PDE2_YEAST
ID PDE2_YEAST Reviewed; 526 AA.
AC P06776; D6W355; Q08836;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=3',5'-cyclic-nucleotide phosphodiesterase 2 {ECO:0000305};
DE Short=PDEase 2;
DE EC=3.1.4.53 {ECO:0000269|PubMed:3025832};
DE AltName: Full=High-affinity cAMP phosphodiesterase {ECO:0000303|PubMed:3025832};
GN Name=PDE2 {ECO:0000303|PubMed:3025832}; Synonyms=SRA5;
GN OrderedLocusNames=YOR360C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3025832; DOI=10.1073/pnas.83.24.9303;
RA Sass P., Field J., Nikawa J., Toda T., Wigler M.;
RT "Cloning and characterization of the high-affinity cAMP phosphodiesterase
RT of Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9303-9307(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Controls the level of cAMP in yeast cells, together with the
CC low-affinity cAMP phosphodiesterase (PDE1).
CC {ECO:0000305|PubMed:3025832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; EC=3.1.4.53;
CC Evidence={ECO:0000269|PubMed:3025832};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000269|PubMed:3025832};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions. {ECO:0000250};
CC -!- SUBUNIT: Monomer.
CC -!- MISCELLANEOUS: Present with 6510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; M14563; AAA34846.1; -; Genomic_DNA.
DR EMBL; Z75268; CAA99689.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11121.1; -; Genomic_DNA.
DR PIR; S67272; S67272.
DR RefSeq; NP_015005.1; NM_001183780.1.
DR AlphaFoldDB; P06776; -.
DR SMR; P06776; -.
DR BioGRID; 34745; 634.
DR DIP; DIP-4055N; -.
DR IntAct; P06776; 3.
DR MINT; P06776; -.
DR STRING; 4932.YOR360C; -.
DR MaxQB; P06776; -.
DR PaxDb; P06776; -.
DR PRIDE; P06776; -.
DR EnsemblFungi; YOR360C_mRNA; YOR360C; YOR360C.
DR GeneID; 854542; -.
DR KEGG; sce:YOR360C; -.
DR SGD; S000005887; PDE2.
DR VEuPathDB; FungiDB:YOR360C; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_028903_0_0_1; -.
DR OMA; KFHNFRH; -.
DR BioCyc; YEAST:YOR360C-MON; -.
DR Reactome; R-SCE-2485179; Activation of the phototransduction cascade.
DR Reactome; R-SCE-4086398; Ca2+ pathway.
DR Reactome; R-SCE-418457; cGMP effects.
DR Reactome; R-SCE-418555; G alpha (s) signalling events.
DR PRO; PR:P06776; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P06776; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:SGD.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; -; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 1: Evidence at protein level;
KW cAMP; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..526
FT /note="3',5'-cyclic-nucleotide phosphodiesterase 2"
FT /id="PRO_0000198851"
FT DOMAIN 182..526
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT ACT_SITE 265
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 82
FT /note="R -> G (in Ref. 1; AAA34846)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..350
FT /note="QL -> LK (in Ref. 1; AAA34846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 61000 MW; 2058659DA87F286B CRC64;
MSTLFLIGIH EIEKSQTIVQ NEHYFDRVIE LQDLDSLMVA LYKDRVSPFP NVHNFETGVS
IVLYDPSKFQ LSVRQLDVLF KRFFPSFNIS AIDHTREENL QRLECVEREN SICRNRITRI
NHWMYHHHDD TPDGINKNSY GTVNGNSVPT QACEANIYTL LLHLNDSKAQ HLRKASVPRL
IRNIEFMSFL SDPIEKISQE GSHYWNILST WDFCALSLST QELIWCGFTL IKKLSKDAKV
LIADNKLLLL LFTLESSYHQ VNKFHNFRHA IDVMQATWRL CTYLLKDNPV QTLLLCMAAI
GHDVGHPGTN NQLLCNCESE VAQNFKNVSI LENFHRELFQ QLLSEHWPQL LSISKKKFDF
ISEAILATDM ALHSQYEDRL MHENPMKQIT LISLIIKAAD ISNVTRTLSI SARWAYLITL
EFNDCALLET FHKAHRPEQD CFGDSYKNVD SPKEDLESIQ NILVNVTDPD DIIKDHPHIP
NGQIFFINTF AEVFFNALSQ KFSGLKFLSD NVKINKEYWM KHKKPQ
