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Q9VFI9

- PDE6_DROME

UniProt

Q9VFI9 - PDE6_DROME

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Protein

cGMP-specific 3',5'-cyclic phosphodiesterase

Gene

Pde6

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

Functioni

Has a role regulating cGMP transport in Malpighian tubule principal cells.1 Publication

Catalytic activityi

Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.2 Publications

Cofactori

a divalent metal cationBy similarityNote: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei718 – 7181Proton donorBy similarity
Metal bindingi722 – 7221Divalent metal cation 1By similarity
Metal bindingi758 – 7581Divalent metal cation 1By similarity
Metal bindingi759 – 7591Divalent metal cation 1By similarity
Metal bindingi759 – 7591Divalent metal cation 2By similarity
Metal bindingi869 – 8691Divalent metal cation 1By similarity

GO - Molecular functioni

  1. 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cGMP metabolic process Source: UniProtKB
  2. negative regulation of nucleobase-containing compound transport Source: FlyBase
  3. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cGMP, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_209420. G alpha (s) signalling events.
REACT_244942. cGMP effects.

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-specific 3',5'-cyclic phosphodiesterase1 Publication (EC:3.1.4.35)
Alternative name(s):
DmPDE5/6
Short name:
DmPDE61 Publication
Gene namesi
Name:Pde6
ORF Names:CG8279
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0038237. Pde6.

Subcellular locationi

Cell membrane 2 Publications; Lipid-anchor 2 Publications; Cytoplasmic side 2 Publications
Note: Expressed on the apical side of the Malpighian tubule principal cell polarized membrane. Loss of prenylation causes protein location to the cytoplasm.

GO - Cellular componenti

  1. apical plasma membrane Source: FlyBase
  2. membrane Source: UniProtKB
  3. plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Flies display increased active transport of cGMP. Overexpression of Pde6 confers inhibition of the active transport and efflux of cGMP by tubules.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1115 – 11151C → S: Impairs prenylation and membrane. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11151115cGMP-specific 3',5'-cyclic phosphodiesterasePRO_0000356892Add
BLAST
Propeptidei1116 – 11183Removed in mature formCuratedPRO_0000356893

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1115 – 11151Cysteine methyl esterCurated
Lipidationi1115 – 11151S-farnesyl cysteineCurated

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiQ9VFI9.

Expressioni

Tissue specificityi

Expressed in Malpighian tubule principal cells.1 Publication

Gene expression databases

BgeeiQ9VFI9.

Interactioni

Subunit structurei

Interacts with PrBP.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9VFI9.
SMRiQ9VFI9. Positions 230-964.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini247 – 399153GAF 1Add
BLAST
Domaini431 – 612182GAF 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 3329Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the cyclic nucleotide phosphodiesterase family.Sequence Analysis
Contains 2 GAF domains.Sequence Analysis

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270709.
GeneTreeiENSGT00760000119066.
InParanoidiQ9VFI9.
KOiK13763.
OrthoDBiEOG7RRF69.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 3 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 3 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9VFI9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTDVSSPAGG AASPVEMSTT SSSSAATTSA SSSKPLTNGA NKTAISTAAG
60 70 80 90 100
GVTPGAVPGP GSGAIPASSS SGNQVKLEHH HRQSNNNRPA VTNRSSETKL
110 120 130 140 150
MTPTGSSSSP SQSPSQTQAS IQTQTSQQDR LAKASTTASQ QDVDEVARLF
160 170 180 190 200
EEKPEAFEKW LTERAPPEAL SRLQEFIENR KPHKRPSVTS DLFQQWMAAS
210 220 230 240 250
PTVQQKSPRS LSNSSASSLP ECRRHLMDLD EGELFMELIR DVANELDIDV
260 270 280 290 300
LCHKILVNVG LLTHADRGSL FLAKGTPTNK YLVAKLFDVT QKTALKDAVT
310 320 330 340 350
RASAEEIIIP FGIGIAGMVA QTKQMINIKE AYKDARFNCE IDLKTGYKTN
360 370 380 390 400
AILCMPICNY EGDIIGVAQI INKTNGCMEF DEHDVEIFRR YLTFCGIGIQ
410 420 430 440 450
NAQLFEMSVQ EYRRNQILLN LARSIFEEQN NLECLVTKIM TEARELLKCE
460 470 480 490 500
RCSVFLVDLD CCEASHLEKI IEKPNQPATR AIKSADSFEE KKMRNRFTVL
510 520 530 540 550
FELGGEYQAA NVSRPSVSEL SSSTLAQIAQ FVATTGQTVN ICDVIEWVRD
560 570 580 590 600
HNQIRAEDEI DSTQAILCMP IMNAQKKVIG VAQLINKANG VPFTDSDASI
610 620 630 640 650
FEAFAIFCGL GIHNTQMYEN ACKLMAKQKV ALECLSYHAT ASQDQTEKLT
660 670 680 690 700
QDVIAEAESY NLYSFTFTDF ELVDDDTCRA VLRMFMQCNL VSQFQIPYDV
710 720 730 740 750
LCRWVLSVRK NYRPVKYHNW RHALNVAQTM FAMLKTGKME RFMTDLEILG
760 770 780 790 800
LLVACLCHDL DHRGTNNAFQ TKTESPLAIL YTTSTMEHHH FDQCVMILNS
810 820 830 840 850
EGNNIFQALS PEDYRSVMKT VESAILSTDL AMYFKKRNAF LELVENGEFD
860 870 880 890 900
WQGEEKKDLL CGMMMTACDV SAIAKPWEVQ HKVAKLVADE FFDQGDLEKL
910 920 930 940 950
QLNTQPVAMM DRERKDELPK MQVGFIDVIC LPLYRVLCDT FPWITPLYEG
960 970 980 990 1000
TLENRRNWQD LAEKVEMGLT WIDHDTIDKP VEEFAACADE EIKDIEFTVT
1010 1020 1030 1040 1050
TLNCNQQSQH GSEDSHTPEH QRSGSRLSMK KTGALGKAVR SKLSKTLYNS
1060 1070 1080 1090 1100
MDGSKPKTSL KLLESHVSED MDDKSPTSPS QPQASGSMGR MSASSSTSSA
1110
GGQMVDKSKK RSKLCALL
Length:1,118
Mass (Da):124,325
Last modified:October 19, 2011 - v4
Checksum:i1CFB89721F84DC5A
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF55066.4.
AY058470 mRNA. Translation: AAL13699.1. Different initiation.
RefSeqiNP_001287327.1. NM_001300398.1.
NP_650369.3. NM_142112.5.

Genome annotation databases

EnsemblMetazoaiFBtr0300330; FBpp0289559; FBgn0038237.
GeneIDi41760.
KEGGidme:Dmel_CG8279.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF55066.4 .
AY058470 mRNA. Translation: AAL13699.1 . Different initiation.
RefSeqi NP_001287327.1. NM_001300398.1.
NP_650369.3. NM_142112.5.

3D structure databases

ProteinModelPortali Q9VFI9.
SMRi Q9VFI9. Positions 230-964.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q9VFI9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0300330 ; FBpp0289559 ; FBgn0038237 .
GeneIDi 41760.
KEGGi dme:Dmel_CG8279.

Organism-specific databases

CTDi 41760.
FlyBasei FBgn0038237. Pde6.

Phylogenomic databases

eggNOGi NOG270709.
GeneTreei ENSGT00760000119066.
InParanoidi Q9VFI9.
KOi K13763.
OrthoDBi EOG7RRF69.

Enzyme and pathway databases

Reactomei REACT_209420. G alpha (s) signalling events.
REACT_244942. cGMP effects.

Miscellaneous databases

GenomeRNAii 41760.
NextBioi 825438.
PROi Q9VFI9.

Gene expression databases

Bgeei Q9VFI9.

Family and domain databases

Gene3Di 1.10.1300.10. 1 hit.
3.30.450.40. 3 hits.
InterProi IPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view ]
SUPFAMi SSF55781. SSF55781. 3 hits.
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-1118.
    Strain: BerkeleyImported.
    Tissue: Head1 Publication.
  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.

Entry informationi

Entry nameiPDE6_DROME
AccessioniPrimary (citable) accession number: Q9VFI9
Secondary accession number(s): Q95TW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: October 19, 2011
Last modified: November 26, 2014
This is version 100 of the entry and version 4 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3