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Protein

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

Gene

Pde4c

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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

a divalent metal cationBy similarityNote: 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.

Pathwayi: 3',5'-cyclic AMP degradation

This protein is involved in step 1 of the subpathway that synthesizes AMP from 3',5'-cyclic AMP.
Proteins known to be involved in this subpathway in this organism are:
  1. High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (Pde7a), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (Pde4d), cAMP-specific 3',5'-cyclic phosphodiesterase 4B (Pde4b), cAMP-specific 3',5'-cyclic phosphodiesterase 4A (Pde4a), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (Pde10a), cAMP-specific 3',5'-cyclic phosphodiesterase 4C (Pde4c)
This subpathway is part of the pathway 3',5'-cyclic AMP degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from 3',5'-cyclic AMP, the pathway 3',5'-cyclic AMP degradation and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei254Proton donorBy similarity1
Metal bindingi258Divalent metal cation 1By similarity1
Metal bindingi294Divalent metal cation 1By similarity1
Metal bindingi295Divalent metal cation 1By similarity1
Metal bindingi295Divalent metal cation 2By similarity1
Binding sitei295cAMPBy similarity1
Metal bindingi412Divalent metal cation 1By similarity1
Binding sitei412cAMPBy similarity1
Sitei415Binds AMP, but not cAMPBy similarity1
Binding sitei463cAMPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi254 – 258cAMPBy similarity5

GO - Molecular functioni

  • 3',5'-cyclic-AMP phosphodiesterase activity Source: RGD
  • drug binding Source: RGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cAMP catabolic process Source: UniProtKB
  • negative regulation of insulin secretion Source: RGD
  • signal transduction Source: InterPro
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 4C (EC:3.1.4.53)
Alternative name(s):
DPDE1
Gene namesi
Name:Pde4c
Synonyms:Dpde1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi727918. Pde4c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2094267.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000198813‹1 – 536cAMP-specific 3',5'-cyclic phosphodiesterase 4CAdd BLAST›536

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei507PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP14644.
PRIDEiP14644.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026457.

Structurei

3D structure databases

ProteinModelPortaliP14644.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi524 – 534Poly-GluAdd BLAST11

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
HOGENOMiHOG000236297.
HOVERGENiHBG108239.
InParanoidiP14644.
PhylomeDBiP14644.

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]

Sequencei

Sequence statusi: Fragment.

P14644-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
NSSRTSSAAS DLHGEDMIVT PFAQVLASLR TVRSNVAALA HGAGSATRQA
60 70 80 90 100
LLGTPPQSSQ QAAPAEESGL QLAQETLEEL DWCLEQLETL QTRRSVGEMA
110 120 130 140 150
SNKFKRMLNR ELTHLSETSR SGNQVSEYIS QTFLDQQAEV ELPAPPTEDH
160 170 180 190 200
PWPMAQITGL RKSCHTSLPT AAIPRFGVQT DQEEQLAKEL EDTNKWGLDV
210 220 230 240 250
FKVAELSGNR PLTAVIFRVL QERDLLKTFQ IPADTLLRYL LTLEGHYHSN
260 270 280 290 300
VAYHNSIHAA DVVQSAHVLL GTPALEAVFT DLEVLAAIFA CAIHDVDHPG
310 320 330 340 350
VSNQFLINTN SELALMYNDS SVLENHHLAV GFKLLQGENC DIFQNLSTKQ
360 370 380 390 400
KLSLRRMVID MVLATDMSKH MSLLADLKTM VETKKVTSLG VLLLDNYSDR
410 420 430 440 450
IQVLQSLVHC ADLSNPAKPL PLYRQWTERI MAEFFQQGDR ERESGLDISP
460 470 480 490 500
MCDKHTASVE KSQVGFIDYI AHPLWETWAD LVHPDAQELL DTLEDNREWY
510 520 530
QSRVPCSPPH AIGPDRFKFE LTLEETEEEE EEDERH
Length:536
Mass (Da):60,064
Last modified:October 1, 1996 - v2
Checksum:i87D12BE2C46642F3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti218R → S in AAA41847 (PubMed:2546153).Curated1
Sequence conflicti507S → N in AAA41847 (PubMed:2546153).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27061 mRNA. Translation: AAA56858.1.
M25347 mRNA. Translation: AAA41847.1.
PIRiI67945.
UniGeneiRn.214181.
Rn.92465.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27061 mRNA. Translation: AAA56858.1.
M25347 mRNA. Translation: AAA41847.1.
PIRiI67945.
UniGeneiRn.214181.
Rn.92465.

3D structure databases

ProteinModelPortaliP14644.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000026457.

Chemistry databases

ChEMBLiCHEMBL2094267.

Proteomic databases

PaxDbiP14644.
PRIDEiP14644.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi727918. Pde4c.

Phylogenomic databases

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
HOGENOMiHOG000236297.
HOVERGENiHBG108239.
InParanoidiP14644.
PhylomeDBiP14644.

Enzyme and pathway databases

UniPathwayiUPA00762; UER00747.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiPDE4C_RAT
AccessioniPrimary (citable) accession number: P14644
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 109 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.