PDE1_YEAST
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 03-AUG-2022, entry version 161.
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<1555::aid-yea43>3.0.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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 83.
DR STRING; 4932.YGL248W; -.
DR iPTMnet; P22434; -.
DR MaxQB; P22434; -.
DR PaxDb; P22434; -.
DR PRIDE; P22434; -.
DR EnsemblFungi; YGL248W_mRNA; YGL248W; YGL248W.
DR GeneID; 852644; -.
DR KEGG; sce:YGL248W; -.
DR SGD; S000003217; PDE1.
DR VEuPathDB; FungiDB:YGL248W; -.
DR eggNOG; ENOG502RFKK; Eukaryota.
DR HOGENOM; CLU_016658_2_1_1; -.
DR OMA; YYITHPH; -.
DR BioCyc; YEAST:YGL248W-MON; -.
DR BRENDA; 3.1.4.17; 984.
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; IBA:GO_Central.
DR GO; GO:0046069; P:cGMP catabolic process; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR024225; cAMP-PdiesteraseII_CS.
DR InterPro; IPR000396; Pdiesterase2.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR28283; PTHR28283; 2.
DR Pfam; PF02112; PDEase_II; 1.
DR PIRSF; PIRSF000962; Cyc_nuc_PDEase; 1.
DR PRINTS; PR00388; PDIESTERASE2.
DR SUPFAM; SSF56281; SSF56281; 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
