDRMDCQ FLNGVFVYMY FQSFIAEKST SVADLLDTAV YSLTTTQQVQ LVEDLQNYLI 

       430 
SHGKTSVQAI CSKLLQNSK 

Q9P381 in FASTA format

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