ID   PDE1_YEAST              Reviewed;         369 AA.
AC   P22434; D6VV87;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=3',5'-cyclic-nucleotide phosphodiesterase 1;
DE            Short=PDEase 1;
DE            EC=3.1.4.17;
DE   AltName: Full=3':5'-CNP;
DE   AltName: Full=Low-affinity cAMP phosphodiesterase;
GN   Name=PDE1; OrderedLocusNames=YGL248W; ORFNames=NRB369;
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].
RX   PubMed=2824992; DOI=10.1128/mcb.7.10.3629-3636.1987;
RA   Nikawa J., Sass P., Wigler M.;
RT   "Cloning and characterization of the low-affinity cyclic AMP
RT   phosphodiesterase gene of Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 7:3629-3636(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8972578;
RX   DOI=10.1002/(sici)1097-0061(199612)12:15%3c1555::aid-yea43%3e3.0.co;2-q;
RA   Coissac E., Maillier E., Robineau S., Netter P.;
RT   "Sequence of a 39,411 bp DNA fragment covering the left end of chromosome
RT   VII of Saccharomyces cerevisiae.";
RL   Yeast 12:1555-1562(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [4]
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   [5]
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).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Controls the level of cAMP in yeast cells, together with the
CC       high-affinity cAMP phosphodiesterase (PDE2).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-
CC         phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
CC   -!- MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-II
CC       family. {ECO:0000305}.
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DR   EMBL; M17781; AAA34896.1; -; Genomic_DNA.
DR   EMBL; X94357; CAA64139.1; -; Genomic_DNA.
DR   EMBL; Z72770; CAA96968.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07871.1; -; Genomic_DNA.
DR   PIR; S61613; ESBYPC.
DR   RefSeq; NP_011266.1; NM_001181114.1.
DR   PDB; 4OJV; X-ray; 1.31 A; A=1-369.
DR   PDB; 4OJX; X-ray; 1.31 A; A=1-369.
DR   PDBsum; 4OJV; -.
DR   PDBsum; 4OJX; -.
DR   AlphaFoldDB; P22434; -.
DR   SMR; P22434; -.
DR   BioGRID; 33031; 85.
DR   STRING; 4932.YGL248W; -.
DR   iPTMnet; P22434; -.
DR   MaxQB; P22434; -.
DR   PaxDb; 4932-YGL248W; -.
DR   PeptideAtlas; P22434; -.
DR   EnsemblFungi; YGL248W_mRNA; YGL248W; YGL248W.
DR   GeneID; 852644; -.
DR   KEGG; sce:YGL248W; -.
DR   AGR; SGD:S000003217; -.
DR   SGD; S000003217; PDE1.
DR   VEuPathDB; FungiDB:YGL248W; -.
DR   eggNOG; ENOG502RFKK; Eukaryota.
DR   HOGENOM; CLU_016658_2_1_1; -.
DR   InParanoid; P22434; -.
DR   OMA; YYITHPH; -.
DR   OrthoDB; 8010at2759; -.
DR   BioCyc; YEAST:YGL248W-MONOMER; -.
DR   BRENDA; 3.1.4.17; 984.
DR   BioGRID-ORCS; 852644; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P22434; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P22434; Protein.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IMP:SGD.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IBA:GO_Central.
DR   GO; GO:0006198; P:cAMP catabolic process; IEA:InterPro.
DR   GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IBA:GO_Central.
DR   CDD; cd07735; class_II_PDE_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR024225; cAMP-PdiesteraseII_CS.
DR   InterPro; IPR000396; Pdiesterase2.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR28283; 3',5'-CYCLIC-NUCLEOTIDE PHOSPHODIESTERASE 1; 1.
DR   PANTHER; PTHR28283:SF1; 3',5'-CYCLIC-NUCLEOTIDE PHOSPHODIESTERASE 1; 1.
DR   Pfam; PF02112; PDEase_II; 1.
DR   PIRSF; PIRSF000962; Cyc_nuc_PDEase; 1.
DR   PRINTS; PR00388; PDIESTERASE2.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS00607; PDEASE_II; 1.
PE   1: Evidence at protein level;
KW   3D-structure; cAMP; Hydrolase; Reference proteome.
FT   CHAIN           1..369
FT                   /note="3',5'-cyclic-nucleotide phosphodiesterase 1"
FT                   /id="PRO_0000206791"
FT   CONFLICT        94
FT                   /note="L -> F (in Ref. 1; AAA34896)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..10
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          14..16
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          18..29
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           44..53
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          64..66
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          69..75
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           76..79
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          86..90
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           92..96
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   TURN            97..100
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           102..107
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           110..119
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          121..125
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           135..140
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           141..145
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          153..157
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           159..168
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          170..175
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           178..180
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          186..190
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          200..215
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   TURN            217..219
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          222..232
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          238..242
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   TURN            250..252
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           256..267
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           270..272
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          273..279
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           288..291
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           297..311
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   TURN            314..319
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          321..325
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   HELIX           336..350
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          357..360
FT                   /evidence="ECO:0007829|PDB:4OJV"
FT   STRAND          365..368
FT                   /evidence="ECO:0007829|PDB:4OJV"
SQ   SEQUENCE   369 AA;  42016 MW;  47B752477E99BA88 CRC64;
     MVVFEITILG ANGGPTEYGT QCFILKPART EDPELIAVDG GAGMYQLREM LVQGRNENEG
     DDELVPSFYE HDREPIEFFI DSKLNIQKGL SKSLLQSLKR QGEHFESANT MKKTYEVFQG
     ITDYYITHPH LDHISGLVVN SPSIYEQENS KKKTIWGLPH TIDVLQKHVF NDLIWPDLTA
     ERSRKLKLKC LNPKEVQKCT IFPWDVIPFK VHHGIGVKTG APVYSTFYIF RDRKSKDCII
     VCGDVEQDRR ESEESLLEEF WSYVAENIPL VHLKGILVEC SCPLSSKPEQ LYGHLSPIYL
     INELSNLNTL YNSSKGLSGL NVIVTHVKST PAKRDPRLTI LEELRFLAEE RNLGDLRISI
     ALEGHTLFL
//