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)

Q3UEI1

- PDE4C_MOUSE

UniProt

Q3UEI1 - PDE4C_MOUSE

Protein

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

Gene

Pde4c

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 78 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    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.By similarity

    Enzyme regulationi

    Inhibited by rolipram.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei389 – 3891Proton donorBy similarity
    Metal bindingi393 – 3931Divalent metal cation 1By similarity
    Metal bindingi429 – 4291Divalent metal cation 1By similarity
    Metal bindingi430 – 4301Divalent metal cation 1By similarity
    Metal bindingi430 – 4301Divalent metal cation 2By similarity
    Binding sitei430 – 4301cAMPBy similarity
    Metal bindingi547 – 5471Divalent metal cation 1By similarity
    Binding sitei547 – 5471cAMPBy similarity
    Sitei550 – 5501Binds AMP, but not cAMPBy similarity
    Binding sitei598 – 5981cAMPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi389 – 3935cAMPBy similarity

    GO - Molecular functioni

    1. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: InterPro
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cAMP catabolic process Source: UniProtKB-UniPathway
    2. signal transduction Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_203795. DARPP-32 events.
    UniPathwayiUPA00762; UER00747.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cAMP-specific 3',5'-cyclic phosphodiesterase 4C (EC:3.1.4.53)
    Gene namesi
    Name:Pde4c
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:99556. Pde4c.

    Subcellular locationi

    Cell projectioncilium 1 Publication

    GO - Cellular componenti

    1. primary cilium Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cilium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 686686cAMP-specific 3',5'-cyclic phosphodiesterase 4CPRO_0000198812Add
    BLAST

    Proteomic databases

    MaxQBiQ3UEI1.
    PaxDbiQ3UEI1.
    PRIDEiQ3UEI1.

    PTM databases

    PhosphoSiteiQ3UEI1.

    Expressioni

    Gene expression databases

    BgeeiQ3UEI1.
    CleanExiMM_PDE4C.
    GenevestigatoriQ3UEI1.

    Interactioni

    Subunit structurei

    Part of a complex containing AKAP5, ADCY5, ADCY6 and PKD2.

    Protein-protein interaction databases

    IntActiQ3UEI1. 1 interaction.
    STRINGi10090.ENSMUSP00000105722.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3UEI1.
    SMRiQ3UEI1. Positions 317-640.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi659 – 66810Poly-Glu

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG122287.
    GeneTreeiENSGT00740000115148.
    HOGENOMiHOG000236297.
    HOVERGENiHBG108239.
    InParanoidiQ3UEI1.
    KOiK01120.
    OMAiGENCDIF.
    OrthoDBiEOG7HQNBC.
    PhylomeDBiQ3UEI1.
    TreeFamiTF314638.

    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q3UEI1-1) [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

    MRRSGTALSF LWTERVREPV DSGVAPVSPL GGGVILRRFS GTLLLPPLSS    50
    RLGSSGEAES AAHVVFTIGT QGTQRNLGSA QSSFDLENGL PGGKGLLDAQ 100
    SGPSLGRALQ PPVHHVQRRE SFLYRSDSDH EPSPKAVSRT SSAASDLHGE 150
    DMIVTPFAQV LASLRTVRNN VAALAHGPGS ATRQVLLGTP PHSSQQAAPT 200
    EDSGLQLVQE TLEELDWCLE QLETLQTRRS VGEMASNKFK RMLNRELSYL 250
    SETSRSGNQV SEYISQTFLD QQAEVELPQP PTEDDPWPMA QITELRRSSH 300
    TSLPTAAIPR FGVQTDQEEQ LAKELEDTNK WGLDVFKVAE LSGNRPLTAV 350
    IFSVFQERDL LKTFQIPADT LLAYLLTLEG HYHSDVAYHN SMHAADVVQS 400
    AHVLLGTPAL EAVFTDLEVL AAIFACAIHD VDHPGVSNQF LINTNSELAL 450
    MYNDSSVLEN HHLAVGFKLL QGENCDIFRN LSTKQRLSLR RMVIDMVLAT 500
    DMSKHMSLLA DLKTMVETKK VTSLGVLLLD NYSDRIQVLQ SLVHCADLSN 550
    PAKPLPLYRQ WTERIMAEFF QQGDRERESG LDISPMCDKH TASMEKSQVG 600
    FIDYIAQPLW ETWADLVHPD AQELLDTLED NREWYQSRIP CSPPHTMGSD 650
    RFKFELTLEE AEEEEEEEDE GQCTALNRES SELPST 686
    Length:686
    Mass (Da):76,090
    Last modified:October 11, 2005 - v1
    Checksum:i4B510001564A2A08
    GO
    Isoform 2 (identifier: Q3UEI1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         537-570: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:652
    Mass (Da):72,106
    Checksum:i75B22BC077830AA9
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei537 – 57034Missing in isoform 2. 1 PublicationVSP_016663Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK149514 mRNA. Translation: BAE28930.1.
    BC030873 mRNA. Translation: AAH30873.1.
    CCDSiCCDS22378.1. [Q3UEI1-2]
    RefSeqiNP_963901.1. NM_201607.2. [Q3UEI1-2]
    UniGeneiMm.255180.

    Genome annotation databases

    EnsembliENSMUST00000034307; ENSMUSP00000034307; ENSMUSG00000031842. [Q3UEI1-2]
    ENSMUST00000110095; ENSMUSP00000105722; ENSMUSG00000031842. [Q3UEI1-1]
    GeneIDi110385.
    KEGGimmu:110385.
    UCSCiuc009mbg.1. mouse. [Q3UEI1-2]
    uc009mbh.1. mouse. [Q3UEI1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK149514 mRNA. Translation: BAE28930.1 .
    BC030873 mRNA. Translation: AAH30873.1 .
    CCDSi CCDS22378.1. [Q3UEI1-2 ]
    RefSeqi NP_963901.1. NM_201607.2. [Q3UEI1-2 ]
    UniGenei Mm.255180.

    3D structure databases

    ProteinModelPortali Q3UEI1.
    SMRi Q3UEI1. Positions 317-640.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q3UEI1. 1 interaction.
    STRINGi 10090.ENSMUSP00000105722.

    Chemistry

    BindingDBi Q3UEI1.
    ChEMBLi CHEMBL2111373.

    PTM databases

    PhosphoSitei Q3UEI1.

    Proteomic databases

    MaxQBi Q3UEI1.
    PaxDbi Q3UEI1.
    PRIDEi Q3UEI1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034307 ; ENSMUSP00000034307 ; ENSMUSG00000031842 . [Q3UEI1-2 ]
    ENSMUST00000110095 ; ENSMUSP00000105722 ; ENSMUSG00000031842 . [Q3UEI1-1 ]
    GeneIDi 110385.
    KEGGi mmu:110385.
    UCSCi uc009mbg.1. mouse. [Q3UEI1-2 ]
    uc009mbh.1. mouse. [Q3UEI1-1 ]

    Organism-specific databases

    CTDi 5143.
    MGIi MGI:99556. Pde4c.

    Phylogenomic databases

    eggNOGi NOG122287.
    GeneTreei ENSGT00740000115148.
    HOGENOMi HOG000236297.
    HOVERGENi HBG108239.
    InParanoidi Q3UEI1.
    KOi K01120.
    OMAi GENCDIF.
    OrthoDBi EOG7HQNBC.
    PhylomeDBi Q3UEI1.
    TreeFami TF314638.

    Enzyme and pathway databases

    UniPathwayi UPA00762 ; UER00747 .
    Reactomei REACT_203795. DARPP-32 events.

    Miscellaneous databases

    ChiTaRSi PDE4C. mouse.
    NextBioi 363905.
    PROi Q3UEI1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q3UEI1.
    CleanExi MM_PDE4C.
    Genevestigatori Q3UEI1.

    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

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Liver.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: FVB/N.
      Tissue: Kidney.
    3. "Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases."
      Choi Y.H., Suzuki A., Hajarnis S., Ma Z., Chapin H.C., Caplan M.J., Pontoglio M., Somlo S., Igarashi P.
      Proc. Natl. Acad. Sci. U.S.A. 108:10679-10684(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AKAP5; ADCY5; ADCY6 AND PKD2.

    Entry informationi

    Entry nameiPDE4C_MOUSE
    AccessioniPrimary (citable) accession number: Q3UEI1
    Secondary accession number(s): Q8K0P4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 78 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3