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Q01062

- PDE2A_RAT

UniProt

Q01062 - PDE2A_RAT

Protein

cGMP-dependent 3',5'-cyclic phosphodiesterase

Gene

Pde2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei419 – 4191cGMPBy similarity
    Binding sitei434 – 4341cGMPBy similarity
    Binding sitei487 – 4871cGMPBy similarity
    Active sitei644 – 6441Proton donorBy similarity
    Metal bindingi648 – 6481Divalent metal cation 1By similarity
    Metal bindingi684 – 6841Divalent metal cation 1By similarity
    Metal bindingi685 – 6851Divalent metal cation 1By similarity
    Metal bindingi685 – 6851Divalent metal cation 2By similarity
    Binding sitei685 – 6851SubstrateBy similarity
    Metal bindingi796 – 7961Divalent metal cation 1By similarity
    Binding sitei796 – 7961SubstrateBy similarity

    GO - Molecular functioni

    1. cAMP binding Source: RGD
    2. cGMP binding Source: RGD
    3. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: RGD
    4. cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
    5. drug binding Source: UniProtKB
    6. metal ion binding Source: UniProtKB-KW
    7. protein binding Source: IntAct
    8. protein homodimerization activity Source: RGD

    GO - Biological processi

    1. cAMP catabolic process Source: UniProtKB
    2. cAMP-mediated signaling Source: UniProtKB
    3. cellular response to cGMP Source: UniProtKB
    4. cellular response to drug Source: UniProtKB
    5. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: UniProtKB
    6. cellular response to macrophage colony-stimulating factor stimulus Source: UniProtKB
    7. cellular response to mechanical stimulus Source: UniProtKB
    8. cGMP catabolic process Source: RGD
    9. cGMP-mediated signaling Source: UniProtKB
    10. establishment of endothelial barrier Source: UniProtKB
    11. negative regulation of cAMP biosynthetic process Source: UniProtKB
    12. negative regulation of protein import into nucleus, translocation Source: UniProtKB
    13. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    14. negative regulation of vascular permeability Source: UniProtKB
    15. positive regulation of inflammatory response Source: UniProtKB
    16. positive regulation of vascular permeability Source: UniProtKB
    17. protein targeting to mitochondrion Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SABIO-RKQ01062.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cGMP-dependent 3',5'-cyclic phosphodiesterase (EC:3.1.4.17)
    Alternative name(s):
    Cyclic GMP-stimulated phosphodiesterase
    Short name:
    CGS-PDE
    Short name:
    cGSPDE
    Gene namesi
    Name:Pde2a
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620965. Pde2a.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB
    4. Golgi apparatus Source: UniProtKB
    5. membrane raft Source: RGD
    6. mitochondrial matrix Source: UniProtKB
    7. nucleus Source: UniProtKB
    8. perinuclear region of cytoplasm Source: UniProtKB
    9. plasma membrane Source: UniProtKB
    10. presynaptic membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 928928cGMP-dependent 3',5'-cyclic phosphodiesterasePRO_0000198798Add
    BLAST

    Proteomic databases

    PRIDEiQ01062.

    PTM databases

    PhosphoSiteiQ01062.

    Expressioni

    Tissue specificityi

    Brain.

    Gene expression databases

    GenevestigatoriQ01062.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AipQ5FWY52EBI-1786062,EBI-1786045

    Protein-protein interaction databases

    IntActiQ01062. 1 interaction.
    STRINGi10116.ENSRNOP00000026586.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01062.
    SMRiQ01062. Positions 210-550, 566-903.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini228 – 365138GAF 1Add
    BLAST
    Domaini397 – 536140GAF 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni621 – 879259CatalyticBy similarityAdd
    BLAST
    Regioni644 – 6485Substrate bindingBy similarity

    Domaini

    GAF 1 functions as a dimerization domain, whereas GAF 2 binds cGMP, which causes activation of the catalytic activity of the enzyme.By similarity

    Sequence similaritiesi

    Contains 2 GAF domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG270709.
    HOGENOMiHOG000007068.
    HOVERGENiHBG053540.
    KOiK18283.
    PhylomeDBiQ01062.

    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. 3 hits.
    SM00471. HDc. 1 hit.
    [Graphical view]
    SUPFAMiSSF55781. SSF55781. 3 hits.
    PROSITEiPS00126. PDEASE_I. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms.

    Isoform PDE2A3 (identifier: Q01062-1) [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

    MVLVLHHILI AVVQFLRRGQ QVFLKPDEPP PQPCADSLQD ALLSLGAVID    50
    IAGLRQAAKD ALSAVLPKVE TVYTYLVDGE SRLVCEDPPH ELPQEGKIRE 100
    AVISRKRLSC DGLGPSDLLG KPLARLVAPL APDTQVLVIP LLDKETGTVA 150
    AVILVHCGQL SDSEEQSLQV VEKHALVALQ RVQALQQRRP EAVQNTSADP 200
    SEDQKDEKGY TAHDRKILQL CGELYDLDAT SLQLKVLRYL QQETQATHCC 250
    LLLVSEDNLQ LSCKVIGEKV LGEEVSFPLT MGRLGQVVED KQCIQLKDLT 300
    SDDVQQLQNM LGCELRAMLC VPVISRATDQ VVALACAFNK LGGDFFTDED 350
    ERAIQHCFHY TGTVLTSTLA FQKEQKLKCE CQALLQVAKN LFTHLDDVSV 400
    LLQEIITEAR NLSNAEICSV FLLDQNELVA KVFDGGVVDD ESYEIRIPAD 450
    QGIAGHVATT GQILNIPDAY AHPLFYRGVD DSTGFRTRNI LCFPIKNENQ 500
    EVIGVAELVN KINGPWFSKF DEDLATAFSI YCGISIAHSL LYKKVNEAQY 550
    RSHLANEMMM YHMKVSDDEY TKLLHDGIQP VAAIDSNFAN FTYTPRSLPE 600
    DDTSMAILSM LQDMNFINNY KIDCPTLARF CLMVKKGYRD PPYHNWMHAF 650
    SVSHFCYLLY KNLELSNYLE DIEIFALFIS CMCHDLDHRG TNNSFQVASK 700
    SVLAALYSSE GSVMERHHFA QAIAILNTHG CNIFDHFSRK DYQRMLDLMR 750
    DIILATDLAH HLRIFKDLQK MAEVGYDRNN KQHHRLLLCL LMTSCDLSDQ 800
    TKGWKTTRKI AELIYKEFFS QGDLEKAMGN RPMEMMDREK AYIPELQISF 850
    MEHIAMPIYK LLQDLFPKAA ELYERVASNR EHWTKVSHKF TIRGLPSNNS 900
    LDFLDEEYEV PDLDVTRAPV NGCCSLEG 928
    Length:928
    Mass (Da):104,664
    Last modified:October 1, 1996 - v2
    Checksum:iEF0B8C1E266EAB18
    GO
    Isoform PDE2A1 (identifier: Q01062-2)

    Sequence is not available
    Length:
    Mass (Da):
    Isoform PDE2A2 (identifier: Q01062-3)

    Sequence is not available
    Length:
    Mass (Da):

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti646 – 6461W → R in AAA40922. (PubMed:1326532)Curated
    Sequence conflicti758 – 7581L → M(PubMed:1326532)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21101 mRNA. Translation: AAA63683.1.
    M94540 mRNA. Translation: AAA40922.1.
    PIRiJC2486.
    RefSeqiNP_001137319.1. NM_001143847.1.
    NP_112341.1. NM_031079.1. [Q01062-1]
    UniGeneiRn.10044.

    Genome annotation databases

    GeneIDi81743.
    KEGGirno:81743.
    UCSCiRGD:620965. rat. [Q01062-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21101 mRNA. Translation: AAA63683.1 .
    M94540 mRNA. Translation: AAA40922.1 .
    PIRi JC2486.
    RefSeqi NP_001137319.1. NM_001143847.1.
    NP_112341.1. NM_031079.1. [Q01062-1 ]
    UniGenei Rn.10044.

    3D structure databases

    ProteinModelPortali Q01062.
    SMRi Q01062. Positions 210-550, 566-903.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q01062. 1 interaction.
    STRINGi 10116.ENSRNOP00000026586.

    Chemistry

    BindingDBi Q01062.
    ChEMBLi CHEMBL4650.

    PTM databases

    PhosphoSitei Q01062.

    Proteomic databases

    PRIDEi Q01062.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 81743.
    KEGGi rno:81743.
    UCSCi RGD:620965. rat. [Q01062-1 ]

    Organism-specific databases

    CTDi 5138.
    RGDi 620965. Pde2a.

    Phylogenomic databases

    eggNOGi NOG270709.
    HOGENOMi HOG000007068.
    HOVERGENi HBG053540.
    KOi K18283.
    PhylomeDBi Q01062.

    Enzyme and pathway databases

    SABIO-RK Q01062.

    Miscellaneous databases

    NextBioi 615464.
    PROi Q01062.

    Gene expression databases

    Genevestigatori Q01062.

    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. 3 hits.
    SM00471. HDc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55781. SSF55781. 3 hits.
    PROSITEi PS00126. PDEASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Brain.
    2. "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 643-759.

    Entry informationi

    Entry nameiPDE2A_RAT
    AccessioniPrimary (citable) accession number: Q01062
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    cGMP binds at an allosteric activator site.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3