P06776 (PDE2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	526 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.4
Sequence similarities	Belongs to the cyclic nucleotide phosphodiesterase family.

Ontologies

Keywords
Ligand	Metal-binding cAMP
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cAMP-mediated signaling Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	3',5'-cyclic-AMP phosphodiesterase activity Inferred from direct assay Ref.1. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 526	526	3',5'-cyclic-nucleotide phosphodiesterase 2		PRO_0000198851
Sites
	Active site	265	1	Proton donor By similarity
	Metal binding	269	1	Divalent metal cation 1 By similarity
	Metal binding	302	1	Divalent metal cation 1 By similarity
	Metal binding	303	1	Divalent metal cation 1 By similarity
	Metal binding	303	1	Divalent metal cation 2 By similarity
	Metal binding	400	1	Divalent metal cation 1 By similarity
Experimental info
	Sequence conflict	82	1	R → G in AAA34846. Ref.1
	Sequence conflict	349 – 350	2	QL → LK in AAA34846. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P06776 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 2058659DA87F286B	FASTA	526	61,000
	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

References

	« Hide 'large scale' referencesShow '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: 3025832] [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: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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: 14562106] [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.
PIR	S67272.
RefSeq	NP_015005.1. NM_001183780.1.
3D structure databases
ProteinModelPortal	P06776.
SMR	P06776. Positions 202-525.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4055N.
IntAct	P06776. 3 interactions.
MINT	MINT-498200.
STRING	P06776.
Proteomic databases
PeptideAtlas	P06776.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR360C; YOR360C; YOR360C.
GeneID	854542.
KEGG	sce:YOR360C.
NMPDR	fig|4932.3.peg.6124.
Organism-specific databases
CYGD	YOR360c.
SGD	S000005887. PDE2.
Phylogenomic databases
eggNOG	fuNOG08278.
GeneTree	EFGT00050000003023.
HOGENOM	HBG202933.
OMA	ATDMALH.
OrthoDB	EOG4S7NZ3.
Gene expression databases
ArrayExpress	P06776.
Genevestigator	P06776.
GermOnline	YOR360C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003607. Metal-dep_PHydrolase_HD_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [Graphical view]
Gene3D	G3DSA:1.10.1300.10. PDEase_catalytic_dom. 1 hit.
KO	K01120.
Pfam	PF00233. PDEase_I. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	976949.

Entry information

Entry name

PDE2_YEAST

Accession

Primary (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:	December 14, 2011
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program