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Q92903

- CDS1_HUMAN

UniProt

Q92903 - CDS1_HUMAN

Protein

Phosphatidate cytidylyltransferase 1

Gene

CDS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    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 activityi

    CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

    Cofactori

    Magnesium.By similarity

    Pathwayi

    GO - Molecular functioni

    1. diacylglycerol cholinephosphotransferase activity Source: UniProtKB
    2. phosphatidate cytidylyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. CDP-choline pathway Source: GOC
    2. CDP-diacylglycerol biosynthetic process Source: UniProtKB
    3. glycerophospholipid biosynthetic process Source: Reactome
    4. phosphatidylinositol biosynthetic process Source: UniProtKB
    5. phospholipid metabolic process Source: Reactome
    6. phototransduction Source: UniProtKB
    7. signal transduction Source: UniProtKB
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    ReactomeiREACT_121000. Synthesis of PI.
    UniPathwayiUPA00557; UER00614.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:CDS1
    Synonyms:CDS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:1800. CDS1.

    Subcellular locationi

    Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
    Note: Cytoplasmic aspect of the endoplasmic reticulum.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26346.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Phosphatidate cytidylyltransferase 1PRO_0000090713Add
    BLAST

    Proteomic databases

    MaxQBiQ92903.
    PaxDbiQ92903.
    PRIDEiQ92903.

    PTM databases

    PhosphoSiteiQ92903.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiQ92903.
    BgeeiQ92903.
    CleanExiHS_CDS1.
    GenevestigatoriQ92903.

    Organism-specific databases

    HPAiHPA036187.

    Interactioni

    Subunit structurei

    Interacts with FOS; this interaction may enhance catalytic activity.By similarity

    Protein-protein interaction databases

    BioGridi107471. 2 interactions.
    STRINGi9606.ENSP00000295887.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92903.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei96 – 11621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei149 – 16921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei183 – 20321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei230 – 25021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei279 – 29921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei357 – 37721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CDS family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0575.
    HOGENOMiHOG000209582.
    HOVERGENiHBG002485.
    InParanoidiQ92903.
    KOiK00981.
    OMAiNFAWTHM.
    OrthoDBiEOG7M98G5.
    PhylomeDBiQ92903.
    TreeFamiTF313464.

    Family and domain databases

    InterProiIPR000374. PC_trans.
    IPR016720. PC_Trfase_euk.
    [Graphical view]
    PfamiPF01148. CTP_transf_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018269. PC_trans_euk. 1 hit.
    PROSITEiPS01315. CDS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q92903-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLELRHRGSC PGPREAVSPP HREGEAAGGD HETESTSDKE TDIDDRYGDL    50
    DSRTDSDIPE IPPSSDRTPE ILKKALSGLS SRWKNWWIRG ILTLTMISLF 100
    FLIIYMGSFM LMLLVLGIQV KCFHEIITIG YRVYHSYDLP WFRTLSWYFL 150
    LCVNYFFYGE TVADYFATFV QREEQLQFLI RYHRFISFAL YLAGFCMFVL 200
    SLVKKHYRLQ FYMFAWTHVT LLITVTQSHL VIQNLFEGMI WFLVPISSVI 250
    CNDITAYLFG FFFGRTPLIK LSPKKTWEGF IGGFFSTVVF GFIAAYVLSK 300
    YQYFVCPVEY RSDVNSFVTE CEPSELFQLQ TYSLPPFLKA VLRQERVSLY 350
    PFQIHSIALS TFASLIGPFG GFFASGFKRA FKIKDFANTI PGHGGIMDRF 400
    DCQYLMATFV HVYITSFIRG PNPSKVLQQL LVLQPEQQLN IYKTLKTHLI 450
    EKGILQPTLK V 461
    Length:461
    Mass (Da):53,304
    Last modified:July 15, 1998 - v2
    Checksum:iE9D761BA285A5AB1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti444 – 46118TLKTH…PTLKV → P in AAC50735. (PubMed:8863531)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti99 – 991L → F.
    Corresponds to variant rs36068434 [ dbSNP | Ensembl ].
    VAR_048736
    Natural varianti204 – 2041K → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036129

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS3608.1.
    RefSeqiNP_001254.2. NM_001263.3.
    UniGeneiHs.654899.
    Hs.708641.

    Genome annotation databases

    EnsembliENST00000295887; ENSP00000295887; ENSG00000163624.
    GeneIDi1040.
    KEGGihsa:1040.
    UCSCiuc011ccv.2. human.

    Polymorphism databases

    DMDMi3123204.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS3608.1.
    RefSeqi NP_001254.2. NM_001263.3.
    UniGenei Hs.654899.
    Hs.708641.

    3D structure databases

    ProteinModelPortali Q92903.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107471. 2 interactions.
    STRINGi 9606.ENSP00000295887.

    PTM databases

    PhosphoSitei Q92903.

    Polymorphism databases

    DMDMi 3123204.

    Proteomic databases

    MaxQBi Q92903.
    PaxDbi Q92903.
    PRIDEi Q92903.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295887 ; ENSP00000295887 ; ENSG00000163624 .
    GeneIDi 1040.
    KEGGi hsa:1040.
    UCSCi uc011ccv.2. human.

    Organism-specific databases

    CTDi 1040.
    GeneCardsi GC04P085428.
    HGNCi HGNC:1800. CDS1.
    HPAi HPA036187.
    MIMi 603548. gene.
    neXtProti NX_Q92903.
    PharmGKBi PA26346.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0575.
    HOGENOMi HOG000209582.
    HOVERGENi HBG002485.
    InParanoidi Q92903.
    KOi K00981.
    OMAi NFAWTHM.
    OrthoDBi EOG7M98G5.
    PhylomeDBi Q92903.
    TreeFami TF313464.

    Enzyme and pathway databases

    UniPathwayi UPA00557 ; UER00614 .
    Reactomei REACT_121000. Synthesis of PI.

    Miscellaneous databases

    GeneWikii CDS1_(gene).
    GenomeRNAii 1040.
    NextBioi 4365.
    PROi Q92903.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92903.
    Bgeei Q92903.
    CleanExi HS_CDS1.
    Genevestigatori Q92903.

    Family and domain databases

    InterProi IPR000374. PC_trans.
    IPR016720. PC_Trfase_euk.
    [Graphical view ]
    Pfami PF01148. CTP_transf_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018269. PC_trans_euk. 1 hit.
    PROSITEi PS01315. CDS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-204.

    Entry informationi

    Entry nameiCDS1_HUMAN
    AccessioniPrimary (citable) accession number: Q92903
    Secondary accession number(s): B2RAL5, O00163
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3