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Q8VID6

- PDE11_RAT

UniProt

Q8VID6 - PDE11_RAT

Protein

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

Gene

Pde11a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      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.1 Publication

    Kineticsi

    1. KM=3.9 µM for cAMP (isoform 1)1 Publication
    2. KM=1.6 µM for cGMP (isoform 1)1 Publication
    3. KM=4.0 µM for cAMP (isoform 2)1 Publication
    4. KM=1.6 µM for cGMP (isoform 2)1 Publication
    5. KM=2.2 µM for cAMP (isoform 3)1 Publication
    6. KM=1.3 µM for cGMP (isoform 3)1 Publication

    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: RGD
    3. cGMP binding Source: RGD
    4. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    5. cyclic-nucleotide phosphodiesterase activity Source: RGD
    6. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cAMP catabolic process Source: RGD
    2. cGMP catabolic process Source: RGD
    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi621793. Pde11a.

    Subcellular locationi

    Cytoplasmcytosol By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 935935Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11APRO_0000247042Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ8VID6.

    PTM databases

    PhosphoSiteiQ8VID6.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed in brain, heart, kidney and liver, but not in prostate. Isoform 2 is specifically expressed in testis. Isoform 3 is expressed in various tissues including brain, lung, skeletal muscle, spleen, testis and prostate.1 Publication

    Gene expression databases

    GenevestigatoriQ8VID6.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VID6.
    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

    GeneTreeiENSGT00750000117253.
    HOGENOMiHOG000007068.
    HOVERGENiHBG101207.
    InParanoidiQ8VID6.
    KOiK13298.
    OMAiDYSDLMQ.
    PhylomeDBiQ8VID6.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8VID6-1) [UniParc]FASTAAdd to Basket

    Also known as: PDE11A4

    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

    MAASRLDFGE VETFLDRHPE LFEDYLMRKG KQELVDKWLQ RHSSGQGASD    50
    LRPALAGASS LAQSSARGST GIGGGAGPQG SANSHPASGG GESAGVPLSP 100
    SWASGSRGDG NLQRRASQKE LRKSFARSKA IHVNRTYDEQ VTSRAQEPLS 150
    SVRRRALLRK ASSLPPTTAH ILSALLESRV NLPQYPPTAI DYKCHLKKHN 200
    ERQFFLELVK DISNDLDLTS LSYKILIFVC LMVDADRCSL FLVEGAAAGK 250
    KTLVSKFFDV HAGTPLLPCS TTENSNEVQV 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 VSKGAYDWSI 800
    TSHRDVFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE QGDRERSELK 850
    LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNAK LKPMLDSVAA 900
    NRRKWEELHQ KRLQVSAASP VPSSPSPAVA GEDRL 935
    Length:935
    Mass (Da):104,571
    Last modified:March 1, 2002 - v1
    Checksum:iE80F1039770F8276
    GO
    Isoform 2 (identifier: Q8VID6-2) [UniParc]FASTAAdd to Basket

    Also known as: PDE11A3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-250: Missing.
         251-304: KTLVSKFFDV...ETVNIPDAYQ → MLKQARRFSF...FLTRMQTRTK

    Show »
    Length:685
    Mass (Da):78,067
    Checksum:i505E8748E9A6C21F
    GO
    Isoform 3 (identifier: Q8VID6-3) [UniParc]FASTAAdd to Basket

    Also known as: PDE11A2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-354: Missing.
         355-357: DEK → MSW

    Show »
    Length:581
    Mass (Da):66,142
    Checksum:i2CA7C2F5DDB37D00
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 354354Missing in isoform 3. 1 PublicationVSP_019902Add
    BLAST
    Alternative sequencei1 – 250250Missing in isoform 2. 1 PublicationVSP_019903Add
    BLAST
    Alternative sequencei251 – 30454KTLVS…PDAYQ → MLKQARRFSFRNVRSATQWR KVGSTRQGQISGAFLAERLD KHQDFLTRMQTRTK in isoform 2. 1 PublicationVSP_019904Add
    BLAST
    Alternative sequencei355 – 3573DEK → MSW in isoform 3. 1 PublicationVSP_019905

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB059360 mRNA. Translation: BAB79627.1.
    AB059361 mRNA. Translation: BAB79628.1.
    AB059362 mRNA. Translation: BAB79629.1.
    RefSeqiNP_001120952.1. NM_001127480.1. [Q8VID6-2]
    NP_001120953.1. NM_001127481.2. [Q8VID6-3]
    NP_543169.1. NM_080893.1. [Q8VID6-1]
    UniGeneiRn.88630.

    Genome annotation databases

    EnsembliENSRNOT00000008301; ENSRNOP00000008300; ENSRNOG00000024457. [Q8VID6-1]
    ENSRNOT00000050355; ENSRNOP00000051289; ENSRNOG00000024457. [Q8VID6-2]
    GeneIDi140928.
    KEGGirno:140928.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB059360 mRNA. Translation: BAB79627.1 .
    AB059361 mRNA. Translation: BAB79628.1 .
    AB059362 mRNA. Translation: BAB79629.1 .
    RefSeqi NP_001120952.1. NM_001127480.1. [Q8VID6-2 ]
    NP_001120953.1. NM_001127481.2. [Q8VID6-3 ]
    NP_543169.1. NM_080893.1. [Q8VID6-1 ]
    UniGenei Rn.88630.

    3D structure databases

    ProteinModelPortali Q8VID6.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q8VID6.

    Proteomic databases

    PRIDEi Q8VID6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000008301 ; ENSRNOP00000008300 ; ENSRNOG00000024457 . [Q8VID6-1 ]
    ENSRNOT00000050355 ; ENSRNOP00000051289 ; ENSRNOG00000024457 . [Q8VID6-2 ]
    GeneIDi 140928.
    KEGGi rno:140928.

    Organism-specific databases

    CTDi 50940.
    RGDi 621793. Pde11a.

    Phylogenomic databases

    GeneTreei ENSGT00750000117253.
    HOGENOMi HOG000007068.
    HOVERGENi HBG101207.
    InParanoidi Q8VID6.
    KOi K13298.
    OMAi DYSDLMQ.
    PhylomeDBi Q8VID6.
    TreeFami TF316499.

    Miscellaneous databases

    NextBioi 620787.
    PROi Q8VID6.

    Gene expression databases

    Genevestigatori Q8VID6.

    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. "Identification of rat cyclic nucleotide phosphodiesterase 11A (PDE11A): comparison of rat and human PDE11A splicing variants."
      Yuasa K., Ohgaru T., Asahina M., Omori K.
      Eur. J. Biochem. 268:4440-4448(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPDE11_RAT
    AccessioniPrimary (citable) accession number: Q8VID6
    Secondary accession number(s): Q8VID7, Q8VID8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 82 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3