Reviewed, UniProtKB/Swiss-Prot Q9P381 (CDSH_SCHPO)

Names and origin

Protein names

Recommended name:
    Putative phosphatidate cytidylyltransferase
    EC=2.7.7.41
Alternative name(s):
    CDP-diglyceride pyrophosphorylase
    CDP-diglyceride synthetase
    CDP-diacylglycerol synthase
      Short name=CDS
    CTP:phosphatidate cytidylyltransferase
    CDP-DG synthetase
    CDP-DAG synthase

Gene names

ORF Names:

SPBC13A2.03

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Supplies CDP-diacylglycerol, which may play an important role as both a precursor to phosphoinositide biosynthesis in the plasma membrane and as a negative effector of phosphatidylinositol 4-kinase activity, thereby exerting an effect on cell proliferation via a lipid-dependent signal transduction cascade By similarity.
Catalytic activity	CTP + phosphatidate = diphosphate + CDP-diacylglycerol.
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Subcellular location	Mitochondrion membrane; Multi-pass membrane protein By similarity. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the CDS family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane Mitochondrion
Domain	Transmembrane
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Ref.2 Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphatidate cytidylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 439	439	Putative phosphatidate cytidylyltransferase		PRO_0000316216
Regions
	Transmembrane	52 – 71	20	Potential
	Transmembrane	76 – 98	23	Potential
	Transmembrane	110 – 130	21	Potential
	Transmembrane	145 – 165	21	Potential
	Transmembrane	180 – 199	20	Potential
	Transmembrane	245 – 265	21	Potential
	Transmembrane	321 – 341	21	Potential
Amino acid modifications
	Modified residue	12	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9P381-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 8285DA1826049BB7	FASTA	439	49,937
	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

References

[1]	"The genome sequence of Schizosaccharomyces pombe." 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. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAB99396.1.
RefSeq	NP_596416.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9P381.
Genome annotation databases
GeneID	2540017.
KEGG	spo:SPBC13A2.03.
NMPDR	fig|4896.1.peg.2282.
Organism-specific databases
GeneDB_Spombe	SPBC13A2.03.
Phylogenomic databases
OMA	IEISPKK.
Enzyme and pathway databases
BRENDA	2.7.7.41. 653.
Gene expression databases
ArrayExpress	Q9P381.
Family and domain databases
InterPro	IPR000374. PC_trans. IPR016720. PC_Trfase_euk. [Graphical view]
Pfam	PF01148. CTP_transf_1. 1 hit. [Graphical view]
PIRSF	PIRSF018269. PC_trans_euk. 1 hit.
PROSITE	PS01315. CDS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDSH_SCHPO

Accession

Primary (citable) accession number: Q9P381

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)