ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P06776


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PDE2_YEAST
Primary accession number P06776
Secondary accession number Q08836
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 73)
Name and origin of the protein
Protein name 3',5'-cyclic-nucleotide phosphodiesterase 2
Synonyms PDEase 2
EC 3.1.4.17
High-affinity cAMP phosphodiesterase
Gene name
Name: PDE2
Synonyms: SRA5
OrderedLocusNames: YOR360C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3025832 [NCBI, ExPASy, EBI, Israel, Japan]
Sass P., Field J., Nikawa J., Toda T., Wigler M.;
"Cloning and characterization of the high-affinity cAMP phosphodiesterase of Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 83:9303-9307(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M14563; AAA34846.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z75268; CAA99689.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S67272; S67272.
RefSeq NP_015005.1; -.
3D structure databases
ModBase P06776.
Protein-protein interaction databases
DIP DIP:4055N; -.
IntAct P06776; -.
Organism-specific databases
CYGD YOR360c; -.
SGD S000005887; PDE2.
Yeast-GFP YOR360C.
Gene expression databases
GermOnline YOR360C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0004115; Molecular function: 3',5'-cyclic-AMP phosphodiesterase activity (inferred from direct assay from SGD).
GO:0019933; Biological process: cAMP-mediated signaling (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR003607; Met-dep_phosphohydro_HD.
IPR002073; PDEase.
Graphical view of domain structure.
Pfam PF00233; PDEase_I; 1.
Pfam graphical view of domain structure.
PRINTS PR00387; PDIESTERASE1.
SMART SM00471; HDc; 1.
SMART graphical view of domain structure.
PROSITE PS00126; PDEASE_I; 1.
BLOCKS P06776.
ProtoNet P06776.
Proteomic databases
PeptideAtlas P06776; -.
Genome annotation databases
Ensembl YOR360C; Saccharomyces cerevisiae. [Contig view]
GeneID 854542; -.
GenomeReviews Y13140_GR; YOR360C.
KEGG sce:YOR360C; -.
NMPDR fig|4932.3.peg.6124; -.
Phylogenomic databases
HOGENOM P06776; -.
Other
LinkHub P06776; -.
NextBio 976949; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
cAMP; Complete proteome; Hydrolase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   526  526     3',5'-cyclic-nucleotide phosphodiesterase 2. PRO_0000198851
CONFLICT   82    82        R -> G (in Ref. 1; AAA34846). 
CONFLICT   349   350        QL -> LK (in Ref. 1; AAA34846). 
Sequence information
Length: 526 AA [This is the length of the unprocessed precursor] Molecular weight: 61000 Da [This is the MW of the unprocessed precursor] CRC64: 2058659DA87F286B [This is a checksum on the sequence]
        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 

P06776 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!