Reviewed, UniProtKB/Swiss-Prot Q99L43 (CDS2_MOUSE)

Names and origin

Protein names

Recommended name:
    Phosphatidate cytidylyltransferase 2
    EC=2.7.7.41
Alternative name(s):
    CDP-diglyceride pyrophosphorylase 2
    CDP-diglyceride synthetase 2
    CDP-diacylglycerol synthase 2
      Short name=CDS 2
    CTP:phosphatidate cytidylyltransferase 2
    CDP-DG synthetase 2
    CDP-DAG synthase 2

Gene names

Name:

Cds2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Provides CDP-diacylglycerol an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin 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 inner membrane; Multi-pass membrane protein; Matrix side Potential.
Sequence similarities	Belongs to the CDS family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transmembrane
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane 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 – 444	444	Phosphatidate cytidylyltransferase 2		PRO_0000090717
Regions
	Transmembrane	78 – 98	21	Potential
	Transmembrane	129 – 149	21	Potential
	Transmembrane	165 – 185	21	Potential
	Transmembrane	212 – 232	21	Potential
	Transmembrane	261 – 281	21	Potential
	Transmembrane	339 – 359	21	Potential
Amino acid modifications
	Modified residue	20	1	Phosphoserine Ref.6
	Modified residue	22	1	Phosphoserine By similarity
	Modified residue	30	1	Phosphothreonine Ref.6
	Modified residue	32	1	Phosphoserine Ref.6 Ref.4 Ref.5 Ref.7
	Modified residue	36	1	Phosphoserine By similarity
	Modified residue	46	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	43	1	L → P in AAH69879. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q99L43-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 6A3568A7E90A6C53	FASTA	444	51,314
	10 20 30 40 50 60 MTELRQRVVR EDAPPEDKES ESEAKLDGET ASDSESRAET APLPTSVDDT PEVLNRALSN 70 80 90 100 110 120 LSSRWKNWWV RGILTLAMIA FFFIIIYLGP MVLMMIVMCV QIKCFHEIIT IGYNVYHSYD 130 140 150 160 170 180 LPWFRTLSWY FLLCVNYFFY GETVTDYFFT LVQREEPLRI LSKYHRFISF ALYLTGFCMF 190 200 210 220 230 240 VLSLVKKHYR LQFYMFGWTH VTLLIVVTQS HLVIHNLFEG MIWFIVPISC VICNDIMAYM 250 260 270 280 290 300 FGFFFGRTPL IKLSPKKTWE GFIGGFFATV VFGLLLSYVM SGYRCFVCPV EYNNDTNSFT 310 320 330 340 350 360 VDCEPSDLFR LQEYNIPGVI QSAIGWKTVR MYPFQIHSIA LSTFASLIGP FGGFFASGFK 370 380 390 400 410 420 RAFKIKDFAN TIPGHGGIMD RFDCQYLMAT FVNVYIASFI RGPNPSKLIQ QFLTLRPDQQ 430 440 LHIFNTLKSH LTDKGILTSA LEDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of murine Cds (CDP-diacylglycerol synthase) 1 and 2." Inglis S.L., Hunt D.M., Halford S. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum, Embryonic stem cell and Lung.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Embryo and Mammary tumor.
[4]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, MASS SPECTROMETRY. Tissue: Brain cortex.
[5]	"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS." Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y. Mol. Cell. Proteomics 6:669-676(2007) [PubMed: 17208939] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; THR-30; SER-32 AND SER-46, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY159802 mRNA. Translation: AAO17790.1. AK036328 mRNA. Translation: BAC29384.1. AK147541 mRNA. Translation: BAE27984.1. AK166001 mRNA. Translation: BAE38511.1. BC003852 mRNA. Translation: AAH03852.1. BC069879 mRNA. Translation: AAH69879.1.
IPI	IPI00468999.
RefSeq	NP_619592.1.
UniGene	Mm.284503
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q99L43.
PTM databases
PhosphoSite	Q99L43.
Proteomic databases
PRIDE	Q99L43.
Genome annotation databases
Ensembl	ENSMUST00000103181; ENSMUSP00000099470; ENSMUSG00000058793; Mus musculus. [Genome view]
GeneID	110911.
KEGG	mmu:110911.
NMPDR	fig|10090.3.peg.6963.
UCSC	uc008mmo.1. mouse.
Organism-specific databases
CTD	110911.
MGI	MGI:1332236. Cds2.
Phylogenomic databases
HOGENOM	Q99L43.
HOVERGEN	Q99L43.
OMA	PDQQLHI.
Enzyme and pathway databases
BRENDA	2.7.7.41. 244.
Gene expression databases
ArrayExpress	Q99L43.
Bgee	Q99L43.
Genevestigator	Q99L43.
GermOnline	ENSMUSG00000058793. Mus musculus.
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...
Other Resources
NextBio	364917.
SOURCE	Search...

Entry information

Entry name

CDS2_MOUSE

Accession

Primary (citable) accession number: Q99L43
Secondary accession number(s): Q3TMD1, Q6NSU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 1, 2001
Last modified:	November 3, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)