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Protein

Phosphatidate cytidylyltransferase, photoreceptor-specific

Gene

CdsA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for the regeneration of the signaling molecule phosphatidylinositol 4,5-bisphosphate (PtdInsP2) from phosphatidic acid and maintenance of its steady supply during signaling thus plays an essential role during phospholipase C-mediated transduction.

Catalytic activityi

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Pathwayi

GO - Molecular functioni

  1. phosphatidate cytidylyltransferase activity Source: FlyBase

GO - Biological processi

  1. CDP-diacylglycerol biosynthetic process Source: FlyBase
  2. phototransduction Source: FlyBase
  3. regulation of lipid storage Source: FlyBase
  4. rhodopsin mediated signaling pathway Source: FlyBase
  5. terminal branching, open tracheal system Source: FlyBase
  6. thermotaxis Source: FlyBase
  7. trachea morphogenesis Source: FlyBase
  8. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism, Sensory transduction, Vision

Enzyme and pathway databases

ReactomeiREACT_180830. Synthesis of PI.
REACT_180833. Synthesis of PG.
UniPathwayiUPA00557; UER00614.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidate cytidylyltransferase, photoreceptor-specific (EC:2.7.7.41)
Alternative name(s):
CDP-DAG synthase
CDP-DG synthase
CDP-diacylglycerol synthase
Short name:
CDS
CDP-diglyceride pyrophosphorylase
CDP-diglyceride synthase
CTP:phosphatidate cytidylyltransferase
Gene namesi
Name:CdsA
ORF Names:CG7962
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0010350. CdsA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei88 – 10821HelicalSequence AnalysisAdd
BLAST
Transmembranei147 – 16721HelicalSequence AnalysisAdd
BLAST
Transmembranei180 – 20021HelicalSequence AnalysisAdd
BLAST
Transmembranei203 – 22321HelicalSequence AnalysisAdd
BLAST
Transmembranei227 – 24721HelicalSequence AnalysisAdd
BLAST
Transmembranei276 – 29621HelicalSequence AnalysisAdd
BLAST
Transmembranei350 – 37021HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Phosphatidate cytidylyltransferase, photoreceptor-specificPRO_0000090720Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301Phosphoserine1 Publication
Modified residuei34 – 341Phosphoserine1 Publication
Modified residuei35 – 351Phosphoserine1 Publication
Modified residuei40 – 401Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP56079.

Expressioni

Tissue specificityi

Retina. Localized to the photoreceptor neurons, both in the compound eyes and ocelli.

Gene expression databases

BgeeiP56079.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
beQ9VXZ31EBI-86600,EBI-143313
ScampQ9VXV61EBI-86600,EBI-188862

Protein-protein interaction databases

BioGridi68739. 10 interactions.
DIPiDIP-23447N.
IntActiP56079. 3 interactions.
MINTiMINT-801533.
STRINGi7227.FBpp0076411.

Structurei

3D structure databases

ProteinModelPortaliP56079.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CDS family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0575.
GeneTreeiENSGT00390000016175.
InParanoidiP56079.
KOiK00981.
OMAiNDIMAYF.
OrthoDBiEOG7M98G5.
PhylomeDBiP56079.

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.

P56079-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEVRRRKGE DEPLEDTAIS GSDAANKRNS AADSSDHVDS EEEKIPEEKF
60 70 80 90 100
VDELAKNLPQ GTDKTPEILD SALKDLPDRW KNWVIRGIFT WIMICGFALI
110 120 130 140 150
IYGGPLALMI TTLLVQVKCF QEIISIGYQV YRIHGLPWFR SLSWYFLLTS
160 170 180 190 200
NYFFYGENLV DYFGVVINRV EYLKFLVTYH RFLSFALYII GFVWFVLSLV
210 220 230 240 250
KKYYIKQFSL FAWTHVSLLI VVTQSYLIIQ NIFEGLIWFI VPVSMIVCND
260 270 280 290 300
VMAYVFGFFF GRTPLIKLSP KKTWEGFIGG GFATVLFGIL FSYVLCNYQY
310 320 330 340 350
FICPIQYSEE QGRMTMSCVP SYLFTPQEYS LKLFGIGKTL NLYPFIWHSI
360 370 380 390 400
SLSLFSSIIG PFGGFFASGF KRAFKIKDFG DMIPGHGGIM DRFDCQFLMA
410 420 430 440
TFVNVYISSF IRTPSPAKLL TQIYNLKPDQ QYQIYQSLKD NLGDMLT
Length:447
Mass (Da):51,511
Last modified:December 1, 2000 - v2
Checksum:i2E690CD02D3F4187
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti444 – 4441D → H no nucleotide entry (PubMed:7816135)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF50483.1.
RefSeqiNP_001286976.1. NM_001300047.1.
NP_524661.1. NM_079922.4.
UniGeneiDm.6770.

Genome annotation databases

EnsemblMetazoaiFBtr0076688; FBpp0076411; FBgn0010350.
GeneIDi43950.
KEGGidme:Dmel_CG7962.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF50483.1.
RefSeqiNP_001286976.1. NM_001300047.1.
NP_524661.1. NM_079922.4.
UniGeneiDm.6770.

3D structure databases

ProteinModelPortaliP56079.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68739. 10 interactions.
DIPiDIP-23447N.
IntActiP56079. 3 interactions.
MINTiMINT-801533.
STRINGi7227.FBpp0076411.

Proteomic databases

PaxDbiP56079.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076688; FBpp0076411; FBgn0010350.
GeneIDi43950.
KEGGidme:Dmel_CG7962.

Organism-specific databases

CTDi43950.
FlyBaseiFBgn0010350. CdsA.

Phylogenomic databases

eggNOGiCOG0575.
GeneTreeiENSGT00390000016175.
InParanoidiP56079.
KOiK00981.
OMAiNDIMAYF.
OrthoDBiEOG7M98G5.
PhylomeDBiP56079.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00614.
ReactomeiREACT_180830. Synthesis of PI.
REACT_180833. Synthesis of PG.

Miscellaneous databases

ChiTaRSiCdsA. fly.
GenomeRNAii43950.
NextBioi836438.

Gene expression databases

BgeeiP56079.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation of PLC-mediated signalling in vivo by CDP-diacylglycerol synthase."
    Wu L., Niemeyer B., Colley N., Socolich M., Zuker C.S.
    Nature 373:216-222(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Retina.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-34; SER-35 AND SER-40, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiCDSA_DROME
AccessioniPrimary (citable) accession number: P56079
Secondary accession number(s): Q9VSE0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: January 7, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.