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Protein

3',5'-cyclic-nucleotide phosphodiesterase 1

Gene

PDE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Controls the level of cAMP in yeast cells, together with the high-affinity cAMP phosphodiesterase (PDE2).

Catalytic activityi

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.

GO - Molecular functioni

  • 3',5'-cyclic-AMP phosphodiesterase activity Source: SGD

GO - Biological processi

  • cAMP catabolic process Source: InterPro
  • cAMP-mediated signaling Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP

Enzyme and pathway databases

BioCyciYEAST:YGL248W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
3',5'-cyclic-nucleotide phosphodiesterase 1 (EC:3.1.4.17)
Short name:
PDEase 1
Alternative name(s):
3':5'-CNP
Low-affinity cAMP phosphodiesterase
Gene namesi
Name:PDE1
Ordered Locus Names:YGL248W
ORF Names:NRB369
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL248w.
EuPathDBiFungiDB:YGL248W.
SGDiS000003217. PDE1.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: GOC
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3693693',5'-cyclic-nucleotide phosphodiesterase 1PRO_0000206791Add
BLAST

Proteomic databases

MaxQBiP22434.
PaxDbiP22434.

Interactioni

Protein-protein interaction databases

BioGridi33031. 26 interactions.
STRINGi4932.YGL248W.

Structurei

Secondary structure

1
369
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Beta strandi14 – 163Combined sources
Beta strandi18 – 2912Combined sources
Beta strandi35 – 395Combined sources
Helixi44 – 5310Combined sources
Beta strandi64 – 663Combined sources
Beta strandi69 – 757Combined sources
Helixi76 – 794Combined sources
Beta strandi86 – 905Combined sources
Helixi92 – 965Combined sources
Turni97 – 1004Combined sources
Helixi102 – 1076Combined sources
Helixi110 – 11910Combined sources
Beta strandi121 – 1255Combined sources
Helixi131 – 1333Combined sources
Helixi135 – 1406Combined sources
Helixi141 – 1455Combined sources
Beta strandi153 – 1575Combined sources
Helixi159 – 16810Combined sources
Beta strandi170 – 1756Combined sources
Helixi178 – 1803Combined sources
Beta strandi186 – 1905Combined sources
Beta strandi200 – 21516Combined sources
Turni217 – 2193Combined sources
Beta strandi222 – 23211Combined sources
Turni233 – 2353Combined sources
Beta strandi238 – 2425Combined sources
Turni250 – 2523Combined sources
Helixi256 – 26712Combined sources
Helixi270 – 2723Combined sources
Beta strandi273 – 2797Combined sources
Helixi288 – 2914Combined sources
Helixi297 – 31115Combined sources
Turni314 – 3196Combined sources
Beta strandi321 – 3255Combined sources
Helixi336 – 35015Combined sources
Beta strandi357 – 3604Combined sources
Beta strandi365 – 3684Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OJVX-ray1.31A1-369[»]
4OJXX-ray1.31A1-369[»]
ProteinModelPortaliP22434.
SMRiP22434. Positions 1-369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5212.
HOGENOMiHOG000248334.
KOiK01120.
OMAiNVIVTHV.
OrthoDBiEOG7X6MB3.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR001279. Beta-lactamas-like.
IPR024225. cAMP-PdiesteraseII_CS.
IPR000396. Pdiesterase2.
[Graphical view]
PfamiPF02112. PDEase_II. 1 hit.
[Graphical view]
PIRSFiPIRSF000962. Cyc_nuc_PDEase. 1 hit.
PRINTSiPR00388. PDIESTERASE2.
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00607. PDEASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVFEITILG ANGGPTEYGT QCFILKPART EDPELIAVDG GAGMYQLREM
60 70 80 90 100
LVQGRNENEG DDELVPSFYE HDREPIEFFI DSKLNIQKGL SKSLLQSLKR
110 120 130 140 150
QGEHFESANT MKKTYEVFQG ITDYYITHPH LDHISGLVVN SPSIYEQENS
160 170 180 190 200
KKKTIWGLPH TIDVLQKHVF NDLIWPDLTA ERSRKLKLKC LNPKEVQKCT
210 220 230 240 250
IFPWDVIPFK VHHGIGVKTG APVYSTFYIF RDRKSKDCII VCGDVEQDRR
260 270 280 290 300
ESEESLLEEF WSYVAENIPL VHLKGILVEC SCPLSSKPEQ LYGHLSPIYL
310 320 330 340 350
INELSNLNTL YNSSKGLSGL NVIVTHVKST PAKRDPRLTI LEELRFLAEE
360
RNLGDLRISI ALEGHTLFL
Length:369
Mass (Da):42,016
Last modified:October 1, 1996 - v2
Checksum:i47B752477E99BA88
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941L → F in AAA34896 (PubMed:2824992).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17781 Genomic DNA. Translation: AAA34896.1.
X94357 Genomic DNA. Translation: CAA64139.1.
Z72770 Genomic DNA. Translation: CAA96968.1.
BK006941 Genomic DNA. Translation: DAA07871.1.
PIRiS61613. ESBYPC.
RefSeqiNP_011266.1. NM_001181114.1.

Genome annotation databases

EnsemblFungiiYGL248W; YGL248W; YGL248W.
GeneIDi852644.
KEGGisce:YGL248W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17781 Genomic DNA. Translation: AAA34896.1.
X94357 Genomic DNA. Translation: CAA64139.1.
Z72770 Genomic DNA. Translation: CAA96968.1.
BK006941 Genomic DNA. Translation: DAA07871.1.
PIRiS61613. ESBYPC.
RefSeqiNP_011266.1. NM_001181114.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OJVX-ray1.31A1-369[»]
4OJXX-ray1.31A1-369[»]
ProteinModelPortaliP22434.
SMRiP22434. Positions 1-369.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33031. 26 interactions.
STRINGi4932.YGL248W.

Proteomic databases

MaxQBiP22434.
PaxDbiP22434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL248W; YGL248W; YGL248W.
GeneIDi852644.
KEGGisce:YGL248W.

Organism-specific databases

CYGDiYGL248w.
EuPathDBiFungiDB:YGL248W.
SGDiS000003217. PDE1.

Phylogenomic databases

eggNOGiCOG5212.
HOGENOMiHOG000248334.
KOiK01120.
OMAiNVIVTHV.
OrthoDBiEOG7X6MB3.

Enzyme and pathway databases

BioCyciYEAST:YGL248W-MONOMER.

Miscellaneous databases

NextBioi971903.
PROiP22434.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR001279. Beta-lactamas-like.
IPR024225. cAMP-PdiesteraseII_CS.
IPR000396. Pdiesterase2.
[Graphical view]
PfamiPF02112. PDEase_II. 1 hit.
[Graphical view]
PIRSFiPIRSF000962. Cyc_nuc_PDEase. 1 hit.
PRINTSiPR00388. PDIESTERASE2.
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00607. PDEASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the low-affinity cyclic AMP phosphodiesterase gene of Saccharomyces cerevisiae."
    Nikawa J., Sass P., Wigler M.
    Mol. Cell. Biol. 7:3629-3636(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae."
    Coissac E., Maillier E., Robineau S., Netter P.
    Yeast 12:1555-1562(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDE1_YEAST
AccessioniPrimary (citable) accession number: P22434
Secondary accession number(s): D6VV87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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 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.