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Protein

cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A

Gene

pdsA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Phosphodiesterase which displays a preference for cAMP over cGMP. Involved in the degradation of extracellular cAMP. Maintains the responsiveness of cells to the chemoattractant cAMP during the aggregation phase of development.1 Publication

Catalytic activityi

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.
Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.

Enzyme regulationi

Inhibited by dithiotreitol (DTT).1 Publication

Kineticsi

cAMP/cGMP selectivity of 3.

  1. KM=0.8 µM for cAMP1 Publication
  2. KM=1.8 µM for cGMP1 Publication

Vmax=700 pmol/min/mg enzyme with cAMP as substrate1 Publication

Vmax=490 pmol/min/mg enzyme with cGMP as substrate1 Publication

GO - Molecular functioni

  1. 3',5'-cyclic-AMP phosphodiesterase activity Source: dictyBase
  2. 3',5'-cyclic-GMP phosphodiesterase activity Source: dictyBase
  3. cAMP binding Source: UniProtKB-KW
  4. cGMP binding Source: UniProtKB-KW

GO - Biological processi

  1. cAMP catabolic process Source: dictyBase
  2. cGMP catabolic process Source: dictyBase
  3. response to catechin Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, cAMP-binding, cGMP, cGMP-binding, Nucleotide-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (EC:3.1.4.35, EC:3.1.4.53)
Short name:
PDEase A
Alternative name(s):
3',5'-cyclic-nucleotide phosphodiesterase
Short name:
3':5'-CNP
Phosphodiesterase 1
Short name:
DdPDE1
cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase 1
Gene namesi
Name:pdsA
Synonyms:pde1, pdeA
ORF Names:DDB_G0285995
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195 Componentsi: Chromosome 4, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0285995. pdsA.

Subcellular locationi

  1. Secretedextracellular space 1 Publication
  2. Cell surface 1 Publication

GO - Cellular componenti

  1. cell surface Source: UniProtKB-SubCell
  2. extracellular region Source: dictyBase
  3. extracellular space Source: UniProtKB-SubCell
  4. plasma membrane Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Propeptidei24 – 4926Sequence AnalysisPRO_0000023352Add
BLAST
Chaini50 – 452403cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase APRO_0000023353Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP12019.

Expressioni

Inductioni

Up-regulated by Pseudomonas aeruginosa, PA14 strain infection but not by Pseudomonas aeruginosa, PA01 strain.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB_0219974.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 358Poly-Asp

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5212.
InParanoidiP12019.
KOiK01120.
OMAiTEYALYF.
PhylomeDBiP12019.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR001279. Beta-lactamas-like.
IPR024225. cAMP-PdiesteraseII_CS.
IPR000396. Pdiesterase2.
[Graphical view]
PfamiPF02112. PDEase_II. 1 hit.
[Graphical view]
PIRSFiPIRSF000962. Cyc_nuc_PDEase. 1 hit.
PRINTSiPR00388. PDIESTERASE2.
SUPFAMiSSF56281. SSF56281. 2 hits.
PROSITEiPS00607. PDEASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12019-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALNKKLISL LLLIFIILNI VNSHQQEDCD DDDEDIGISA ERSERRSVKN
60 70 80 90 100
SNDGSNFYNL NDYYTPENWN YYSGSFATKD CRDASYITIP LGTTGGLDEG
110 120 130 140 150
NLSSFLLTKK GSNLFIALDA GTVWQGVRRL TTFKYFNTLF NITYPSWAVL
160 170 180 190 200
PEQRTSWFLK NHVMSYFIGH SHLDHVGGLI LVSPEDYLAK NWIDVQPPIN
210 220 230 240 250
NGIMGLIRKL GFKPTDFTSS SILQKKTIMG LPSTINSIST NLFNNQVWPN
260 270 280 290 300
LPSFGRYQYF SLASGIEYPF TELVPYNATT MSLVANEFPF SVKVKPFELC
310 320 330 340 350
HDNLISTSFL FTDSISGEQI AFFSDTGVPS SVACDWEGKI YAVWKQIKID
360 370 380 390 400
KLKAIYIETS FPNNTPDSAM FGHLRPRDVM KLMDQLLVQS IQTSPPMTNL
410 420 430 440 450
KHVKLIIEHI KPQVAEDPNG WTTQRVIYQQ LKEANNNGVR IIIPNQGDPI

CI
Length:452
Mass (Da):51,093
Last modified:February 1, 1996 - v2
Checksum:iA8F3C190D4603BD1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 692NW → LT in AAA33238 (PubMed:3020155).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02628 mRNA. Translation: AAA68447.1.
M23449 Genomic DNA. Translation: AAA63168.1.
AAFI02000083 Genomic DNA. Translation: EAL64439.1.
M15738 mRNA. Translation: AAA33238.1.
PIRiA32573. A25346.
RefSeqiXP_637948.1. XM_632856.1.

Genome annotation databases

EnsemblProtistsiDDB0219974; DDB0219974; DDB_G0285995.
GeneIDi8625393.
KEGGiddi:DDB_G0285995.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02628 mRNA. Translation: AAA68447.1.
M23449 Genomic DNA. Translation: AAA63168.1.
AAFI02000083 Genomic DNA. Translation: EAL64439.1.
M15738 mRNA. Translation: AAA33238.1.
PIRiA32573. A25346.
RefSeqiXP_637948.1. XM_632856.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB_0219974.

Proteomic databases

PRIDEiP12019.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0219974; DDB0219974; DDB_G0285995.
GeneIDi8625393.
KEGGiddi:DDB_G0285995.

Organism-specific databases

dictyBaseiDDB_G0285995. pdsA.

Phylogenomic databases

eggNOGiCOG5212.
InParanoidiP12019.
KOiK01120.
OMAiTEYALYF.
PhylomeDBiP12019.

Miscellaneous databases

PROiP12019.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR001279. Beta-lactamas-like.
IPR024225. cAMP-PdiesteraseII_CS.
IPR000396. Pdiesterase2.
[Graphical view]
PfamiPF02112. PDEase_II. 1 hit.
[Graphical view]
PIRSFiPIRSF000962. Cyc_nuc_PDEase. 1 hit.
PRINTSiPR00388. PDIESTERASE2.
SUPFAMiSSF56281. SSF56281. 2 hits.
PROSITEiPS00607. PDEASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and developmental expression of the cyclic nucleotide phosphodiesterase gene of Dictyostelium discoideum."
    Lacombe M.-L., Podgorski G.J., Franke J., Kessin R.H.
    J. Biol. Chem. 261:16811-16817(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The cyclic nucleotide phosphodiesterase gene of Dictyostelium discoideum utilizes alternate promoters and splicing for the synthesis of multiple mRNAs."
    Podgorski G.J., Franke J., Faure M., Kessin R.H.
    Mol. Cell. Biol. 9:3938-3950(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  4. "Isolation of a cDNA encoding a portion of the cyclic nucleotide phosphodiesterase of Dictyostelium discoideum."
    Podgorski G.J., Franke J., Kessin R.H.
    J. Gen. Microbiol. 132:1043-1050(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-69.
  5. "Identification and characterization of two unusual cGMP-stimulated phoshodiesterases in dictyostelium."
    Bosgraaf L., Russcher H., Snippe H., Bader S., Wind J., Van Haastert P.J.M.
    Mol. Biol. Cell 13:3878-3889(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  6. "Seven Dictyostelium discoideum phosphodiesterases degrade three pools of cAMP and cGMP."
    Bader S., Kortholt A., Van Haastert P.J.M.
    Biochem. J. 402:153-161(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ENZYME REGULATION.
  7. "Precedence temporal networks to represent temporal relationships in gene expression data."
    Sacchi L., Larizza C., Magni P., Bellazzi R.
    J. Biomed. Inform. 40:761-774(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  8. "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common and specific effects from PAO1 and PA14 strains."
    Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R., Ivens A., Martinez J.L., Escalante R.
    BMC Microbiol. 8:109-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDE1_DICDI
AccessioniPrimary (citable) accession number: P12019
Secondary accession number(s): Q54ME9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1996
Last modified: April 29, 2015
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.