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Q9VJ79

- PDE11_DROME

UniProt

Q9VJ79 - PDE11_DROME

Protein

Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11

Gene

Pde11

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 90 (01 Oct 2014)
      Sequence version 4 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively.1 Publication

    Catalytic activityi

    Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.
    Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.

    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

    Kineticsi

    1. KM=18.5 µM for cAMP KM=6 µM for cGMP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei860 – 8601Proton donorBy similarity
    Metal bindingi864 – 8641Divalent metal cation 1By similarity
    Metal bindingi900 – 9001Divalent metal cation 1By similarity
    Metal bindingi901 – 9011Divalent metal cation 1By similarity
    Metal bindingi901 – 9011Divalent metal cation 2By similarity
    Metal bindingi904 – 9041Divalent metal cation 2By similarity
    Metal bindingi929 – 9291Divalent metal cation 2By similarity
    Metal bindingi1011 – 10111Divalent metal cation 1By similarity
    Binding sitei1064 – 10641cAMP or cGMPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cAMP metabolic process Source: UniProtKB
    2. cGMP metabolic process Source: UniProtKB
    3. lateral inhibition Source: FlyBase
    4. signal transduction Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, cGMP, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11 (EC:3.1.4.17, EC:3.1.4.35)
    Alternative name(s):
    cAMP and cGMP phosphodiesterase 11
    Gene namesi
    Name:Pde11
    ORF Names:CG34341
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0085370. Pde11.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14511451Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11PRO_0000247044Add
    BLAST

    Proteomic databases

    PaxDbiQ9VJ79.

    Expressioni

    Tissue specificityi

    In adults, it is enriched in Malpighian tubules.1 Publication

    Gene expression databases

    BgeeiQ9VJ79.

    Interactioni

    Protein-protein interaction databases

    BioGridi61102. 6 interactions.
    MINTiMINT-1027877.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VJ79.
    SMRiQ9VJ79. Positions 402-1137.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini419 – 572154GAF 1Add
    BLAST
    Domaini604 – 754151GAF 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni836 – 1100265CatalyticBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1121 – 11244Poly-Gln
    Compositional biasi1328 – 1436109His-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 GAF domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG270709.
    GeneTreeiENSGT00750000117253.
    InParanoidiQ9VJ79.
    KOiK13298.
    OMAiCEIDSLT.
    OrthoDBiEOG7RRF69.
    PhylomeDBiQ9VJ79.

    Family and domain databases

    Gene3Di1.10.1300.10. 1 hit.
    3.30.450.40. 2 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. 2 hits.
    PROSITEiPS00126. PDEASE_I. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: Q9VJ79-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGQAASMCRF RGCRYKNKNK SSKQQQQQQQ QQQQQQQQHQ QQQQQTPSHS     50
    PQIQHHSEII PATTGLHLRS IEEPATTPLQ FQPTGRMNTE QGGTGYGGYG 100
    SSEHSLLIAT RHAGVPLPLA QHQPLPAHYQ PLNHSGAAPP SSSNGSSSSG 150
    GGVQTSATPQ QQQQYQVQQP YQYQYQHHYH HQANSPQHHR PYDPEHARME 200
    AWLDENQEFV QDYFIRKATR QTVDAWLVSH ATSAGNDVVS STSPTHANGQ 250
    TSSSRGGSGA TTPVRKISAH EFERGGLLKP IVNTIDGTPT FLSIGPPMDN 300
    GSVGGSCSNL QNVGGVVAGQ YQYNHQQHHH NHAHLHHSQH SHYQAGGAVG 350
    SSSLGSTGGA SGAGGAPSLG GSGGAGNGHQ YPYYHCHQRP QRLSRNELKQ 400
    LDEKELIFEL VKDICNELEV RTLCHKILQN VSILLNADRG SLFLVQGRCN 450
    GPDGLKKCLV SKLFDVCPRS TVEEMEQQDE VRVAWGTGIA GHVAESGEPV 500
    NIPDAYQDER FNCEIDSLTG YRTKALLCMP IKDSSGDVIG VAQVINKMNG 550
    ECFSEIDEKV FSSYLQFCGI GLRNAQLYEK SQLEIKRNQV LLDLARMIFE 600
    EQSTIEHMVF RILTHMQSLI QCQRVQILLV HEADKGSFSR VFDFEANDLS 650
    EEEATSRTSP YESRFPINIG ITGHVATTGE TVNVPNAYED DRFDASVDEN 700
    SCFKHRSILC MAIKNSLGQI IGVIQLINKF NELDFTKNDE NFVEAFAIFC 750
    GMGIHNTHMY EKAIVAMAKQ SVTLEVLSYH ASATMDEAHR LRRLRVPSAV 800
    HFRLHDFKFD DIHFEDDDTL KACLRMFLDL DFVERFHIDY EVLCRWLLSV 850
    KKNYRNVTYH NWRHAFNVAQ MMFAILTTTQ WWKIFGEIEC LALIIGCLCH 900
    DLDHRGTNNS FQIKASSPLA QLYSTSTMEH HHFDQCLMIL NSPGNQILAN 950
    LSSDDYCRVI RVLEDAILST DLAVYFKKRG PFLESVSQPT SYWVAEEPRA 1000
    LLRAMSMTVC DLSAITKPWE IEKRVADLVS SEFFEQGDME KQELNITPID 1050
    IMNREKEDEL PMMQVNFIDS ICLPIYEAFA TLSDKLEPLV EGVRDNRGHW 1100
    IDLADVVKTK TSQDQEPEEE QQQQNVISNG DCKAMSDDDV AASEAEVAVD 1150
    SPSEKASVNG SNVANNSSNT NKKIAVASHP TSTQPSDDDN DVDADADDVD 1200
    EQAAEENGHD AEVDEASCRS NSTCSSSTAS SCLSTPPPTG EDDSTPVSPL 1250
    KTLQAKLVAA NLNALQRQTS NQAQTQKQRC KSCDHSRSGL QVRKTSSLRG 1300
    AQELDLDSKT RNGTHAALCK STPVINNHSH HHNHSHSHNH NHHHHHHHHS 1350
    HHNHSQHGIG IGSASIGGSG LISLTTPLLA MDSDRIPKIV GKIGNLDGLP 1400
    FANGIGGPQN GHGLPFGSYQ HHHHHQHHHH LLARRHSETN SNGATAMAVE 1450
    K 1451

    Note: No experimental confirmation available.

    Length:1,451
    Mass (Da):160,930
    Last modified:January 15, 2008 - v4
    Checksum:iDFEC01058FB600A9
    GO
    Isoform C (identifier: Q9VJ79-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-44: Missing.
         45-64: QTPSHSPQIQHHSEIIPATT → MASSPNNAAPPVLWRARRKI

    Note: No experimental confirmation available.

    Show »
    Length:1,407
    Mass (Da):155,622
    Checksum:iDC01CA40E8325C1E
    GO
    Isoform D (identifier: Q9VJ79-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MKVTQSEENT...GLTFALLAGP

    Note: No experimental confirmation available.

    Show »
    Length:1,539
    Mass (Da):170,998
    Checksum:iE1EBAD64C5391214
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381Q → QQQ in AAM52774. (PubMed:12537569)Curated
    Sequence conflicti1192 – 11921V → A in AAM52774. (PubMed:12537569)Curated
    Sequence conflicti1196 – 11961A → V in AAM52774. (PubMed:12537569)Curated
    Sequence conflicti1232 – 12321C → R in AAM52774. (PubMed:12537569)Curated
    Sequence conflicti1342 – 13421H → HNH in AAM52774. (PubMed:12537569)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4444Missing in isoform C. CuratedVSP_030328Add
    BLAST
    Alternative sequencei1 – 11M → MKVTQSEENTRNTSDRSKSV QTNRKFDNFNWLLSCGLLAA VKSTKLIPQLPRQQQPKKYN LRYAAELLKFDKIQFIKTEG LTFALLAGP in isoform D. 1 PublicationVSP_019906
    Alternative sequencei45 – 6420QTPSH…IPATT → MASSPNNAAPPVLWRARRKI in isoform C. CuratedVSP_030329Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF53675.3.
    AE014134 Genomic DNA. Translation: AAF53676.2.
    AY122262 mRNA. Translation: AAM52774.1.
    RefSeqiNP_001097177.1. NM_001103707.1. [Q9VJ79-3]
    NP_609885.2. NM_136041.2. [Q9VJ79-1]
    UniGeneiDm.13948.

    Genome annotation databases

    EnsemblMetazoaiFBtr0112544; FBpp0111456; FBgn0085370. [Q9VJ79-1]
    GeneIDi35107.
    KEGGidme:Dmel_CG34341.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF53675.3 .
    AE014134 Genomic DNA. Translation: AAF53676.2 .
    AY122262 mRNA. Translation: AAM52774.1 .
    RefSeqi NP_001097177.1. NM_001103707.1. [Q9VJ79-3 ]
    NP_609885.2. NM_136041.2. [Q9VJ79-1 ]
    UniGenei Dm.13948.

    3D structure databases

    ProteinModelPortali Q9VJ79.
    SMRi Q9VJ79. Positions 402-1137.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 61102. 6 interactions.
    MINTi MINT-1027877.

    Proteomic databases

    PaxDbi Q9VJ79.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0112544 ; FBpp0111456 ; FBgn0085370 . [Q9VJ79-1 ]
    GeneIDi 35107.
    KEGGi dme:Dmel_CG34341.

    Organism-specific databases

    CTDi 35107.
    FlyBasei FBgn0085370. Pde11.

    Phylogenomic databases

    eggNOGi NOG270709.
    GeneTreei ENSGT00750000117253.
    InParanoidi Q9VJ79.
    KOi K13298.
    OMAi CEIDSLT.
    OrthoDBi EOG7RRF69.
    PhylomeDBi Q9VJ79.

    Miscellaneous databases

    GenomeRNAii 35107.
    NextBioi 791899.

    Gene expression databases

    Bgeei Q9VJ79.

    Family and domain databases

    Gene3Di 1.10.1300.10. 1 hit.
    3.30.450.40. 2 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. 2 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, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
      Strain: Berkeley.
      Tissue: Embryo.
    4. "Cyclic nucleotide phosphodiesterases in Drosophila melanogaster."
      Day J.P., Dow J.A.T., Houslay M.D., Davies S.A.
      Biochem. J. 388:333-342(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPDE11_DROME
    AccessioniPrimary (citable) accession number: Q9VJ79
    Secondary accession number(s): Q8MQW0, Q9VJ78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 90 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