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Protein

3',5'-cyclic-nucleotide phosphodiesterase 2

Gene

PDE2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Controls the level of cAMP in yeast cells, together with the low-affinity cAMP phosphodiesterase (PDE1).

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei265 – 2651Proton donorBy similarity
Metal bindingi269 – 2691Divalent metal cation 1By similarity
Metal bindingi302 – 3021Divalent metal cation 1By similarity
Metal bindingi303 – 3031Divalent metal cation 1By similarity
Metal bindingi303 – 3031Divalent metal cation 2By similarity
Metal bindingi400 – 4001Divalent metal cation 1By similarity

GO - Molecular functioni

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

GO - Biological processi

  • cAMP-mediated signaling Source: SGD
  • metabolic process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YOR360C-MONOMER.
ReactomeiREACT_345177. G alpha (s) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
3',5'-cyclic-nucleotide phosphodiesterase 2 (EC:3.1.4.17)
Short name:
PDEase 2
Alternative name(s):
High-affinity cAMP phosphodiesterase
Gene namesi
Name:PDE2
Synonyms:SRA5
Ordered Locus Names:YOR360C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOR360c.
EuPathDBiFungiDB:YOR360C.
SGDiS000005887. PDE2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5265263',5'-cyclic-nucleotide phosphodiesterase 2PRO_0000198851Add
BLAST

Proteomic databases

MaxQBiP06776.
PaxDbiP06776.
PeptideAtlasiP06776.

Expressioni

Gene expression databases

GenevestigatoriP06776.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi34745. 237 interactions.
DIPiDIP-4055N.
IntActiP06776. 3 interactions.
MINTiMINT-498200.
STRINGi4932.YOR360C.

Structurei

3D structure databases

ProteinModelPortaliP06776.
SMRiP06776. Positions 176-521.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG282089.
HOGENOMiHOG000066009.
KOiK01120.
OMAiLSISARW.
OrthoDBiEOG71RXW4.

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: Complete.

P06776-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLFLIGIH EIEKSQTIVQ NEHYFDRVIE LQDLDSLMVA LYKDRVSPFP
60 70 80 90 100
NVHNFETGVS IVLYDPSKFQ LSVRQLDVLF KRFFPSFNIS AIDHTREENL
110 120 130 140 150
QRLECVEREN SICRNRITRI NHWMYHHHDD TPDGINKNSY GTVNGNSVPT
160 170 180 190 200
QACEANIYTL LLHLNDSKAQ HLRKASVPRL IRNIEFMSFL SDPIEKISQE
210 220 230 240 250
GSHYWNILST WDFCALSLST QELIWCGFTL IKKLSKDAKV LIADNKLLLL
260 270 280 290 300
LFTLESSYHQ VNKFHNFRHA IDVMQATWRL CTYLLKDNPV QTLLLCMAAI
310 320 330 340 350
GHDVGHPGTN NQLLCNCESE VAQNFKNVSI LENFHRELFQ QLLSEHWPQL
360 370 380 390 400
LSISKKKFDF ISEAILATDM ALHSQYEDRL MHENPMKQIT LISLIIKAAD
410 420 430 440 450
ISNVTRTLSI SARWAYLITL EFNDCALLET FHKAHRPEQD CFGDSYKNVD
460 470 480 490 500
SPKEDLESIQ NILVNVTDPD DIIKDHPHIP NGQIFFINTF AEVFFNALSQ
510 520
KFSGLKFLSD NVKINKEYWM KHKKPQ
Length:526
Mass (Da):61,000
Last modified:November 1, 1997 - v2
Checksum:i2058659DA87F286B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821R → G in AAA34846 (PubMed:3025832).Curated
Sequence conflicti349 – 3502QL → LK in AAA34846 (PubMed:3025832).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14563 Genomic DNA. Translation: AAA34846.1.
Z75268 Genomic DNA. Translation: CAA99689.1.
BK006948 Genomic DNA. Translation: DAA11121.1.
PIRiS67272.
RefSeqiNP_015005.1. NM_001183780.1.

Genome annotation databases

EnsemblFungiiYOR360C; YOR360C; YOR360C.
GeneIDi854542.
KEGGisce:YOR360C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14563 Genomic DNA. Translation: AAA34846.1.
Z75268 Genomic DNA. Translation: CAA99689.1.
BK006948 Genomic DNA. Translation: DAA11121.1.
PIRiS67272.
RefSeqiNP_015005.1. NM_001183780.1.

3D structure databases

ProteinModelPortaliP06776.
SMRiP06776. Positions 176-521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34745. 237 interactions.
DIPiDIP-4055N.
IntActiP06776. 3 interactions.
MINTiMINT-498200.
STRINGi4932.YOR360C.

Proteomic databases

MaxQBiP06776.
PaxDbiP06776.
PeptideAtlasiP06776.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR360C; YOR360C; YOR360C.
GeneIDi854542.
KEGGisce:YOR360C.

Organism-specific databases

CYGDiYOR360c.
EuPathDBiFungiDB:YOR360C.
SGDiS000005887. PDE2.

Phylogenomic databases

eggNOGiNOG282089.
HOGENOMiHOG000066009.
KOiK01120.
OMAiLSISARW.
OrthoDBiEOG71RXW4.

Enzyme and pathway databases

BioCyciYEAST:YOR360C-MONOMER.
ReactomeiREACT_345177. G alpha (s) signalling events.

Miscellaneous databases

NextBioi976949.
PROiP06776.

Gene expression databases

GenevestigatoriP06776.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the high-affinity cAMP phosphodiesterase of Saccharomyces cerevisiae."
    Sass P., Field J., Nikawa J., Toda T., Wigler M.
    Proc. Natl. Acad. Sci. U.S.A. 83:9303-9307(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDE2_YEAST
AccessioniPrimary (citable) accession number: P06776
Secondary accession number(s): D6W355, Q08836
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1997
Last modified: April 29, 2015
This is version 125 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 6510 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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