Reviewed, UniProtKB/Swiss-Prot Q92903 (CDS1_HUMAN)

Names and origin

Protein names

Recommended name:
    Phosphatidate cytidylyltransferase 1
    EC=2.7.7.41
Alternative name(s):
    CDP-diglyceride pyrophosphorylase 1
    CDP-diglyceride synthetase 1
    CDP-diacylglycerol synthase 1
      Short name=CDS 1
    CTP:phosphatidate cytidylyltransferase 1
    CDP-DG synthetase 1
    CDP-DAG synthase 1

Gene names

Name:	CDS1
Synonyms:	CDS

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Provides CDP-diacylglycerol an important precursor for the synthesis of phosphatidylinositol (PtdIns), phosphatidylglycerol, and cardiolipin. Overexpression may amplify cellular signaling responses from cytokines. May also play an important role in the signal transduction mechanism of retina and neural cells.
Catalytic activity	CTP + phosphatidate = diphosphate + CDP-diacylglycerol.
Cofactor	Magnesium By similarity.
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Cytoplasmic aspect of the endoplasmic reticulum By similarity.
Tissue specificity	Expressed in adult tissues such as placenta, brain, small intestine, ovary, testis and prostate. Highly expressed in fetal kidney, lung and brain. Lower level in fetal liver.
Sequence similarities	Belongs to the CDS family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Ligand	Magnesium
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Ref.2 Traceable author statement. Source: ProtInc visual perception Ref.4 Traceable author statement. Source: ProtInc
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	diacylglycerol cholinephosphotransferase activity Ref.2 Traceable author statement. Source: ProtInc magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 461	461	Phosphatidate cytidylyltransferase 1		PRO_0000090713
Regions
	Transmembrane	96 – 116	21	Potential
	Transmembrane	149 – 169	21	Potential
	Transmembrane	183 – 203	21	Potential
	Transmembrane	230 – 250	21	Potential
	Transmembrane	279 – 299	21	Potential
	Transmembrane	357 – 377	21	Potential
Natural variations
	Natural variant	99	1	L → F: dbSNP rs36068434.		VAR_048736
	Natural variant	204	1	K → T in a breast cancer sample; somatic mutation. Ref.8		VAR_036129
Experimental info
	Sequence conflict	444 – 461	18	TLKTH…PTLKV → P in AAC50735. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q92903-1 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: E9D761BA285A5AB1	FASTA	461	53,304
	10 20 30 40 50 60 MLELRHRGSC PGPREAVSPP HREGEAAGGD HETESTSDKE TDIDDRYGDL DSRTDSDIPE 70 80 90 100 110 120 IPPSSDRTPE ILKKALSGLS SRWKNWWIRG ILTLTMISLF FLIIYMGSFM LMLLVLGIQV 130 140 150 160 170 180 KCFHEIITIG YRVYHSYDLP WFRTLSWYFL LCVNYFFYGE TVADYFATFV QREEQLQFLI 190 200 210 220 230 240 RYHRFISFAL YLAGFCMFVL SLVKKHYRLQ FYMFAWTHVT LLITVTQSHL VIQNLFEGMI 250 260 270 280 290 300 WFLVPISSVI CNDITAYLFG FFFGRTPLIK LSPKKTWEGF IGGFFSTVVF GFIAAYVLSK 310 320 330 340 350 360 YQYFVCPVEY RSDVNSFVTE CEPSELFQLQ TYSLPPFLKA VLRQERVSLY PFQIHSIALS 370 380 390 400 410 420 TFASLIGPFG GFFASGFKRA FKIKDFANTI PGHGGIMDRF DCQYLMATFV HVYITSFIRG 430 440 450 460 PNPSKVLQQL LVLQPEQQLN IYKTLKTHLI EKGILQPTLK V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of CDP-diacylglycerol synthase from a human neuronal cell line." Heacock A.M., Uhler M.D., Agranoff B.W. J. Neurochem. 67:2200-2203(1996) [PubMed: 8863531] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Neuron.
[2]	"Isolation and expression of an isoform of human CDP-diacylglycerol synthase cDNA." Weeks R., Dowhan W., Shen H., Balantac N., Meengs B., Nudelman E., Leung D.W. DNA Cell Biol. 16:281-289(1997) [PubMed: 9115637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leukocyte and Placenta.
[3]	"The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content." Lykidis A., Jackson P.D., Rock C.O., Jackowski S. J. Biol. Chem. 272:33402-33409(1997) [PubMed: 9407135] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[4]	"Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes." Halford S., Dulai K.S., Daw S.C.M., Fitzgibbon J., Hunt D.M. Genomics 54:140-144(1998) [PubMed: 9806839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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]. Tissue: Lung.
[8]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-204.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U65887 mRNA. Translation: AAC50735.1. U60808 mRNA. Translation: AAC51184.1. AK314245 mRNA. Translation: BAG36912.1. CH471057 Genomic DNA. Translation: EAX05950.1. BC074833 mRNA. Translation: AAH74833.1. BC074881 mRNA. Translation: AAH74881.1.
IPI	IPI00024234.
RefSeq	NP_001254.2.
UniGene	Hs.654899 Hs.708641
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q92903.
PTM databases
PhosphoSite	Q92903.
Proteomic databases
PRIDE	Q92903.
Genome annotation databases
Ensembl	ENST00000295887; ENSP00000295887; ENSG00000163624; Homo sapiens. [Genome view]
GeneID	1040.
KEGG	hsa:1040.
NMPDR	fig|9606.3.peg.24370.
UCSC	uc003hpb.1. human.
Organism-specific databases
CTD	1040.
GeneCards	GC04P085797.
H-InvDB	HIX0031410.
HGNC	HGNC:1800. CDS1.
MIM	603548. gene.
PharmGKB	PA26346.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q92903.
HOVERGEN	Q92903.
OMA	IEISPKK.
Enzyme and pathway databases
BRENDA	2.7.7.41. 247.
Gene expression databases
ArrayExpress	Q92903.
Bgee	Q92903.
CleanEx	HS_CDS1.
Genevestigator	Q92903.
GermOnline	ENSG00000163624. Homo sapiens.
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	4365.
SOURCE	Search...

Entry information

Entry name

CDS1_HUMAN

Accession

Primary (citable) accession number: Q92903
Secondary accession number(s): B2RAL5, O00163

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 15, 1998
Last modified:	November 3, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.