P12019 (PDE1_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A
Short name=PDEase A
EC=3.1.4.35
EC=3.1.4.53

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 names

Name:	pdsA
Synonyms:	pde1, pdeA
ORF Names:	DDB_G0285995

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5
Catalytic activity	Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.
Enzyme regulation	Inhibited by dithiotreitol (DTT). Ref.6
Subcellular location	Secreted › extracellular space. Cell surface Ref.6.
Induction	Up-regulated by Pseudomonas aeruginosa, PA14 strain infection but not by Pseudomonas aeruginosa, PA01 strain. Ref.6 Ref.8
Sequence similarities	Belongs to the cAMP phosphodiesterase class-II family.
Biophysicochemical properties	Kinetic parameters: cAMP/cGMP selectivity of 3. KM=0.8 µM for cAMP Ref.5 KM=1.8 µM for cGMP Vmax=700 pmol/min/mg enzyme with cAMP as substrate Vmax=490 pmol/min/mg enzyme with cGMP as substrate

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Nucleotide-binding Zinc cAMP cAMP-binding cGMP cGMP-binding
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cAMP catabolic process Inferred from mutant phenotype Ref.6. Source: dictyBase cGMP catabolic process Inferred from direct assay. Source: dictyBase
Cellular component	cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3',5'-cyclic-AMP phosphodiesterase activity Inferred from mutant phenotype Ref.6. Source: dictyBase 3',5'-cyclic-GMP phosphodiesterase activity Inferred from direct assay. Source: dictyBase cAMP binding Inferred from electronic annotation. Source: UniProtKB-KW cGMP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Propeptide	24 – 49	26	Potential		PRO_0000023352
	Chain	50 – 452	403	cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A		PRO_0000023353
Regions
	Compositional bias	28 – 35	8	Poly-Asp
Amino acid modifications
	Glycosylation	101	1	N-linked (GlcNAc...) Potential
	Glycosylation	141	1	N-linked (GlcNAc...) Potential
	Glycosylation	277	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	68 – 69	2	NW → LT in AAA33238. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P12019 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: A8F3C190D4603BD1	FASTA	452	51,093
	10 20 30 40 50 60 MALNKKLISL LLLIFIILNI VNSHQQEDCD DDDEDIGISA ERSERRSVKN SNDGSNFYNL 70 80 90 100 110 120 NDYYTPENWN YYSGSFATKD CRDASYITIP LGTTGGLDEG NLSSFLLTKK GSNLFIALDA 130 140 150 160 170 180 GTVWQGVRRL TTFKYFNTLF NITYPSWAVL PEQRTSWFLK NHVMSYFIGH SHLDHVGGLI 190 200 210 220 230 240 LVSPEDYLAK NWIDVQPPIN NGIMGLIRKL GFKPTDFTSS SILQKKTIMG LPSTINSIST 250 260 270 280 290 300 NLFNNQVWPN LPSFGRYQYF SLASGIEYPF TELVPYNATT MSLVANEFPF SVKVKPFELC 310 320 330 340 350 360 HDNLISTSFL FTDSISGEQI AFFSDTGVPS SVACDWEGKI YAVWKQIKID KLKAIYIETS 370 380 390 400 410 420 FPNNTPDSAM FGHLRPRDVM KLMDQLLVQS IQTSPPMTNL KHVKLIIEHI KPQVAEDPNG 430 440 450 WTTQRVIYQQ LKEANNNGVR IIIPNQGDPI CI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3023365] [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: 2779573] [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: 15875012] [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: 3020155] [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: 12429832] [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: 17040207] [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: 17644489] [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: 18590548] [Abstract] Cited for: INDUCTION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02628 mRNA. Translation: AAA68447.1. M23449 Genomic DNA. Translation: AAA63168.1. AAFI02000083 Genomic DNA. Translation: EAL64439.1. M15738 mRNA. Translation: AAA33238.1.
PIR	A25346. A32573.
RefSeq	XP_637948.1. XM_632856.1.
3D structure databases
ProteinModelPortal	P12019.
ModBase	Search...
Protein-protein interaction databases
STRING	P12019.
Proteomic databases
PRIDE	P12019.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0219974; DDB0219974; DDB_G0285995.
GeneID	8625393.
GenomeReviews	Gene locus pdsA in contig CM000153_GR.
KEGG	ddi:DDB_G0285995.
Organism-specific databases
dictyBase	DDB_G0285995. pdsA.
Phylogenomic databases
eggNOG	euNOG09520.
GeneTree	EPrGT00050000005437.
HOGENOM	HBG082131.
PhylomeDB	P12019.
ProtClustDB	CLSZ2429813.
Family and domain databases
InterPro	IPR024225. cAMP-PdiesteraseII_CS. IPR000396. Pdiesterase2. [Graphical view]
KO	K01120.
Pfam	PF02112. PDEase_II. 1 hit. [Graphical view]
PIRSF	PIRSF000962. Cyc_nuc_PDEase. 1 hit.
PRINTS	PR00388. PDIESTERASE2.
PROSITE	PS00607. PDEASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDE1_DICDI

Accession

Primary (citable) accession number: P12019
Secondary accession number(s): Q54ME9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	February 1, 1996
Last modified:	November 16, 2011
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)