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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: -Experimental evidence at protein leveli

Functioni

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

Miscellaneous

Present with 6510 molecules/cell in log phase SD medium.1 Publication

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)DescriptionActionsGraphical viewLength
Active sitei265Proton donorBy similarity1
Metal bindingi269Divalent metal cation 1By similarity1
Metal bindingi302Divalent metal cation 1By similarity1
Metal bindingi303Divalent metal cation 1By similarity1
Metal bindingi303Divalent metal cation 2By similarity1
Metal bindingi400Divalent metal cation 1By similarity1

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

Keywordsi

Molecular functionHydrolase
LigandcAMP, Metal-binding

Enzyme and pathway databases

BioCyciYEAST:YOR360C-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
3',5'-cyclic-nucleotide phosphodiesterase 2 (EC:3.1.4.53)
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
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR360C
SGDiS000005887 PDE2

Subcellular locationi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001988511 – 5263',5'-cyclic-nucleotide phosphodiesterase 2Add BLAST526

Proteomic databases

MaxQBiP06776
PaxDbiP06776
PRIDEiP06776

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi34745, 559 interactors
DIPiDIP-4055N
IntActiP06776, 9 interactors
MINTiP06776
STRINGi4932.YOR360C

Structurei

3D structure databases

ProteinModelPortaliP06776
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini182 – 526PDEasePROSITE-ProRule annotationAdd BLAST345

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000066009
KOiK01120
OMAiGQIFFIN
OrthoDBiEOG092C0DHA

Family and domain databases

CDDicd00077 HDc, 1 hit
Gene3Di1.10.1300.10, 1 hit
InterProiView protein in InterPro
IPR003607 HD/PDEase_dom
IPR023088 PDEase
IPR002073 PDEase_catalytic_dom
IPR036971 PDEase_catalytic_dom_sf
IPR023174 PDEase_CS
PfamiView protein in Pfam
PF00233 PDEase_I, 1 hit
PRINTSiPR00387 PDIESTERASE1
SMARTiView protein in SMART
SM00471 HDc, 1 hit
PROSITEiView protein in PROSITE
PS00126 PDEASE_I_1, 1 hit
PS51845 PDEASE_I_2, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti82R → G in AAA34846 (PubMed:3025832).Curated1
Sequence conflicti349 – 350QL → LK in AAA34846 (PubMed:3025832).Curated2

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

Similar proteinsi

Entry informationi

Entry nameiPDE2_YEAST
AccessioniPrimary (citable) accession number: P06776
Secondary accession number(s): D6W355, Q08836
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 153 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health