SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q01063

- PDE4D_MOUSE

UniProt

Q01063 - PDE4D_MOUSE

(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)

Protein
cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Gene
Pde4d
Organism
Mus musculus (Mouse)
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 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.

Enzyme regulationi

Inhibited by rolipram. Activated by phosphatidic acid By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei401 – 4011Proton donor By similarity
Metal bindingi405 – 4051Divalent metal cation 1 By similarity
Metal bindingi441 – 4411Divalent metal cation 1 By similarity
Metal bindingi442 – 4421Divalent metal cation 1 By similarity
Metal bindingi442 – 4421Divalent metal cation 2 By similarity
Binding sitei442 – 4421cAMP By similarity
Metal bindingi559 – 5591Divalent metal cation 1 By similarity
Sitei562 – 5621Binds AMP, but not cAMP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4055cAMP By similarity

GO - Molecular functioni

  1. 3',5'-cyclic-AMP phosphodiesterase activity Source: Ensembl
  2. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
  3. ATPase binding Source: BHF-UCL
  4. cAMP binding Source: Ensembl
  5. drug binding Source: Ensembl
  6. ion channel binding Source: BHF-UCL
  7. metal ion binding Source: UniProtKB-KW
  8. protein binding Source: IntAct

GO - Biological processi

  1. T cell receptor signaling pathway Source: Ensembl
  2. aging Source: MGI
  3. cAMP catabolic process Source: BHF-UCL
  4. cellular response to cAMP Source: Ensembl
  5. cellular response to epinephrine stimulus Source: BHF-UCL
  6. cellular response to lipopolysaccharide Source: MGI
  7. establishment of endothelial barrier Source: UniProtKB
  8. leukocyte migration Source: MGI
  9. multicellular organism growth Source: MGI
  10. negative regulation of heart contraction Source: BHF-UCL
  11. negative regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  12. negative regulation of relaxation of cardiac muscle Source: BHF-UCL
  13. neutrophil chemotaxis Source: MGI
  14. positive regulation of interferon-gamma production Source: Ensembl
  15. positive regulation of interleukin-2 production Source: Ensembl
  16. positive regulation of interleukin-5 production Source: Ensembl
  17. regulation of cardiac muscle cell contraction Source: BHF-UCL
  18. regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
  19. regulation of heart rate Source: BHF-UCL
  20. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  21. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  22. smooth muscle contraction Source: MGI
Complete GO annotation...

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 4D (EC:3.1.4.53)
Alternative name(s):
DPDE3
Gene namesi
Name:Pde4d
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:99555. Pde4d.

Subcellular locationi

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

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB-SubCell
  2. calcium channel complex Source: BHF-UCL
  3. cytosol Source: Ensembl
  4. microtubule organizing center Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 747747cAMP-specific 3',5'-cyclic phosphodiesterase 4D
PRO_0000198815Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei238 – 2381Phosphoserine By similarity
Modified residuei240 – 2401Phosphoserine By similarity
Cross-linki326 – 326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Post-translational modificationi

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

PaxDbiQ01063.
PRIDEiQ01063.

PTM databases

PhosphoSiteiQ01063.

Expressioni

Tissue specificityi

Expressed in brain (at protein level). Isoform 7 is detected in heart, brain, lung, kidney and testis.2 Publications

Inductioni

Up-regulated by cAMP and follicle-stimulating hormone By similarity.

Gene expression databases

ArrayExpressiQ01063.
BgeeiQ01063.
CleanExiMM_PDE4D.
GenevestigatoriQ01063.

Interactioni

Subunit structurei

Homodimer for the long isoforms. Isoforms with truncated N-termini are monomeric. Binds ARRB2. Interacts with PDE4DIP By similarity. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Interacts (via N-terminal region) with SHANK2 (via proline-rich region); the interaction is increased in a PKA-dependent manner.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Adrb1P349713EBI-7764239,EBI-7764182

Protein-protein interaction databases

BioGridi232023. 3 interactions.
DIPiDIP-29706N.
IntActiQ01063. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ01063.
SMRiQ01063. Positions 244-678.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG122287.
GeneTreeiENSGT00740000115148.
HOGENOMiHOG000236297.
HOVERGENiHBG108239.
KOiK01120.
OMAiQHEVEMP.
OrthoDBiEOG7HQNBC.
PhylomeDBiQ01063.

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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 7 (identifier: Q01063-1) [UniParc]FASTAAdd to Basket

Also known as: PDE4D7

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

MERDTCDVLS RSKSASEETL HSCNEEEDPF RGMEPYLVRR LSSRSIQLPP    50
LAFRQLEQAD LRSESENIPR PTSLPLKILP LIAVTSADSS GFDVDNGTSA 100
GRSPLDPMTS PGSGLILQAN FVHSQRRESF LYRSDSDYDL SPKSMSRNSS 150
IASDIHGDDL IVTPFAQVLA SLRTVRNNFA ALTNLQDRAP SKRSPMCNQP 200
SINKATITEE AYQKLASETL EELDWCLDQL ETLQTRHSVS EMASNKFKRM 250
LNRELTHLSE MSRSGNQVSE YISNTFLDKQ HEVEIPSPTQ KEKEKKKRPM 300
SQISGVKKLM HSSSLTNSCI PRFGVKTEQE DVLAKELEDV NKWGLHVFRI 350
AELSGNRPLT VIMHTIFQER DLLKTFKIPV DTLITYLMTL EDHYHADVAY 400
HNNIHAADVV QSTHVLLSTP ALEAVFTDLE ILAAIFASAI HDVDHPGVSN 450
QFLINTNSEL ALMYNDSSVL ENHHLAVGFK LLQEENCDIF QNLTKKQRQS 500
LRKMVIDIVL ATDMSKHMNL LADLKTMVET KKVTSSGVLL LDNYSDRIQV 550
LQNMVHCADL SNPTKPLQLY RQWTDRIMEE FFRQGDRERE RGMEISPMCD 600
KHNASVEKSQ VGFIDYIVHP LWETWADLVH PDAQDILDTL EDNREWYQST 650
IPQSPSPAPD DQEEGRQGQT EKFQFELTLE EDCESDTEKD SGSQVEEDTS 700
CSDSKTLCTQ DSESTEIPLD EQVEEEAVAE EESQPETCVP DDCCPDT 747
Length:747
Mass (Da):84,563
Last modified:January 4, 2005 - v2
Checksum:i68402163664B3676
GO
Isoform 9 (identifier: Q01063-2) [UniParc]FASTAAdd to Basket

Also known as: PDE4D9

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.
     70-91: RPTSLPLKILPLIAVTSADSSG → MSIIMKPRSRSTSSLRTTEAVC

Show »
Length:678
Mass (Da):76,817
Checksum:i51D44F3467C9B71A
GO
Isoform 3 (identifier: Q01063-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: Missing.
     164-208: PFAQVLASLR...QPSINKATIT → MKEQPSCAGT...TESSFPCLFA

Show »
Length:584
Mass (Da):66,394
Checksum:iCEDFA3A57387798E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 163163Missing in isoform 3.
VSP_012394Add
BLAST
Alternative sequencei1 – 6969Missing in isoform 9.
VSP_012395Add
BLAST
Alternative sequencei70 – 9122RPTSL…ADSSG → MSIIMKPRSRSTSSLRTTEA VC in isoform 9.
VSP_012396Add
BLAST
Alternative sequencei164 – 20845PFAQV…KATIT → MKEQPSCAGTGHPSMAGYGR MAPFELAGGPVKRLRTESSF PCLFA in isoform 3.
VSP_012397Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti403 – 4042NI → SR in AAA37368. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF536978 mRNA. Translation: AAN10120.1.
AY388962 mRNA. Translation: AAQ90406.1.
AK081466 mRNA. Translation: BAC38226.1.
CT025605, AC161585, AC163650 Genomic DNA. Translation: CAQ51656.1.
M94541 mRNA. Translation: AAA37368.1. Different termination.
CCDSiCCDS49359.1. [Q01063-1]
RefSeqiNP_035186.1. NM_011056.3. [Q01063-1]
XP_006517710.1. XM_006517647.1. [Q01063-2]
UniGeneiMm.434429.

Genome annotation databases

EnsembliENSMUST00000074103; ENSMUSP00000073742; ENSMUSG00000021699. [Q01063-2]
ENSMUST00000120664; ENSMUSP00000113024; ENSMUSG00000021699. [Q01063-3]
ENSMUST00000122041; ENSMUSP00000113488; ENSMUSG00000021699. [Q01063-1]
ENSMUST00000177907; ENSMUSP00000136485; ENSMUSG00000021699. [Q01063-1]
GeneIDi238871.
KEGGimmu:238871.
UCSCiuc007rvg.2. mouse. [Q01063-1]
uc007rvj.2. mouse. [Q01063-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF536978 mRNA. Translation: AAN10120.1 .
AY388962 mRNA. Translation: AAQ90406.1 .
AK081466 mRNA. Translation: BAC38226.1 .
CT025605 , AC161585 , AC163650 Genomic DNA. Translation: CAQ51656.1 .
M94541 mRNA. Translation: AAA37368.1 . Different termination.
CCDSi CCDS49359.1. [Q01063-1 ]
RefSeqi NP_035186.1. NM_011056.3. [Q01063-1 ]
XP_006517710.1. XM_006517647.1. [Q01063-2 ]
UniGenei Mm.434429.

3D structure databases

ProteinModelPortali Q01063.
SMRi Q01063. Positions 244-678.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 232023. 3 interactions.
DIPi DIP-29706N.
IntActi Q01063. 2 interactions.

Chemistry

BindingDBi Q01063.
ChEMBLi CHEMBL2111373.
DrugBanki DB00131. Adenosine monophosphate.

PTM databases

PhosphoSitei Q01063.

Proteomic databases

PaxDbi Q01063.
PRIDEi Q01063.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000074103 ; ENSMUSP00000073742 ; ENSMUSG00000021699 . [Q01063-2 ]
ENSMUST00000120664 ; ENSMUSP00000113024 ; ENSMUSG00000021699 . [Q01063-3 ]
ENSMUST00000122041 ; ENSMUSP00000113488 ; ENSMUSG00000021699 . [Q01063-1 ]
ENSMUST00000177907 ; ENSMUSP00000136485 ; ENSMUSG00000021699 . [Q01063-1 ]
GeneIDi 238871.
KEGGi mmu:238871.
UCSCi uc007rvg.2. mouse. [Q01063-1 ]
uc007rvj.2. mouse. [Q01063-2 ]

Organism-specific databases

CTDi 5144.
MGIi MGI:99555. Pde4d.

Phylogenomic databases

eggNOGi NOG122287.
GeneTreei ENSGT00740000115148.
HOGENOMi HOG000236297.
HOVERGENi HBG108239.
KOi K01120.
OMAi QHEVEMP.
OrthoDBi EOG7HQNBC.
PhylomeDBi Q01063.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi 383911.
PROi Q01063.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q01063.
Bgeei Q01063.
CleanExi MM_PDE4D.
Genevestigatori Q01063.

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. "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] (ISOFORM 7), TISSUE SPECIFICITY.
    Strain: BALB/c.
  2. Chai H., Gaweda B., De Vivo M., Wang D.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
  3. "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 3).
    Strain: C57BL/6J.
    Tissue: Head.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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 400-514.
  6. "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, TISSUE SPECIFICITY.
  7. "Remodeling of ryanodine receptor complex causes 'leaky' channels: a molecular mechanism for decreased exercise capacity."
    Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.
    Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH RYR1; FKBP1A; PKA AND PP1.

Entry informationi

Entry nameiPDE4D_MOUSE
AccessioniPrimary (citable) accession number: Q01063
Secondary accession number(s): B2KF58
, Q6TRH9, Q8C4Q7, Q8CG05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 4, 2005
Last modified: September 3, 2014
This is version 131 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi