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P14270

- PDE4D_RAT

UniProt

P14270 - PDE4D_RAT

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Protein

cAMP-specific 3',5'-cyclic phosphodiesterase 4D

Gene
Pde4d
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes.

Catalytic activityi

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.

Enzyme regulationi

Activated by phosphatidic acid By similarity. Inhibited by rolipram.1 Publication

Kineticsi

    Vmax=18 pmol/min/mg enzyme for cAMP (in the absence of follicle-stimulating hormone (FSH))1 Publication

    Vmax=5 pmol/min/mg enzyme for cAMP (in the presence of follicle-stimulating hormone (FSH))

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei457 – 4571Proton donor By similarity
    Metal bindingi461 – 4611Divalent metal cation 1 By similarity
    Metal bindingi497 – 4971Divalent metal cation 1 By similarity
    Metal bindingi498 – 4981Divalent metal cation 1 By similarity
    Metal bindingi498 – 4981Divalent metal cation 2 By similarity
    Binding sitei498 – 4981cAMP By similarity
    Metal bindingi615 – 6151Divalent metal cation 1 By similarity
    Sitei618 – 6181Binds AMP, but not cAMP By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi457 – 4615cAMP By similarity

    GO - Molecular functioni

    1. 3',5'-cyclic-AMP phosphodiesterase activity Source: RGD
    2. beta-2 adrenergic receptor binding Source: BHF-UCL
    3. cAMP binding Source: RGD
    4. cyclic-nucleotide phosphodiesterase activity Source: RGD
    5. enzyme binding Source: BHF-UCL
    6. metal ion binding Source: UniProtKB-KW
    7. protein binding Source: IntAct
    8. protein domain specific binding Source: RGD
    9. SH3 domain binding Source: RGD

    GO - Biological processi

    1. adrenergic receptor signaling pathway Source: BHF-UCL
    2. adrenergic receptor signaling pathway involved in positive regulation of heart rate Source: BHF-UCL
    3. cAMP catabolic process Source: UniProtKB
    4. cellular protein complex assembly Source: RGD
    5. establishment of endothelial barrier Source: UniProtKB
    6. lung development Source: RGD
    7. memory Source: RGD
    8. positive regulation of smooth muscle cell migration Source: RGD
    9. positive regulation of smooth muscle cell proliferation Source: RGD
    10. regulation of cardiac muscle cell contraction Source: BHF-UCL
    11. regulation of G-protein coupled receptor protein signaling pathway Source: RGD
    12. regulation of protein kinase A signaling Source: RGD
    13. regulation of receptor activity Source: BHF-UCL
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00762; UER00747.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cAMP-specific 3',5'-cyclic phosphodiesterase 4D (EC:3.1.4.53)
    Alternative name(s):
    DPDE3
    Gene namesi
    Name:Pde4d
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi3281. Pde4d.

    Subcellular locationi

    Apical cell membrane. Cytoplasm. Membrane. Cytoplasmcytoskeleton. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Found in the soluble fraction, associated with membranes, and associated with the cytoskeleton and the centrosome. Colocalized with SHANK2 to the apical membrane of colonic crypt cells.3 Publications

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. centrosome Source: RGD
    3. Golgi apparatus Source: RGD
    4. myofibril Source: RGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 803803cAMP-specific 3',5'-cyclic phosphodiesterase 4DPRO_0000198816Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei294 – 2941Phosphoserine By similarity
    Modified residuei296 – 2961Phosphoserine By similarity
    Cross-linki382 – 382Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

    Post-translational modificationi

    Isoform 1 and isoform 9 are rapidly activated by PKA through phosphorylation. Long isoforms that share a conserved PKA phosphorylation site in the N-terminus are also activated.
    Sumoylation of long isoforms by PIAS4 augments their activation by PKA phosphorylation and represses their inhibition by ERK phosphorylation By similarity.

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP14270.

    PTM databases

    PhosphoSiteiP14270.

    Expressioni

    Tissue specificityi

    Expressed in epithelial cells. Isoform 33, isoform 4, isoform 5 and isoform 9 are expressed in brain. Isoform 33, isoform 5, isoform 8 and isoform 9 are expressed in heart (at protein level). Isoform 4 and isoform 6 are strongly expressed in cortex and cerebellum. Isoform 7 is strongly expressed in cortex and testis; weakly expressed in kidney, lung, spleen and cerebellum. Isoform 8 is strongly expressed in lung, heart and liver. Isoform 31, isoform 32, isoform 33, isoform 5 and isoform 9 are widely distributed.2 Publications

    Inductioni

    Up-regulated by cAMP and follicle-stimulating hormone.2 Publications

    Gene expression databases

    GenevestigatoriP14270.

    Interactioni

    Subunit structurei

    Homodimer for the long isoforms. Isoforms with truncated N-termini are monomeric. Binds ARRB2. Isoform 33 is part of a ternary complex containing PRKAR2A, PRKAR2B and AKAP9. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) By similarity. Interacts with PDE4DIP. Isoform 5 interacts (via N-terminal region) with SHANK2 (via proline-rich region); the interaction is increased in a PKA-dependent manner. Isoform 33, isoform 4, isoform 7, isoform 8 and isoform 9 but not isoform 32 and isoform 6 interact with SHANK2. Isoform 31 interacts weakly with SHANK2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADRB1P085882EBI-8333209,EBI-991009From a different organism.
    Shank2Q9QX744EBI-9032440,EBI-397902

    Protein-protein interaction databases

    BioGridi246765. 4 interactions.
    IntActiP14270. 2 interactions.
    STRINGi10116.ENSRNOP00000015138.

    Structurei

    3D structure databases

    ProteinModelPortaliP14270.
    SMRiP14270. Positions 376-736.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG122287.
    GeneTreeiENSGT00740000115148.
    HOVERGENiHBG108239.
    KOiK01120.
    OMAiQHEVEMP.
    PhylomeDBiP14270.

    Family and domain databases

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

    Sequences (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Isoform 4 (identifier: P14270-5) [UniParc]FASTAAdd to Basket

    Also known as: PDE4D4

    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

    MEAEGSSVPA RAGSHEGSDS SGGAALKAPK HLWRHEQHHQ YPLRQPQFRL    50
    LHPHHHLPPP PPPSPQPQLQ PPPPPPLPPP PPPPGATRGR YASSGASRVR 100
    HRGYSDTERY LYCRAMDRTS YAVETGHRPG LKKSRMSWPS SFQGLRRFDV 150
    DNGTSAGRSP LDPMTSPGSG LILQANFVHS QRRESFLYRS DSDYDLSPKS 200
    MSRNSSIASD IHGDDLIVTP FAQVLASLRT VRNNFAALTN LQDRAPSKRS 250
    PMCNQPSINK ATITEEAYQK LASETLEELD WCLDQLETLQ TRHSVSEMAS 300
    NKFKRMLNRE LTHLSEMSRS GNQVSEYISN TFLDKQHEVE IPSPTQKEKE 350
    KKKRPMSQIS GVKKLMHSSS LTNSCIPRFG VKTEQEDVLA KELEDVNKWG 400
    LHVFRIAELS GNRPLTVIMH TIFQERDLLK TFKIPVDTLI TYLMTLEDHY 450
    HADVAYHNNI HAADVVQSTH VLLSTPALEA VFTDLEILAA IFASAIHDVD 500
    HPGVSNQFLI NTNSELALMY NDSSVLENHH LAVGFKLLQE ENCDIFQNLT 550
    KKQRQSLRKM AIDIVLATDM SKHMNLLADL KTMVETKKVT SSGVLLLDNY 600
    SDRIQVLQNM VHCADLSNPT KPLQLYRQWT DRIMEEFFRQ GDRERERGME 650
    ISPMCDKHNA SVEKSQVGFI DYIVHPLWET WADLVHPDAQ DILDTLEDNR 700
    EWYQSTIPQS PSPAPDDQED GRQGQTEKFQ FELTLEEDGE SDTEKDSGSQ 750
    VEEDTSCSDS KTLCTQDSES TEIPLDEQVE EEAVAEEESQ PQTGVADDCC 800
    PDT 803
    Length:803
    Mass (Da):90,552
    Last modified:January 4, 2005 - v4
    Checksum:i13E28B257556496D
    GO
    Isoform 33 (identifier: P14270-1) [UniParc]FASTAAdd to Basket

    Also known as: PDE4D3, PDE3.3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-131: Missing.
         132-147: KKSRMSWPSSFQGLRR → MMHVNTFPFRRHSWIC

    Show »
    Length:672
    Mass (Da):76,263
    Checksum:i63CE38FA654A0BDD
    GO
    Isoform 31 (identifier: P14270-2) [UniParc]FASTAAdd to Basket

    Also known as: PDE3.1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-264: MEAEGSSVPA...QPSINKATIT → MKEQPSCAGT...TESPFPCLFA

    Show »
    Length:584
    Mass (Da):66,243
    Checksum:i7C0DAEB75774F2F8
    GO
    Isoform 32 (identifier: P14270-3) [UniParc]FASTAAdd to Basket

    Also known as: PDE3.2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-297: Missing.

    Show »
    Length:506
    Mass (Da):57,601
    Checksum:i7DCA5A564384FC34
    GO
    Isoform 5 (identifier: P14270-8) [UniParc]FASTAAdd to Basket

    Also known as: PDE4D5

    The sequence of this isoform differs from the canonical sequence as follows:
         1-147: MEAEGSSVPA...WPSSFQGLRR → MAQQTTSPDT...QRRFTVAHTC

    Show »
    Length:745
    Mass (Da):84,335
    Checksum:i09DEADF7223F77BF
    GO
    Isoform 6 (identifier: P14270-7) [UniParc]FASTAAdd to Basket

    Also known as: PDE4D6

    The sequence of this isoform differs from the canonical sequence as follows:
         1-286: Missing.
         287-301: ETLQTRHSVSEMASN → MPEANYLLSVSWGYI

    Show »
    Length:517
    Mass (Da):58,923
    Checksum:i251BF853D7CE6870
    GO
    Isoform 7 (identifier: P14270-4) [UniParc]FASTAAdd to Basket

    Also known as: PDE4D7

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: Missing.
         57-147: LPPPPPPSPQ...WPSSFQGLRR → MERNTCDVLS...IAVTSADSTG

    Show »
    Length:747
    Mass (Da):84,430
    Checksum:iD63B9EF50AA3EFC9
    GO
    Isoform 8 (identifier: P14270-9) [UniParc]FASTAAdd to Basket

    Also known as: PDE4D8

    The sequence of this isoform differs from the canonical sequence as follows:
         1-147: MEAEGSSVPA...WPSSFQGLRR → MAFVWDPLGVTVPGPSPRTRTRLRFSKSYS

    Show »
    Length:686
    Mass (Da):77,611
    Checksum:iD1F73EAEBDC6AA66
    GO
    Isoform 9 (identifier: P14270-6) [UniParc]FASTAAdd to Basket

    Also known as: PDE4D9

    The sequence of this isoform differs from the canonical sequence as follows:
         1-125: Missing.
         126-147: GHRPGLKKSRMSWPSSFQGLRR → MSIIMKPRSRSTSSLRTTEAVC

    Show »
    Length:678
    Mass (Da):76,656
    Checksum:iE3069D16ADEBEC6C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 297297Missing in isoform 32. VSP_004582Add
    BLAST
    Alternative sequencei1 – 286286Missing in isoform 6. VSP_012404Add
    BLAST
    Alternative sequencei1 – 264264MEAEG…KATIT → MKEQPSCAGTGHPSMAGYGR MAPFELAGGPVKRLRTESPF PCLFA in isoform 31. VSP_004581Add
    BLAST
    Alternative sequencei1 – 147147MEAEG…QGLRR → MAQQTTSPDTLTVPEVDNPH VPNPWLNEDLVKSLRENLLQ HEKSKTARKSVSPKLSPVIS PRNSPRLLRRMLLSSNIPKQ RRFTVAHTC in isoform 5. VSP_053485Add
    BLAST
    Alternative sequencei1 – 147147MEAEG…QGLRR → MAFVWDPLGVTVPGPSPRTR TRLRFSKSYS in isoform 8. VSP_053486Add
    BLAST
    Alternative sequencei1 – 131131Missing in isoform 33. VSP_012398Add
    BLAST
    Alternative sequencei1 – 125125Missing in isoform 9. VSP_012402Add
    BLAST
    Alternative sequencei1 – 5656Missing in isoform 7. VSP_012400Add
    BLAST
    Alternative sequencei57 – 14791LPPPP…QGLRR → MERNTCDVLSRSKSASEETL HSCNDEEDPFRGMEPYLVRR LSSRSIQLPPLAFRQLEQTD LRSESENIPRPTSLPLKILP LIAVTSADSTG in isoform 7. VSP_012401Add
    BLAST
    Alternative sequencei126 – 14722GHRPG…QGLRR → MSIIMKPRSRSTSSLRTTEA VC in isoform 9. VSP_012403Add
    BLAST
    Alternative sequencei132 – 14716KKSRM…QGLRR → MMHVNTFPFRRHSWIC in isoform 33. VSP_012399Add
    BLAST
    Alternative sequencei287 – 30115ETLQT…EMASN → MPEANYLLSVSWGYI in isoform 6. VSP_012405Add
    BLAST

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti226 – 2261A → N in AAA56857. 1 Publication
    Sequence conflicti357 – 3571S → P in AAQ90405. 1 Publication
    Sequence conflicti480 – 4867Missing in AAA18924. 1 Publication
    Sequence conflicti480 – 4867Missing in AAA18925. 1 Publication
    Sequence conflicti641 – 6411G → E in AAC26969. 1 Publication
    Sequence conflicti757 – 7571C → Y in AAA56857. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09455 mRNA. Translation: AAA20401.1.
    U09457 mRNA. Translation: AAB81869.1.
    U09456 mRNA. Translation: AAA20393.1.
    U01280
    , U01278, U01282, U01283, U01284, U01285, U01286, U01287, U01279 Unassigned DNA. Translation: AAA18925.1.
    U01280
    , U01278, U01282, U01283, U01284, U01285, U01286, U01287, U01279 Unassigned DNA. Translation: AAA18924.1.
    AF031373 mRNA. Translation: AAB95266.1.
    AF536974 mRNA. Translation: AAN10116.1.
    EF102484 mRNA. Translation: ABK97408.1.
    EF121818 mRNA. Translation: ABL14108.1.
    AF536979 mRNA. Translation: AAN10121.1.
    AY388961 mRNA. Translation: AAQ90405.1.
    AABR06012736 Genomic DNA. No translation available.
    AABR06012737 Genomic DNA. No translation available.
    AABR06012738 Genomic DNA. No translation available.
    AABR06012739 Genomic DNA. No translation available.
    AABR06012740 Genomic DNA. No translation available.
    AABR06012741 Genomic DNA. No translation available.
    AABR06012742 Genomic DNA. No translation available.
    AABR06012743 Genomic DNA. No translation available.
    AABR06012744 Genomic DNA. No translation available.
    AABR06012745 Genomic DNA. No translation available.
    AABR06012746 Genomic DNA. No translation available.
    AABR06012747 Genomic DNA. No translation available.
    AABR06012748 Genomic DNA. No translation available.
    AABR06012749 Genomic DNA. No translation available.
    AABR06012750 Genomic DNA. No translation available.
    AABR06012751 Genomic DNA. No translation available.
    AABR06012752 Genomic DNA. No translation available.
    AABR06012753 Genomic DNA. No translation available.
    AABR06012754 Genomic DNA. No translation available.
    AABR06012755 Genomic DNA. No translation available.
    AABR06012756 Genomic DNA. No translation available.
    AABR06012757 Genomic DNA. No translation available.
    AABR06012758 Genomic DNA. No translation available.
    AABR06012759 Genomic DNA. No translation available.
    AABR06012760 Genomic DNA. No translation available.
    L27059 mRNA. Translation: AAA56857.1.
    L27060 mRNA. Translation: AAC26969.1.
    PIRiB53109.
    I61259.
    RefSeqiNP_001106799.1. NM_001113328.1.
    NP_001106800.1. NM_001113329.1. [P14270-4]
    NP_001106803.1. NM_001113332.1. [P14270-8]
    NP_001106805.1. NM_001113334.1. [P14270-9]
    NP_058728.1. NM_017032.1. [P14270-1]
    UniGeneiRn.163460.
    Rn.95959.

    Genome annotation databases

    EnsembliENSRNOT00000015138; ENSRNOP00000015138; ENSRNOG00000042536. [P14270-6]
    ENSRNOT00000066384; ENSRNOP00000063446; ENSRNOG00000042536. [P14270-9]
    ENSRNOT00000067546; ENSRNOP00000062384; ENSRNOG00000042536. [P14270-7]
    ENSRNOT00000073552; ENSRNOP00000067171; ENSRNOG00000042536. [P14270-8]
    GeneIDi24627.
    KEGGirno:24627.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09455 mRNA. Translation: AAA20401.1 .
    U09457 mRNA. Translation: AAB81869.1 .
    U09456 mRNA. Translation: AAA20393.1 .
    U01280
    , U01278 , U01282 , U01283 , U01284 , U01285 , U01286 , U01287 , U01279 Unassigned DNA. Translation: AAA18925.1 .
    U01280
    , U01278 , U01282 , U01283 , U01284 , U01285 , U01286 , U01287 , U01279 Unassigned DNA. Translation: AAA18924.1 .
    AF031373 mRNA. Translation: AAB95266.1 .
    AF536974 mRNA. Translation: AAN10116.1 .
    EF102484 mRNA. Translation: ABK97408.1 .
    EF121818 mRNA. Translation: ABL14108.1 .
    AF536979 mRNA. Translation: AAN10121.1 .
    AY388961 mRNA. Translation: AAQ90405.1 .
    AABR06012736 Genomic DNA. No translation available.
    AABR06012737 Genomic DNA. No translation available.
    AABR06012738 Genomic DNA. No translation available.
    AABR06012739 Genomic DNA. No translation available.
    AABR06012740 Genomic DNA. No translation available.
    AABR06012741 Genomic DNA. No translation available.
    AABR06012742 Genomic DNA. No translation available.
    AABR06012743 Genomic DNA. No translation available.
    AABR06012744 Genomic DNA. No translation available.
    AABR06012745 Genomic DNA. No translation available.
    AABR06012746 Genomic DNA. No translation available.
    AABR06012747 Genomic DNA. No translation available.
    AABR06012748 Genomic DNA. No translation available.
    AABR06012749 Genomic DNA. No translation available.
    AABR06012750 Genomic DNA. No translation available.
    AABR06012751 Genomic DNA. No translation available.
    AABR06012752 Genomic DNA. No translation available.
    AABR06012753 Genomic DNA. No translation available.
    AABR06012754 Genomic DNA. No translation available.
    AABR06012755 Genomic DNA. No translation available.
    AABR06012756 Genomic DNA. No translation available.
    AABR06012757 Genomic DNA. No translation available.
    AABR06012758 Genomic DNA. No translation available.
    AABR06012759 Genomic DNA. No translation available.
    AABR06012760 Genomic DNA. No translation available.
    L27059 mRNA. Translation: AAA56857.1 .
    L27060 mRNA. Translation: AAC26969.1 .
    PIRi B53109.
    I61259.
    RefSeqi NP_001106799.1. NM_001113328.1.
    NP_001106800.1. NM_001113329.1. [P14270-4 ]
    NP_001106803.1. NM_001113332.1. [P14270-8 ]
    NP_001106805.1. NM_001113334.1. [P14270-9 ]
    NP_058728.1. NM_017032.1. [P14270-1 ]
    UniGenei Rn.163460.
    Rn.95959.

    3D structure databases

    ProteinModelPortali P14270.
    SMRi P14270. Positions 376-736.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246765. 4 interactions.
    IntActi P14270. 2 interactions.
    STRINGi 10116.ENSRNOP00000015138.

    Chemistry

    BindingDBi P14270.
    ChEMBLi CHEMBL2094267.

    PTM databases

    PhosphoSitei P14270.

    Proteomic databases

    PRIDEi P14270.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000015138 ; ENSRNOP00000015138 ; ENSRNOG00000042536 . [P14270-6 ]
    ENSRNOT00000066384 ; ENSRNOP00000063446 ; ENSRNOG00000042536 . [P14270-9 ]
    ENSRNOT00000067546 ; ENSRNOP00000062384 ; ENSRNOG00000042536 . [P14270-7 ]
    ENSRNOT00000073552 ; ENSRNOP00000067171 ; ENSRNOG00000042536 . [P14270-8 ]
    GeneIDi 24627.
    KEGGi rno:24627.

    Organism-specific databases

    CTDi 5144.
    RGDi 3281. Pde4d.

    Phylogenomic databases

    eggNOGi NOG122287.
    GeneTreei ENSGT00740000115148.
    HOVERGENi HBG108239.
    KOi K01120.
    OMAi QHEVEMP.
    PhylomeDBi P14270.

    Enzyme and pathway databases

    UniPathwayi UPA00762 ; UER00747 .

    Miscellaneous databases

    NextBioi 35580187.

    Gene expression databases

    Genevestigatori P14270.

    Family and domain databases

    Gene3Di 1.10.1300.10. 1 hit.
    InterProi IPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    [Graphical view ]
    Pfami PF00233. PDEase_I. 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

    « Hide 'large scale' publications
    1. "The mRNA encoding a high-affinity cAMP phosphodiesterase is regulated by hormones and cAMP."
      Swinnen J.V., Joseph D.R., Conti M.
      Proc. Natl. Acad. Sci. U.S.A. 86:8197-8201(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 31), INDUCTION.
      Tissue: Testis.
    2. "The ratPDE3/IVd phosphodiesterase gene codes for multiple proteins differentially activated by cAMP-dependent protein kinase."
      Sette C., Vicini E., Conti M.
      J. Biol. Chem. 269:18271-18274(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 31; 32 AND 33).
    3. Conti M.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 6.
    4. "Structure of two rat genes coding for closely related rolipram-sensitive cAMP phosphodiesterases. Multiple mRNA variants originate from alternative splicing and multiple start sites."
      Monaco L., Vicini E., Conti M.
      J. Biol. Chem. 269:347-357(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 31 AND 32).
      Strain: Wistar.
    5. Erratum
      Monaco L., Vicini E., Conti M.
      J. Biol. Chem. 269:20806-20806(1994)
    6. "Characterization of a cAMP-specific phosphodiesterase variant (PDE4D4) expressed in the rat brain."
      Jin S.-L.C., Kuo W.-P., Conti M.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
      Strain: Sprague-Dawley.
      Tissue: Brain.
    7. "Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7."
      Wang D., Deng C., Bugaj-Gaweda B., Kwan M., Gunwaldsen C., Leonard C., Xin X., Hu Y., Unterbeck A., De Vivo M.
      Cell. Signal. 15:883-891(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7).
      Strain: Sprague-Dawley.
    8. "Alterations in proteoglycan synthesis selectively impair FSH-induced particulate cAMP-phosphodiesterase 4 (PDE4) activation in immature rat Sertoli cells."
      Levallet G., Levallet J., Bonnamy P.J.
      Biochim. Biophys. Acta 1770:638-648(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 8), BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
    9. "Novel PDE4D isoform, PDE4D9."
      Gaweda B., De Vivo M., Wang D.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
    10. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    11. "Molecular cloning of rat homologues of the Drosophila melanogaster dunce cAMP phosphodiesterase: evidence for a family of genes."
      Swinnen J.V., Joseph D.R., Conti M.
      Proc. Natl. Acad. Sci. U.S.A. 86:5325-5329(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 224-672.
      Tissue: Testis.
    12. "Differential CNS expression of alternative mRNA isoforms of the mammalian genes encoding cAMP-specific phosphodiesterases."
      Bolger G.B., Rodgers L., Riggs M.
      Gene 149:237-244(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 226-803 (ISOFORM 33), NUCLEOTIDE SEQUENCE [MRNA] OF 253-803 (ISOFORM 31).
    13. "Phosphorylation-mediated activation and translocation of the cyclic AMP-specific phosphodiesterase PDE4D3 by cyclic AMP-dependent protein kinase and mitogen-activated protein kinases. A potential mechanism allowing for the coordinated regulation of PDE4D activity and targeting."
      Liu H., Maurice D.H.
      J. Biol. Chem. 274:10557-10565(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
    14. "Myomegalin is a novel protein of the Golgi/centrosome that interacts with a cyclic nucleotide phosphodiesterase."
      Verde I., Pahlke G., Salanova M., Zhang G., Wang S., Coletti D., Onuffer J., Jin S.-L.C., Conti M.
      J. Biol. Chem. 276:11189-11198(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDE4DIP.
    15. "Phosphodiesterase 4D and protein kinase a type II constitute a signaling unit in the centrosomal area."
      Tasken K.A., Collas P., Kemmner W.A., Witczak O., Conti M., Tasken K.
      J. Biol. Chem. 276:21999-22002(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH THE CENTROSOME (ISOFORM 33).
    16. "Splice variants of the cyclic nucleotide phosphodiesterase PDE4D are differentially expressed and regulated in rat tissue."
      Richter W., Jin S.L., Conti M.
      Biochem. J. 388:803-811(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 4; 5; 6; 7; 8; 9; 31; 32 AND 33).
    17. "Dynamic regulation of cystic fibrosis transmembrane conductance regulator by competitive interactions of molecular adaptors."
      Lee J.H., Richter W., Namkung W., Kim K.H., Kim E., Conti M., Lee M.G.
      J. Biol. Chem. 282:10414-10422(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHANK2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPDE4D_RAT
    AccessioniPrimary (citable) accession number: P14270
    Secondary accession number(s): A1E347
    , A1EC59, F1M1H7, O35470, Q6TRI0, Q8CG04, Q8CG06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 4, 2005
    Last modified: June 11, 2014
    This is version 126 of the entry and version 4 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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