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Q9VFI9

- PDE6_DROME

UniProt

Q9VFI9 - PDE6_DROME

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
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 4 (19 Oct 2011)
      Previous versions | rss
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    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

    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.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
    3. protein binding Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cGMP, Metal-binding

    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

    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.
    GeneTreeiENSGT00750000117253.
    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

    MTDVSSPAGG AASPVEMSTT SSSSAATTSA SSSKPLTNGA NKTAISTAAG     50
    GVTPGAVPGP GSGAIPASSS SGNQVKLEHH HRQSNNNRPA VTNRSSETKL 100
    MTPTGSSSSP SQSPSQTQAS IQTQTSQQDR LAKASTTASQ QDVDEVARLF 150
    EEKPEAFEKW LTERAPPEAL SRLQEFIENR KPHKRPSVTS DLFQQWMAAS 200
    PTVQQKSPRS LSNSSASSLP ECRRHLMDLD EGELFMELIR DVANELDIDV 250
    LCHKILVNVG LLTHADRGSL FLAKGTPTNK YLVAKLFDVT QKTALKDAVT 300
    RASAEEIIIP FGIGIAGMVA QTKQMINIKE AYKDARFNCE IDLKTGYKTN 350
    AILCMPICNY EGDIIGVAQI INKTNGCMEF DEHDVEIFRR YLTFCGIGIQ 400
    NAQLFEMSVQ EYRRNQILLN LARSIFEEQN NLECLVTKIM TEARELLKCE 450
    RCSVFLVDLD CCEASHLEKI IEKPNQPATR AIKSADSFEE KKMRNRFTVL 500
    FELGGEYQAA NVSRPSVSEL SSSTLAQIAQ FVATTGQTVN ICDVIEWVRD 550
    HNQIRAEDEI DSTQAILCMP IMNAQKKVIG VAQLINKANG VPFTDSDASI 600
    FEAFAIFCGL GIHNTQMYEN ACKLMAKQKV ALECLSYHAT ASQDQTEKLT 650
    QDVIAEAESY NLYSFTFTDF ELVDDDTCRA VLRMFMQCNL VSQFQIPYDV 700
    LCRWVLSVRK NYRPVKYHNW RHALNVAQTM FAMLKTGKME RFMTDLEILG 750
    LLVACLCHDL DHRGTNNAFQ TKTESPLAIL YTTSTMEHHH FDQCVMILNS 800
    EGNNIFQALS PEDYRSVMKT VESAILSTDL AMYFKKRNAF LELVENGEFD 850
    WQGEEKKDLL CGMMMTACDV SAIAKPWEVQ HKVAKLVADE FFDQGDLEKL 900
    QLNTQPVAMM DRERKDELPK MQVGFIDVIC LPLYRVLCDT FPWITPLYEG 950
    TLENRRNWQD LAEKVEMGLT WIDHDTIDKP VEEFAACADE EIKDIEFTVT 1000
    TLNCNQQSQH GSEDSHTPEH QRSGSRLSMK KTGALGKAVR SKLSKTLYNS 1050
    MDGSKPKTSL KLLESHVSED MDDKSPTSPS QPQASGSMGR MSASSSTSSA 1100
    GGQMVDKSKK RSKLCALL 1118
    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF55066.4.
    AY058470 mRNA. Translation: AAL13699.1. Different initiation.
    RefSeqiNP_650369.3. NM_142112.4.
    UniGeneiDm.4259.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF55066.4 .
    AY058470 mRNA. Translation: AAL13699.1 . Different initiation.
    RefSeqi NP_650369.3. NM_142112.4.
    UniGenei Dm.4259.

    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 ENSGT00750000117253.
    InParanoidi Q9VFI9.
    KOi K13763.
    OrthoDBi EOG7RRF69.

    Miscellaneous databases

    ChiTaRSi Pde6. drosophila.
    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

    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: October 1, 2014
    This is version 98 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