PDE1_DICDI
ID PDE1_DICDI Reviewed; 452 AA.
AC P12019; Q54ME9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A;
DE Short=PDEase A;
DE EC=3.1.4.35;
DE EC=3.1.4.53;
DE AltName: Full=3',5'-cyclic-nucleotide phosphodiesterase;
DE Short=3':5'-CNP;
DE AltName: Full=Phosphodiesterase 1;
DE Short=DdPDE1;
DE AltName: Full=cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase 1;
DE Flags: Precursor;
GN Name=pdsA; Synonyms=pde1, pdeA; ORFNames=DDB_G0285995;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3023365; DOI=10.1016/s0021-9258(19)75960-2;
RA Lacombe M.-L., Podgorski G.J., Franke J., Kessin R.H.;
RT "Molecular cloning and developmental expression of the cyclic nucleotide
RT phosphodiesterase gene of Dictyostelium discoideum.";
RL J. Biol. Chem. 261:16811-16817(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2779573; DOI=10.1128/mcb.9.9.3938-3950.1989;
RA Podgorski G.J., Franke J., Faure M., Kessin R.H.;
RT "The cyclic nucleotide phosphodiesterase gene of Dictyostelium discoideum
RT utilizes alternate promoters and splicing for the synthesis of multiple
RT mRNAs.";
RL Mol. Cell. Biol. 9:3938-3950(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-69.
RX PubMed=3020155; DOI=10.1099/00221287-132-4-1043;
RA Podgorski G.J., Franke J., Kessin R.H.;
RT "Isolation of a cDNA encoding a portion of the cyclic nucleotide
RT phosphodiesterase of Dictyostelium discoideum.";
RL J. Gen. Microbiol. 132:1043-1050(1986).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12429832; DOI=10.1091/mbc.e02-05-0302;
RA Bosgraaf L., Russcher H., Snippe H., Bader S., Wind J.,
RA Van Haastert P.J.M.;
RT "Identification and characterization of two unusual cGMP-stimulated
RT phosphodiesterases in dictyostelium.";
RL Mol. Biol. Cell 13:3878-3889(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RX PubMed=17040207; DOI=10.1042/bj20061153;
RA Bader S., Kortholt A., Van Haastert P.J.M.;
RT "Seven Dictyostelium discoideum phosphodiesterases degrade three pools of
RT cAMP and cGMP.";
RL Biochem. J. 402:153-161(2007).
RN [7]
RP IDENTIFICATION.
RX PubMed=17644489; DOI=10.1016/j.jbi.2007.06.003;
RA Sacchi L., Larizza C., Magni P., Bellazzi R.;
RT "Precedence temporal networks to represent temporal relationships in gene
RT expression data.";
RL J. Biomed. Inform. 40:761-774(2007).
RN [8]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA Ivens A., Martinez J.L., Escalante R.;
RT "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT and specific effects from PAO1 and PA14 strains.";
RL BMC Microbiol. 8:109-109(2008).
CC -!- FUNCTION: Phosphodiesterase which displays a preference for cAMP over
CC cGMP. Involved in the degradation of extracellular cAMP. Maintains the
CC responsiveness of cells to the chemoattractant cAMP during the
CC aggregation phase of development. {ECO:0000269|PubMed:12429832}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC ChEBI:CHEBI:58115; EC=3.1.4.35;
CC -!- ACTIVITY REGULATION: Inhibited by dithiotreitol (DTT).
CC {ECO:0000269|PubMed:17040207}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for cAMP {ECO:0000269|PubMed:12429832};
CC KM=1.8 uM for cGMP {ECO:0000269|PubMed:12429832};
CC Vmax=700 pmol/min/mg enzyme with cAMP as substrate
CC {ECO:0000269|PubMed:12429832};
CC Vmax=490 pmol/min/mg enzyme with cGMP as substrate
CC {ECO:0000269|PubMed:12429832};
CC Note=cAMP/cGMP selectivity of 3.;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:17040207}. Cell surface
CC {ECO:0000269|PubMed:17040207}.
CC -!- INDUCTION: Up-regulated by Pseudomonas aeruginosa, PA14 strain
CC infection but not by Pseudomonas aeruginosa, PA01 strain.
CC {ECO:0000269|PubMed:18590548}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-II
CC family. {ECO:0000305}.
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DR EMBL; J02628; AAA68447.1; -; mRNA.
DR EMBL; M23449; AAA63168.1; -; Genomic_DNA.
DR EMBL; AAFI02000083; EAL64439.1; -; Genomic_DNA.
DR EMBL; M15738; AAA33238.1; -; mRNA.
DR PIR; A32573; A25346.
DR RefSeq; XP_637948.1; XM_632856.1.
DR AlphaFoldDB; P12019; -.
DR SMR; P12019; -.
DR STRING; 44689.DDB0219974; -.
DR PaxDb; P12019; -.
DR EnsemblProtists; EAL64439; EAL64439; DDB_G0285995.
DR GeneID; 8625393; -.
DR KEGG; ddi:DDB_G0285995; -.
DR dictyBase; DDB_G0285995; pdsA.
DR eggNOG; ENOG502RC36; Eukaryota.
DR HOGENOM; CLU_606124_0_0_1; -.
DR InParanoid; P12019; -.
DR OMA; CHDNLIS; -.
DR PhylomeDB; P12019; -.
DR SABIO-RK; P12019; -.
DR PRO; PR:P12019; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:dictyBase.
DR GO; GO:0005576; C:extracellular region; IDA:dictyBase.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:dictyBase.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IDA:dictyBase.
DR GO; GO:0030552; F:cAMP binding; IDA:dictyBase.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0006198; P:cAMP catabolic process; IDA:dictyBase.
DR GO; GO:0046069; P:cGMP catabolic process; IBA:GO_Central.
DR GO; GO:1900115; P:extracellular regulation of signal transduction; IMP:dictyBase.
DR GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0051591; P:response to cAMP; IDA:dictyBase.
DR GO; GO:1902168; P:response to catechin; IDA:dictyBase.
DR GO; GO:1903013; P:response to differentiation-inducing factor 1; IDA:dictyBase.
DR GO; GO:0072720; P:response to dithiothreitol; IDA:dictyBase.
DR GO; GO:0031153; P:slug development involved in sorocarp development; IMP:dictyBase.
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 cAMP; cAMP-binding; cGMP; cGMP-binding; Glycoprotein; Hydrolase;
KW Nucleotide-binding; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..49
FT /evidence="ECO:0000255"
FT /id="PRO_0000023352"
FT CHAIN 50..452
FT /note="cAMP/cGMP-dependent 3',5'-cAMP/cGMP
FT phosphodiesterase A"
FT /id="PRO_0000023353"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 68..69
FT /note="NW -> LT (in Ref. 4; AAA33238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 51093 MW; A8F3C190D4603BD1 CRC64;
MALNKKLISL LLLIFIILNI VNSHQQEDCD DDDEDIGISA ERSERRSVKN SNDGSNFYNL
NDYYTPENWN YYSGSFATKD CRDASYITIP LGTTGGLDEG NLSSFLLTKK GSNLFIALDA
GTVWQGVRRL TTFKYFNTLF NITYPSWAVL PEQRTSWFLK NHVMSYFIGH SHLDHVGGLI
LVSPEDYLAK NWIDVQPPIN NGIMGLIRKL GFKPTDFTSS SILQKKTIMG LPSTINSIST
NLFNNQVWPN LPSFGRYQYF SLASGIEYPF TELVPYNATT MSLVANEFPF SVKVKPFELC
HDNLISTSFL FTDSISGEQI AFFSDTGVPS SVACDWEGKI YAVWKQIKID KLKAIYIETS
FPNNTPDSAM FGHLRPRDVM KLMDQLLVQS IQTSPPMTNL KHVKLIIEHI KPQVAEDPNG
WTTQRVIYQQ LKEANNNGVR IIIPNQGDPI CI
