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P06776 (PDE2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3',5'-cyclic-nucleotide phosphodiesterase 2

Short name=PDEase 2
EC=3.1.4.17
Alternative name(s):
High-affinity cAMP phosphodiesterase
Gene names
Name:PDE2
Synonyms:SRA5
Ordered Locus Names:YOR360C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

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.

Subunit structure

Monomer.

Miscellaneous

Present with 6510 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5265263',5'-cyclic-nucleotide phosphodiesterase 2
PRO_0000198851

Sites

Active site2651Proton donor By similarity
Metal binding2691Divalent metal cation 1 By similarity
Metal binding3021Divalent metal cation 1 By similarity
Metal binding3031Divalent metal cation 1 By similarity
Metal binding3031Divalent metal cation 2 By similarity
Metal binding4001Divalent metal cation 1 By similarity

Experimental info

Sequence conflict821R → G in AAA34846. Ref.1
Sequence conflict349 – 3502QL → LK in AAA34846. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P06776 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 2058659DA87F286B

FASTA52661,000
        10         20         30         40         50         60 
MSTLFLIGIH EIEKSQTIVQ NEHYFDRVIE LQDLDSLMVA LYKDRVSPFP NVHNFETGVS 

        70         80         90        100        110        120 
IVLYDPSKFQ LSVRQLDVLF KRFFPSFNIS AIDHTREENL QRLECVEREN SICRNRITRI 

       130        140        150        160        170        180 
NHWMYHHHDD TPDGINKNSY GTVNGNSVPT QACEANIYTL LLHLNDSKAQ HLRKASVPRL 

       190        200        210        220        230        240 
IRNIEFMSFL SDPIEKISQE GSHYWNILST WDFCALSLST QELIWCGFTL IKKLSKDAKV 

       250        260        270        280        290        300 
LIADNKLLLL LFTLESSYHQ VNKFHNFRHA IDVMQATWRL CTYLLKDNPV QTLLLCMAAI 

       310        320        330        340        350        360 
GHDVGHPGTN NQLLCNCESE VAQNFKNVSI LENFHRELFQ QLLSEHWPQL LSISKKKFDF 

       370        380        390        400        410        420 
ISEAILATDM ALHSQYEDRL MHENPMKQIT LISLIIKAAD ISNVTRTLSI SARWAYLITL 

       430        440        450        460        470        480 
EFNDCALLET FHKAHRPEQD CFGDSYKNVD SPKEDLESIQ NILVNVTDPD DIIKDHPHIP 

       490        500        510        520 
NGQIFFINTF AEVFFNALSQ KFSGLKFLSD NVKINKEYWM KHKKPQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14563 Genomic DNA. Translation: AAA34846.1.
Z75268 Genomic DNA. Translation: CAA99689.1.
BK006948 Genomic DNA. Translation: DAA11121.1.
PIRS67272.
RefSeqNP_015005.1. NM_001183780.1.

3D structure databases

ProteinModelPortalP06776.
SMRP06776. Positions 176-521.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34745. 233 interactions.
DIPDIP-4055N.
IntActP06776. 3 interactions.
MINTMINT-498200.
STRING4932.YOR360C.

Proteomic databases

PaxDbP06776.
PeptideAtlasP06776.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR360C; YOR360C; YOR360C.
GeneID854542.
KEGGsce:YOR360C.

Organism-specific databases

CYGDYOR360c.
SGDS000005887. PDE2.

Phylogenomic databases

eggNOGNOG282089.
HOGENOMHOG000066009.
KOK01120.
OMAKFHNFRH.
OrthoDBEOG71RXW4.

Enzyme and pathway databases

BioCycYEAST:YOR360C-MONOMER.

Gene expression databases

GenevestigatorP06776.

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

NextBio976949.

Entry information

Entry namePDE2_YEAST
AccessionPrimary (citable) accession number: P06776
Secondary accession number(s): D6W355, Q08836
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families