Q92903 (CDS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphatidate cytidylyltransferase 1
EC=2.7.7.41

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

Gene names

Name:	CDS1
Synonyms:	CDS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
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	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Magnesium
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CDP-diacylglycerol biosynthetic process Inferred from direct assay Ref.3. Source: UniProtKB phosphatidylinositol biosynthetic process Inferred from direct assay Ref.3. Source: UniProtKB phototransduction Non-traceable author statement Ref.4. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	diacylglycerol cholinephosphotransferase activity Non-traceable author statement Ref.2. Source: UniProtKB phosphatidate cytidylyltransferase activity Inferred from direct assay Ref.3. Source: UniProtKB
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	Helical; Potential
	Transmembrane	149 – 169	21	Helical; Potential
	Transmembrane	183 – 203	21	Helical; Potential
	Transmembrane	230 – 250	21	Helical; Potential
	Transmembrane	279 – 299	21	Helical; Potential
	Transmembrane	357 – 377	21	Helical; Potential
Natural variations
	Natural variant	99	1	L → F. Corresponds to variant rs36068434 [ dbSNP | Ensembl ].		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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-204.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. NM_001263.3.
UniGene	Hs.654899. Hs.708641.
3D structure databases
ProteinModelPortal	Q92903.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000295887.
PTM databases
PhosphoSite	Q92903.
Polymorphism databases
DMDM	3123204.
Proteomic databases
PaxDb	Q92903.
PRIDE	Q92903.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000295887; ENSP00000295887; ENSG00000163624.
GeneID	1040.
KEGG	hsa:1040.
UCSC	uc011ccv.2. human.
Organism-specific databases
CTD	1040.
GeneCards	GC04P085428.
HGNC	HGNC:1800. CDS1.
HPA	HPA036187.
MIM	603548. gene.
neXtProt	NX_Q92903.
PharmGKB	PA26346.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0575.
HOGENOM	HOG000209582.
HOVERGEN	HBG002485.
InParanoid	Q92903.
KO	K00981.
OMA	WVIRGIF.
OrthoDB	EOG4V437K.
PhylomeDB	Q92903.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00557; UER00614.
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
GenomeRNAi	1040.
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:	April 3, 2013
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.