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P0C1Q2

- PDE11_MOUSE

UniProt

P0C1Q2 - PDE11_MOUSE

Protein

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

Gene

Pde11a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (25 Jul 2006)
      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 By similarity.By similarity

    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

    Enzyme regulationi

    Inhibited by 3-isobutyl-1-methylxanthine (IBMX), zaprinast and dipyridamole. cGMP acts as an allosteric activator By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei664 – 6641Proton donorBy similarity
    Metal bindingi668 – 6681Divalent metal cation 1By similarity
    Metal bindingi704 – 7041Divalent metal cation 1By similarity
    Metal bindingi705 – 7051Divalent metal cation 1By similarity
    Metal bindingi705 – 7051Divalent metal cation 2By similarity
    Metal bindingi708 – 7081Divalent metal cation 2By similarity
    Metal bindingi734 – 7341Divalent metal cation 2By similarity
    Metal bindingi816 – 8161Divalent metal cation 1By similarity
    Binding sitei869 – 8691cAMP or cGMPBy similarity

    GO - Molecular functioni

    1. 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB-EC
    2. cAMP binding Source: Ensembl
    3. cGMP binding Source: UniProtKB
    4. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    5. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cAMP catabolic process Source: Ensembl
    2. cGMP catabolic process Source: Ensembl
    3. 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 11A (EC:3.1.4.17, EC:3.1.4.35)
    Alternative name(s):
    cAMP and cGMP phosphodiesterase 11A
    Gene namesi
    Name:Pde11a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:3036251. Pde11a.

    Subcellular locationi

    Cytoplasmcytosol By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. perikaryon Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mice live well and have no impaired fertility. They do however display reduced sperm concentration, rate of forward progression and percentage of live spermatozoa. Pre-ejaculated sperm display increased premature/spontaneous capacitance.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 933933Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11APRO_0000247041Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei239 – 2391PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP0C1Q2.

    PTM databases

    PhosphoSiteiP0C1Q2.

    Expressioni

    Tissue specificityi

    Expressed in testis and developing spermatoza.1 Publication

    Gene expression databases

    BgeeiP0C1Q2.
    CleanExiMM_PDE11A.
    GenevestigatoriP0C1Q2.

    Structurei

    3D structure databases

    ProteinModelPortaliP0C1Q2.
    SMRiP0C1Q2. Positions 205-911.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini217 – 370154GAF 1Add
    BLAST
    Domaini402 – 558157GAF 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni640 – 905266CatalyticBy similarityAdd
    BLAST

    Domaini

    The tandem GAF domains bind cGMP, and regulate enzyme activity. The binding of cGMP stimulates enzyme activity By similarity.By similarity

    Sequence similaritiesi

    Contains 2 GAF domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG270709.
    GeneTreeiENSGT00750000117253.
    HOGENOMiHOG000007068.
    HOVERGENiHBG101207.
    InParanoidiP0C1Q2.
    KOiK13298.
    OMAiDYSDLMQ.
    OrthoDBiEOG7RRF69.
    PhylomeDBiP0C1Q2.
    TreeFamiTF316499.

    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]

    Sequencei

    Sequence statusi: Complete.

    P0C1Q2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASRLDFGE VETFLDRHPE LFEDYLMRKG KQELVDKWLQ RHTSGQGASS    50
    LRPALAGASS LAQSNAKGSP GIGGGAGPQG SAHSHPTPGG GESAGVPLSP 100
    SWASGSRGDG SLQRRASQKE LRKSFARSKA IHVNRTYDEQ VTSRAQEPLS 150
    SVRRRALLRK ASSLPPTTAH ILSALLESRV NLPQYPPTAI DYKCHLKKHN 200
    ERQFFLELVK DISNDLDLTS LSYKILIFVC LMVDADRCSL FLVEGAAAGK 250
    KTLVSKFFDV HAGTPLLPCS STENSNEVQV PWGKGIIGYV GEHGETVNIP 300
    DAYQDRRFND EIDKLTGYKT KSLLCMPIRN SDGEIIGVAQ AINKVPEGAP 350
    FTEDDEKVMQ MYLPFCGIAI SNAQLFAASR KEYERSRALL EVVNDLFEEQ 400
    TDLEKIVKKI MHRAQTLLKC ERCSVLLLED IESPVVKFTK SFELMSPKCS 450
    ADAENSFKES VEKSSYSDWL INNSIAELVA STGLPVNVSD AYQDPRFDAE 500
    ADQISGFHIR SVLCVPIWNS NHQIIGVAQV LNRLDGKPFD DADQRLFEAF 550
    VIFCGLGINN TIMYDQVKKS WAKQSVALDV LSYHATCSKA EVDKFKAANI 600
    PLVSELAIDD IHFDDFSLDV DAMITAALRM FMELGMVQKF KIDYETLCRW 650
    LLTVRKNYRM VLYHNWRHAF NVCQLMFAML TTAGFQEILT EVEILAVIVG 700
    CLCHDLDHRG TNNAFQAKSD SALAQLYGTS ATLEHHHFNH AVMILQSEGH 750
    NIFANLSSKE YSDLMQLLKQ SILATDLTLY FERRTEFFEL VRKGDYDWSI 800
    TSHRDVFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE QGDRERSELK 850
    LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNAK LKPMLDSVAA 900
    NRRKWEELHQ KRLQVSAASP DPASPMVAGE DRL 933
    Length:933
    Mass (Da):104,563
    Last modified:July 25, 2006 - v1
    Checksum:i07B7CA1E4F905755
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL772341, AL845373, AL929133 Genomic DNA. Translation: CAM16587.1.
    AL845373, AL772341, AL929133 Genomic DNA. Translation: CAM17618.1.
    AL929133, AL772341, AL845373 Genomic DNA. Translation: CAM23980.1.
    AL929589 Genomic DNA. No translation available.
    CCDSiCCDS38152.1.
    RefSeqiNP_001074502.1. NM_001081033.1.
    UniGeneiMm.246613.

    Genome annotation databases

    EnsembliENSMUST00000099992; ENSMUSP00000097572; ENSMUSG00000075270.
    GeneIDi241489.
    KEGGimmu:241489.
    UCSCiuc008kex.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL772341 , AL845373 , AL929133 Genomic DNA. Translation: CAM16587.1 .
    AL845373 , AL772341 , AL929133 Genomic DNA. Translation: CAM17618.1 .
    AL929133 , AL772341 , AL845373 Genomic DNA. Translation: CAM23980.1 .
    AL929589 Genomic DNA. No translation available.
    CCDSi CCDS38152.1.
    RefSeqi NP_001074502.1. NM_001081033.1.
    UniGenei Mm.246613.

    3D structure databases

    ProteinModelPortali P0C1Q2.
    SMRi P0C1Q2. Positions 205-911.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P0C1Q2.

    Proteomic databases

    PRIDEi P0C1Q2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000099992 ; ENSMUSP00000097572 ; ENSMUSG00000075270 .
    GeneIDi 241489.
    KEGGi mmu:241489.
    UCSCi uc008kex.1. mouse.

    Organism-specific databases

    CTDi 50940.
    MGIi MGI:3036251. Pde11a.

    Phylogenomic databases

    eggNOGi NOG270709.
    GeneTreei ENSGT00750000117253.
    HOGENOMi HOG000007068.
    HOVERGENi HBG101207.
    InParanoidi P0C1Q2.
    KOi K13298.
    OMAi DYSDLMQ.
    OrthoDBi EOG7RRF69.
    PhylomeDBi P0C1Q2.
    TreeFami TF316499.

    Miscellaneous databases

    NextBioi 385015.
    PROi P0C1Q2.
    SOURCEi Search...

    Gene expression databases

    Bgeei P0C1Q2.
    CleanExi MM_PDE11A.
    Genevestigatori P0C1Q2.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "Phosphodiesterase 11 (PDE11) regulation of spermatozoa physiology."
      Wayman C., Phillips S., Lunny C., Webb T., Fawcett L., Baxendale R., Burgess G.
      Int. J. Impot. Res. 17:216-223(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiPDE11_MOUSE
    AccessioniPrimary (citable) accession number: P0C1Q2
    Secondary accession number(s): A2AKR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: July 25, 2006
    Last modified: October 1, 2014
    This is version 67 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3