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Reviewed, UniProtKB/Swiss-Prot P56079 (CDSA_DROME)

Last modified November 3, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Phosphatidate cytidylyltransferase, photoreceptor-specific
    EC=2.7.7.41
Alternative name(s):
    CDP-diglyceride pyrophosphorylase
    CDP-diglyceride synthetase
    CDP-diacylglycerol synthase
      Short name=CDS
    CTP:phosphatidate cytidylyltransferase
    CDP-DG synthetase
    CDP-DAG synthase
Gene names
Name: CdsA
ORF Names: CG7962
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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 activity

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

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

Sequence similarities

Belongs to the CDS family.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG32594-RCQ9VXZ31EBI-86600,EBI-143313
ScampQ9VXV61EBI-86600,EBI-188862

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Phosphatidate cytidylyltransferase, photoreceptor-specific
PRO_0000090720

Regions

Transmembrane88 – 10821 Potential
Transmembrane147 – 16721 Potential
Transmembrane180 – 20021 Potential
Transmembrane203 – 22321 Potential
Transmembrane227 – 24721 Potential
Transmembrane276 – 29621 Potential
Transmembrane350 – 37021 Potential

Amino acid modifications

Modified residue301Phosphoserine Ref.4
Modified residue341Phosphoserine Ref.4
Modified residue351Phosphoserine Ref.4
Modified residue401Phosphoserine Ref.4

Experimental info

Sequence conflict4441D → H Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P56079-1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 2E690CD02D3F4187

FASTA44751,511
        10         20         30         40         50         60 
MAEVRRRKGE DEPLEDTAIS GSDAANKRNS AADSSDHVDS EEEKIPEEKF VDELAKNLPQ 

        70         80         90        100        110        120 
GTDKTPEILD SALKDLPDRW KNWVIRGIFT WIMICGFALI IYGGPLALMI TTLLVQVKCF 

       130        140        150        160        170        180 
QEIISIGYQV YRIHGLPWFR SLSWYFLLTS NYFFYGENLV DYFGVVINRV EYLKFLVTYH 

       190        200        210        220        230        240 
RFLSFALYII GFVWFVLSLV KKYYIKQFSL FAWTHVSLLI VVTQSYLIIQ NIFEGLIWFI 

       250        260        270        280        290        300 
VPVSMIVCND VMAYVFGFFF GRTPLIKLSP KKTWEGFIGG GFATVLFGIL FSYVLCNYQY 

       310        320        330        340        350        360 
FICPIQYSEE QGRMTMSCVP SYLFTPQEYS LKLFGIGKTL NLYPFIWHSI SLSLFSSIIG 

       370        380        390        400        410        420 
PFGGFFASGF KRAFKIKDFG DMIPGHGGIM DRFDCQFLMA TFVNVYISSF IRTPSPAKLL 

       430        440 
TQIYNLKPDQ QYQIYQSLKD NLGDMLT

« Hide

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References

« Hide 'large scale' references
[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: 7816135] [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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[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: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-34; SER-35 AND SER-40, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AE014296 Genomic DNA. Translation: AAF50483.1.
RefSeqNP_524661.1.
UniGeneDm.6770

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:23447N.
IntActP56079. 3 interactions.
STRINGP56079.

Genome annotation databases

EnsemblFBtr0076688; FBpp0076411; FBgn0010350; Drosophila melanogaster. [Genome view]
GeneID43950.
KEGGdme:Dmel_CG7962.
NMPDRfig|7227.3.peg.8793.

Organism-specific databases

CTD43950.
FlyBaseFBgn0010350. CdsA.

Phylogenomic databases

HOGENOMP56079.
OMAIEISPKK.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-015693-MON.
BRENDA2.7.7.41. 48.

Gene expression databases

ArrayExpressP56079.
BgeeP56079.
GermOnlineCG7962. Drosophila melanogaster.

Family and domain databases

InterProIPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view]
PfamPF01148. CTP_transf_1. 1 hit.
[Graphical view]
PIRSFPIRSF018269. PC_trans_euk. 1 hit.
PROSITEPS01315. CDS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio836438.

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Entry information

Entry nameCDSA_DROME
AccessionPrimary (citable) accession number: P56079
Secondary accession number(s): Q9VSE0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 1, 2000
Last modified: November 3, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents