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Q9VFI9 (PDE6_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cGMP-specific 3',5'-cyclic phosphodiesterase

EC=3.1.4.35
Alternative name(s):
DmPDE5/6
Short name=DmPDE6
Gene names
Name:Pde6
ORF Names:CG8279
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a role regulating cGMP transport in Malpighian tubule principal cells. Ref.4

Catalytic activity

Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate. Ref.4 Ref.5

Cofactor

Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions By similarity.

Subunit structure

Interacts with PrBP. Ref.5

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side. Note: Expressed on the apical side of the Malpighian tubule principal cell polarized membrane. Loss of prenylation causes protein location to the cytoplasm. Ref.4 Ref.5

Tissue specificity

Expressed in Malpighian tubule principal cells. Ref.4

Disruption phenotype

Flies display increased active transport of cGMP. Overexpression of Pde6 confers inhibition of the active transport and efflux of cGMP by tubules. Ref.4

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Contains 2 GAF domains.

Sequence caution

The sequence AAL13699.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11151115cGMP-specific 3',5'-cyclic phosphodiesterase
PRO_0000356892
Propeptide1116 – 11183Removed in mature form Probable
PRO_0000356893

Regions

Domain247 – 399153GAF 1
Domain431 – 612182GAF 2
Compositional bias5 – 3329Ser-rich

Sites

Active site7181Proton donor By similarity
Metal binding7221Divalent metal cation 1 By similarity
Metal binding7581Divalent metal cation 1 By similarity
Metal binding7591Divalent metal cation 1 By similarity
Metal binding7591Divalent metal cation 2 By similarity
Metal binding8691Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue11151Cysteine methyl ester Probable
Lipidation11151S-farnesyl cysteine Probable

Experimental info

Mutagenesis11151C → S: Impairs prenylation and membrane. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9VFI9 [UniParc].

Last modified October 19, 2011. Version 4.
Checksum: 1CFB89721F84DC5A

FASTA1,118124,325
        10         20         30         40         50         60 
MTDVSSPAGG AASPVEMSTT SSSSAATTSA SSSKPLTNGA NKTAISTAAG GVTPGAVPGP 

        70         80         90        100        110        120 
GSGAIPASSS SGNQVKLEHH HRQSNNNRPA VTNRSSETKL MTPTGSSSSP SQSPSQTQAS 

       130        140        150        160        170        180 
IQTQTSQQDR LAKASTTASQ QDVDEVARLF EEKPEAFEKW LTERAPPEAL SRLQEFIENR 

       190        200        210        220        230        240 
KPHKRPSVTS DLFQQWMAAS PTVQQKSPRS LSNSSASSLP ECRRHLMDLD EGELFMELIR 

       250        260        270        280        290        300 
DVANELDIDV LCHKILVNVG LLTHADRGSL FLAKGTPTNK YLVAKLFDVT QKTALKDAVT 

       310        320        330        340        350        360 
RASAEEIIIP FGIGIAGMVA QTKQMINIKE AYKDARFNCE IDLKTGYKTN AILCMPICNY 

       370        380        390        400        410        420 
EGDIIGVAQI INKTNGCMEF DEHDVEIFRR YLTFCGIGIQ NAQLFEMSVQ EYRRNQILLN 

       430        440        450        460        470        480 
LARSIFEEQN NLECLVTKIM TEARELLKCE RCSVFLVDLD CCEASHLEKI IEKPNQPATR 

       490        500        510        520        530        540 
AIKSADSFEE KKMRNRFTVL FELGGEYQAA NVSRPSVSEL SSSTLAQIAQ FVATTGQTVN 

       550        560        570        580        590        600 
ICDVIEWVRD HNQIRAEDEI DSTQAILCMP IMNAQKKVIG VAQLINKANG VPFTDSDASI 

       610        620        630        640        650        660 
FEAFAIFCGL GIHNTQMYEN ACKLMAKQKV ALECLSYHAT ASQDQTEKLT QDVIAEAESY 

       670        680        690        700        710        720 
NLYSFTFTDF ELVDDDTCRA VLRMFMQCNL VSQFQIPYDV LCRWVLSVRK NYRPVKYHNW 

       730        740        750        760        770        780 
RHALNVAQTM FAMLKTGKME RFMTDLEILG LLVACLCHDL DHRGTNNAFQ TKTESPLAIL 

       790        800        810        820        830        840 
YTTSTMEHHH FDQCVMILNS EGNNIFQALS PEDYRSVMKT VESAILSTDL AMYFKKRNAF 

       850        860        870        880        890        900 
LELVENGEFD WQGEEKKDLL CGMMMTACDV SAIAKPWEVQ HKVAKLVADE FFDQGDLEKL 

       910        920        930        940        950        960 
QLNTQPVAMM DRERKDELPK MQVGFIDVIC LPLYRVLCDT FPWITPLYEG TLENRRNWQD 

       970        980        990       1000       1010       1020 
LAEKVEMGLT WIDHDTIDKP VEEFAACADE EIKDIEFTVT TLNCNQQSQH GSEDSHTPEH 

      1030       1040       1050       1060       1070       1080 
QRSGSRLSMK KTGALGKAVR SKLSKTLYNS MDGSKPKTSL KLLESHVSED MDDKSPTSPS 

      1090       1100       1110 
QPQASGSMGR MSASSSTSSA GGQMVDKSKK RSKLCALL 

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-1118.
Strain: Berkeley.
Tissue: Head.
[4]"A novel role for a Drosophila homologue of cGMP-specific phosphodiesterase in the active transport of cGMP."
Day J.P., Houslay M.D., Davies S.-A.
Biochem. J. 393:481-488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[5]"Regulation of a Drosophila melanogaster cGMP-specific phosphodiesterase by prenylation and interaction with a prenyl-binding protein."
Day J.P., Cleghon V., Houslay M.D., Davies S.-A.
Biochem. J. 414:363-374(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, INTERACTION WITH PRBP, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-1115.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014297 Genomic DNA. Translation: AAF55066.4.
AY058470 mRNA. Translation: AAL13699.1. Different initiation.
RefSeqNP_650369.3. NM_142112.4.
UniGeneDm.4259.

3D structure databases

ProteinModelPortalQ9VFI9.
SMRQ9VFI9. Positions 230-964.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9VFI9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0300330; FBpp0289559; FBgn0038237.
GeneID41760.
KEGGdme:Dmel_CG8279.

Organism-specific databases

CTD41760.
FlyBaseFBgn0038237. Pde6.

Phylogenomic databases

eggNOGNOG270709.
GeneTreeENSGT00750000117253.
InParanoidQ9VFI9.
KOK13763.
OrthoDBEOG7RRF69.

Gene expression databases

BgeeQ9VFI9.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
3.30.450.40. 3 hits.
InterProIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMSSF55781. SSF55781. 3 hits.
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPde6. drosophila.
GenomeRNAi41760.
NextBio825438.
PROQ9VFI9.

Entry information

Entry namePDE6_DROME
AccessionPrimary (citable) accession number: Q9VFI9
Secondary accession number(s): Q95TW8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: October 19, 2011
Last modified: July 9, 2014
This is version 97 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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