Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q01065

- PDE1B_MOUSE

UniProt

Q01065 - PDE1B_MOUSE

Protein

Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B

Gene

Pde1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate By similarity.By similarity

    Catalytic activityi

    Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 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

    Type I PDE are activated by the binding of calmodulin in the presence of Ca2+.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei222 – 2221Proton donorBy similarity
    Metal bindingi226 – 2261Divalent metal cation 1By similarity
    Metal bindingi262 – 2621Divalent metal cation 1By similarity
    Metal bindingi263 – 2631Divalent metal cation 1By similarity
    Metal bindingi263 – 2631Divalent metal cation 2By similarity
    Metal bindingi369 – 3691Divalent metal cation 1By similarity

    GO - Molecular functioni

    1. 3',5'-cyclic-AMP phosphodiesterase activity Source: Ensembl
    2. calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity Source: MGI
    3. calmodulin-dependent cyclic-nucleotide phosphodiesterase activity Source: MGI
    4. cyclic-nucleotide phosphodiesterase activity Source: MGI
    5. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cAMP catabolic process Source: Ensembl
    2. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: Ensembl
    3. cellular response to macrophage colony-stimulating factor stimulus Source: Ensembl
    4. cGMP catabolic process Source: Ensembl
    5. locomotory behavior Source: MGI
    6. monocyte differentiation Source: Ensembl
    7. regulation of dopamine metabolic process Source: MGI
    8. regulation of neurotransmitter levels Source: MGI
    9. response to amphetamine Source: MGI
    10. serotonin metabolic process Source: MGI
    11. signal transduction Source: MGI
    12. visual learning Source: MGI

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calmodulin-binding, cAMP, cGMP, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_227001. Cam-PDE 1 activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (EC:3.1.4.17)
    Short name:
    Cam-PDE 1B
    Alternative name(s):
    63 kDa Cam-PDE
    Gene namesi
    Name:Pde1b
    Synonyms:Pde1b1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:97523. Pde1b.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. neuronal cell body Source: Ensembl
    3. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 535535Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1BPRO_0000198790Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei465 – 4651Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ01065.
    PaxDbiQ01065.
    PRIDEiQ01065.

    PTM databases

    PhosphoSiteiQ01065.

    Expressioni

    Gene expression databases

    ArrayExpressiQ01065.
    BgeeiQ01065.
    CleanExiMM_PDE1B.
    GenevestigatoriQ01065.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi202075. 2 interactions.
    IntActiQ01065. 1 interaction.
    MINTiMINT-4106830.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01065.
    SMRiQ01065. Positions 145-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni27 – 4721Calmodulin-bindingSequence AnalysisAdd
    BLAST
    Regioni196 – 495300CatalyticBy similarityAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG139098.
    GeneTreeiENSGT00660000095451.
    HOGENOMiHOG000231888.
    HOVERGENiHBG056120.
    InParanoidiQ01065.
    KOiK13755.
    OMAiSTAVHNC.
    OrthoDBiEOG7X9G6J.
    PhylomeDBiQ01065.
    TreeFamiTF314638.

    Family and domain databases

    Gene3Di1.10.1300.10. 2 hits.
    InterProiIPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    IPR013706. PDEase_N.
    [Graphical view]
    PfamiPF00233. PDEase_I. 1 hit.
    PF08499. PDEase_I_N. 1 hit.
    [Graphical view]
    PRINTSiPR00387. PDIESTERASE1.
    SMARTiSM00471. HDc. 1 hit.
    [Graphical view]
    PROSITEiPS00126. PDEASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q01065-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELSPRSPPE MLESDCPSPL ELKSAPSKKM WIKLRSLLRY MVKQLENGEV    50
    NIEELKKNLE YTASLLEAVY IDETRQILDT EDELRELRSD AVPSEVRDWL 100
    ASTFTQQTRA KGRRAEEKPK FRSIVHAVQA GIFVERMFRR TYTSVGPTYS 150
    TAVHNCLKNL DLWCFDVFSL NRAADDHALR TIVFELLTRH SLISRFKIPT 200
    VFLMSFLEAL ETGYGKYKNP YHNQIHAADV TQTVHCFLLR TGMVHCLSEI 250
    EVLAIIFAAA IHDYEHTGTT NSFHIQTKSE CAILYNDRSV LENHHISSVF 300
    RMMQDDEMNI FINLTKDEFA ELRALVIEMV LATDMSCHFQ QVKTMKTALQ 350
    QLERIDKSKA LSLLLHAADI SHPTKQWSVH SRWTKALMEE FFRQGDKEAE 400
    LGLPFSPLCD RTSTLVAQSQ IGFIDFIVEP TFSVLTDVAE KSVQPLADDD 450
    SKPKSQPSFQ WRQPSLDVDV GDPNPDVVSF RATWTKYIQE NKQKWKERAA 500
    SGITNQMSID ELSPCEEEAP SSPAEDEHNQ NGNLD 535
    Length:535
    Mass (Da):61,226
    Last modified:October 1, 1996 - v2
    Checksum:iF87A585537C8D1CD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381L → M(PubMed:9657856)Curated
    Sequence conflicti224 – 2241Q → R in AAA37367. (PubMed:1326532)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01695 mRNA. Translation: AAA39902.1.
    AH007066 Genomic DNA. Translation: AAC96022.1.
    M94538 mRNA. Translation: AAA37367.1.
    CCDSiCCDS27904.1.
    PIRiA46378.
    RefSeqiNP_032826.1. NM_008800.2.
    UniGeneiMm.390792.

    Genome annotation databases

    EnsembliENSMUST00000023132; ENSMUSP00000023132; ENSMUSG00000022489.
    GeneIDi18574.
    KEGGimmu:18574.
    UCSCiuc007xyh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L01695 mRNA. Translation: AAA39902.1 .
    AH007066 Genomic DNA. Translation: AAC96022.1 .
    M94538 mRNA. Translation: AAA37367.1 .
    CCDSi CCDS27904.1.
    PIRi A46378.
    RefSeqi NP_032826.1. NM_008800.2.
    UniGenei Mm.390792.

    3D structure databases

    ProteinModelPortali Q01065.
    SMRi Q01065. Positions 145-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202075. 2 interactions.
    IntActi Q01065. 1 interaction.
    MINTi MINT-4106830.

    PTM databases

    PhosphoSitei Q01065.

    Proteomic databases

    MaxQBi Q01065.
    PaxDbi Q01065.
    PRIDEi Q01065.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023132 ; ENSMUSP00000023132 ; ENSMUSG00000022489 .
    GeneIDi 18574.
    KEGGi mmu:18574.
    UCSCi uc007xyh.1. mouse.

    Organism-specific databases

    CTDi 5153.
    MGIi MGI:97523. Pde1b.

    Phylogenomic databases

    eggNOGi NOG139098.
    GeneTreei ENSGT00660000095451.
    HOGENOMi HOG000231888.
    HOVERGENi HBG056120.
    InParanoidi Q01065.
    KOi K13755.
    OMAi STAVHNC.
    OrthoDBi EOG7X9G6J.
    PhylomeDBi Q01065.
    TreeFami TF314638.

    Enzyme and pathway databases

    Reactomei REACT_227001. Cam-PDE 1 activation.

    Miscellaneous databases

    NextBioi 294424.
    PROi Q01065.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01065.
    Bgeei Q01065.
    CleanExi MM_PDE1B.
    Genevestigatori Q01065.

    Family and domain databases

    Gene3Di 1.10.1300.10. 2 hits.
    InterProi IPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    IPR013706. PDEase_N.
    [Graphical view ]
    Pfami PF00233. PDEase_I. 1 hit.
    PF08499. PDEase_I_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00387. PDIESTERASE1.
    SMARTi SM00471. HDc. 1 hit.
    [Graphical view ]
    PROSITEi PS00126. PDEASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of DNA encoding a calmodulin-dependent phosphodiesterase enriched in striatum."
      Polli J.W., Kincaid R.L.
      Proc. Natl. Acad. Sci. U.S.A. 89:11079-11083(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Genomic structure and chromosome location of the murine PDE1B phosphodiesterase gene."
      Reed T.M., Browning J.E., Blough R.I., Vorhees C.V., Repaske D.R.
      Mamm. Genome 9:571-576(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-535.
      Strain: 129/SvJ.
    3. "A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase."
      Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.
      J. Biol. Chem. 267:18683-18688(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 221-336.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.

    Entry informationi

    Entry nameiPDE1B_MOUSE
    AccessioniPrimary (citable) accession number: Q01065
    Secondary accession number(s): O35384
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    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