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P14270 (PDE4D_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase 4D

EC=3.1.4.53
Alternative name(s):
DPDE3
Gene names
Name:Pde4d
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length803 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.

Cofactor

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 regulation

Activated by phosphatidic acid By similarity. Inhibited by rolipram. Ref.8

Pathway

Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.

Subunit structure

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. Ref.14 Ref.15 Ref.17

Subcellular location

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. Ref.13 Ref.15 Ref.17

Tissue specificity

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. Ref.8 Ref.17

Induction

Up-regulated by cAMP and follicle-stimulating hormone. Ref.1 Ref.8

Post-translational modification

Isoform 1and 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.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily.

Biophysicochemical properties

Kinetic parameters:

Vmax=18 pmol/min/mg enzyme for cAMP (in the absence of follicle-stimulating hormone (FSH)) Ref.8

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

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   LigandcAMP
Metal-binding
   Molecular functionHydrolase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadrenergic receptor signaling pathway

Inferred from mutant phenotype PubMed 19801680. Source: BHF-UCL

adrenergic receptor signaling pathway involved in positive regulation of heart rate

Inferred by curator PubMed 19801680. Source: BHF-UCL

cAMP catabolic process

Inferred from direct assay PubMed 21724846. Source: UniProtKB

cellular protein complex assembly

Inferred from direct assay Ref.14. Source: RGD

establishment of endothelial barrier

Inferred from direct assay PubMed 20139324. Source: UniProtKB

lung development

Inferred from expression pattern PubMed 20652950. Source: RGD

memory

Inferred from mutant phenotype PubMed 21649644. Source: RGD

positive regulation of smooth muscle cell migration

Inferred from mutant phenotype PubMed 21776361. Source: RGD

positive regulation of smooth muscle cell proliferation

Inferred from mutant phenotype PubMed 21776361. Source: RGD

regulation of G-protein coupled receptor protein signaling pathway

Inferred from direct assay PubMed 12552097. Source: RGD

regulation of cardiac muscle cell contraction

Inferred from mutant phenotype PubMed 19801680. Source: BHF-UCL

regulation of protein kinase A signaling

Inferred from mutant phenotype PubMed 11296225. Source: RGD

regulation of receptor activity

Inferred from mutant phenotype PubMed 19801680. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.14. Source: RGD

apical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

centrosome

Inferred from direct assay Ref.14. Source: RGD

myofibril

Inferred from direct assay Ref.14. Source: RGD

   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from direct assay PubMed 12181425PubMed 18073242. Source: RGD

SH3 domain binding

Inferred from physical interaction PubMed 18073242. Source: RGD

beta-2 adrenergic receptor binding

Inferred from physical interaction PubMed 19801680. Source: BHF-UCL

cAMP binding

Inferred from mutant phenotype PubMed 11296225. Source: RGD

cyclic-nucleotide phosphodiesterase activity

Inferred from direct assay Ref.7. Source: RGD

enzyme binding

Inferred from physical interaction PubMed 22975349. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 23381222. Source: IntAct

protein domain specific binding

Inferred from physical interaction PubMed 11296225. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ADRB1P085882EBI-8333209,EBI-991009From a different organism.
Shank2Q9QX744EBI-9032440,EBI-397902

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: P14270-5)

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.
Isoform 33 (identifier: P14270-1)

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
Isoform 31 (identifier: P14270-2)

Also known as: PDE3.1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-264: MEAEGSSVPA...QPSINKATIT → MKEQPSCAGT...TESPFPCLFA
Isoform 32 (identifier: P14270-3)

Also known as: PDE3.2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-297: Missing.
Isoform 5 (identifier: P14270-8)

Also known as: PDE4D5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-147: MEAEGSSVPA...WPSSFQGLRR → MAQQTTSPDT...QRRFTVAHTC
Isoform 6 (identifier: P14270-7)

Also known as: PDE4D6;

The sequence of this isoform differs from the canonical sequence as follows:
     1-286: Missing.
     287-301: ETLQTRHSVSEMASN → MPEANYLLSVSWGYI
Isoform 7 (identifier: P14270-4)

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
Isoform 8 (identifier: P14270-9)

Also known as: PDE4D8;

The sequence of this isoform differs from the canonical sequence as follows:
     1-147: MEAEGSSVPA...WPSSFQGLRR → MAFVWDPLGVTVPGPSPRTRTRLRFSKSYS
Isoform 9 (identifier: P14270-6)

Also known as: PDE4D9;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 803803cAMP-specific 3',5'-cyclic phosphodiesterase 4D
PRO_0000198816

Regions

Nucleotide binding457 – 4615cAMP By similarity

Sites

Active site4571Proton donor By similarity
Metal binding4611Divalent metal cation 1 By similarity
Metal binding4971Divalent metal cation 1 By similarity
Metal binding4981Divalent metal cation 1 By similarity
Metal binding4981Divalent metal cation 2 By similarity
Metal binding6151Divalent metal cation 1 By similarity
Binding site4981cAMP By similarity
Site6181Binds AMP, but not cAMP By similarity

Amino acid modifications

Modified residue2941Phosphoserine By similarity
Modified residue2961Phosphoserine By similarity
Cross-link382Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 297297Missing in isoform 32.
VSP_004582
Alternative sequence1 – 286286Missing in isoform 6.
VSP_012404
Alternative sequence1 – 264264MEAEG…KATIT → MKEQPSCAGTGHPSMAGYGR MAPFELAGGPVKRLRTESPF PCLFA in isoform 31.
VSP_004581
Alternative sequence1 – 147147MEAEG…QGLRR → MAQQTTSPDTLTVPEVDNPH VPNPWLNEDLVKSLRENLLQ HEKSKTARKSVSPKLSPVIS PRNSPRLLRRMLLSSNIPKQ RRFTVAHTC in isoform 5.
VSP_053485
Alternative sequence1 – 147147MEAEG…QGLRR → MAFVWDPLGVTVPGPSPRTR TRLRFSKSYS in isoform 8.
VSP_053486
Alternative sequence1 – 131131Missing in isoform 33.
VSP_012398
Alternative sequence1 – 125125Missing in isoform 9.
VSP_012402
Alternative sequence1 – 5656Missing in isoform 7.
VSP_012400
Alternative sequence57 – 14791LPPPP…QGLRR → MERNTCDVLSRSKSASEETL HSCNDEEDPFRGMEPYLVRR LSSRSIQLPPLAFRQLEQTD LRSESENIPRPTSLPLKILP LIAVTSADSTG in isoform 7.
VSP_012401
Alternative sequence126 – 14722GHRPG…QGLRR → MSIIMKPRSRSTSSLRTTEA VC in isoform 9.
VSP_012403
Alternative sequence132 – 14716KKSRM…QGLRR → MMHVNTFPFRRHSWIC in isoform 33.
VSP_012399
Alternative sequence287 – 30115ETLQT…EMASN → MPEANYLLSVSWGYI in isoform 6.
VSP_012405

Experimental info

Sequence conflict2261A → N in AAA56857. Ref.12
Sequence conflict3571S → P in AAQ90405. Ref.9
Sequence conflict480 – 4867Missing in AAA18924. Ref.4
Sequence conflict480 – 4867Missing in AAA18925. Ref.4
Sequence conflict6411G → E in AAC26969. Ref.12
Sequence conflict7571C → Y in AAA56857. Ref.12

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 (PDE4D4) [UniParc].

Last modified January 4, 2005. Version 4.
Checksum: 13E28B257556496D

FASTA80390,552
        10         20         30         40         50         60 
MEAEGSSVPA RAGSHEGSDS SGGAALKAPK HLWRHEQHHQ YPLRQPQFRL LHPHHHLPPP 

        70         80         90        100        110        120 
PPPSPQPQLQ PPPPPPLPPP PPPPGATRGR YASSGASRVR HRGYSDTERY LYCRAMDRTS 

       130        140        150        160        170        180 
YAVETGHRPG LKKSRMSWPS SFQGLRRFDV DNGTSAGRSP LDPMTSPGSG LILQANFVHS 

       190        200        210        220        230        240 
QRRESFLYRS DSDYDLSPKS MSRNSSIASD IHGDDLIVTP FAQVLASLRT VRNNFAALTN 

       250        260        270        280        290        300 
LQDRAPSKRS PMCNQPSINK ATITEEAYQK LASETLEELD WCLDQLETLQ TRHSVSEMAS 

       310        320        330        340        350        360 
NKFKRMLNRE LTHLSEMSRS GNQVSEYISN TFLDKQHEVE IPSPTQKEKE KKKRPMSQIS 

       370        380        390        400        410        420 
GVKKLMHSSS LTNSCIPRFG VKTEQEDVLA KELEDVNKWG LHVFRIAELS GNRPLTVIMH 

       430        440        450        460        470        480 
TIFQERDLLK TFKIPVDTLI TYLMTLEDHY HADVAYHNNI HAADVVQSTH VLLSTPALEA 

       490        500        510        520        530        540 
VFTDLEILAA IFASAIHDVD HPGVSNQFLI NTNSELALMY NDSSVLENHH LAVGFKLLQE 

       550        560        570        580        590        600 
ENCDIFQNLT KKQRQSLRKM AIDIVLATDM SKHMNLLADL KTMVETKKVT SSGVLLLDNY 

       610        620        630        640        650        660 
SDRIQVLQNM VHCADLSNPT KPLQLYRQWT DRIMEEFFRQ GDRERERGME ISPMCDKHNA 

       670        680        690        700        710        720 
SVEKSQVGFI DYIVHPLWET WADLVHPDAQ DILDTLEDNR EWYQSTIPQS PSPAPDDQED 

       730        740        750        760        770        780 
GRQGQTEKFQ FELTLEEDGE SDTEKDSGSQ VEEDTSCSDS KTLCTQDSES TEIPLDEQVE 

       790        800 
EEAVAEEESQ PQTGVADDCC PDT 

« Hide

Isoform 33 (PDE4D3) (PDE3.3) [UniParc].

Checksum: 63CE38FA654A0BDD
Show »

FASTA67276,263
Isoform 31 (PDE3.1) [UniParc].

Checksum: 7C0DAEB75774F2F8
Show »

FASTA58466,243
Isoform 32 (PDE3.2) [UniParc].

Checksum: 7DCA5A564384FC34
Show »

FASTA50657,601
Isoform 5 (PDE4D5) [UniParc].

Checksum: 09DEADF7223F77BF
Show »

FASTA74584,335
Isoform 6 (PDE4D6) [UniParc].

Checksum: 251BF853D7CE6870
Show »

FASTA51758,923
Isoform 7 (PDE4D7) [UniParc].

Checksum: D63B9EF50AA3EFC9
Show »

FASTA74784,430
Isoform 8 (PDE4D8) [UniParc].

Checksum: D1F73EAEBDC6AA66
Show »

FASTA68677,611
Isoform 9 (PDE4D9) [UniParc].

Checksum: E3069D16ADEBEC6C
Show »

FASTA67876,656

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09455 mRNA. Translation: AAA20401.1.
U09457 mRNA. Translation: AAB81869.1.
U09456 mRNA. Translation: AAA20393.1.
U01280 expand/collapse EMBL AC list , U01278, U01282, U01283, U01284, U01285, U01286, U01287, U01279 Unassigned DNA. Translation: AAA18925.1.
U01280 expand/collapse EMBL AC list , 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.
PIRB53109.
I61259.
RefSeqNP_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]
UniGeneRn.163460.
Rn.95959.

3D structure databases

ProteinModelPortalP14270.
SMRP14270. Positions 376-736.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246765. 4 interactions.
IntActP14270. 2 interactions.
STRING10116.ENSRNOP00000015138.

Chemistry

BindingDBP14270.
ChEMBLCHEMBL2094267.

PTM databases

PhosphoSiteP14270.

Proteomic databases

PRIDEP14270.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015138; ENSRNOP00000015138; ENSRNOG00000042536. [P14270-6]
ENSRNOT00000066384; ENSRNOP00000063446; ENSRNOG00000042536. [P14270-9]
ENSRNOT00000067546; ENSRNOP00000062384; ENSRNOG00000042536. [P14270-7]
ENSRNOT00000073552; ENSRNOP00000067171; ENSRNOG00000042536. [P14270-8]
GeneID24627.
KEGGrno:24627.

Organism-specific databases

CTD5144.
RGD3281. Pde4d.

Phylogenomic databases

eggNOGNOG122287.
GeneTreeENSGT00740000115148.
HOVERGENHBG108239.
KOK01120.
OMAQHEVEMP.
PhylomeDBP14270.

Enzyme and pathway databases

UniPathwayUPA00762; UER00747.

Gene expression databases

GenevestigatorP14270.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio35580187.

Entry information

Entry namePDE4D_RAT
AccessionPrimary (citable) accession number: P14270
Secondary accession number(s): A1E347 expand/collapse secondary AC list , A1EC59, F1M1H7, O35470, Q6TRI0, Q8CG04, Q8CG06
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways