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Protein

cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase 7

Gene

pde7

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

Functioni

Phosphodiesterase with dual cAMP/cGMP specificity. However, displays a preference for cAMP over cGMP. Seems to regulate cAMP/cGMP concentration especially during cell aggregation.

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

  1. KM=12.5 µM for cAMP1 Publication
  2. KM=36 µM for cGMP1 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
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase 7 (EC:3.1.4.35, EC:3.1.4.53)
Alternative name(s):
Phosphodiesterase 7
Short name:
ddPDE7
Gene namesi
Name:pde7
ORF Names:DDB_G0289145
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195: Chromosome 5, UP000002195: Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0289145. pde7.

Subcellular locationi

Secretedextracellular space 1 Publication. Cell surface 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 425408cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase 7PRO_0000363968Add
BLAST

Expressioni

Inductioni

Down-regulated by growth on bacteria.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi44689.DDBDRAFT_0188281.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5212.
InParanoidiQ54HY0.
OMAiDIMKLMD.
PhylomeDBiQ54HY0.

Family and domain databases

Gene3Di3.60.15.10. 3 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.

Q54HY0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKYLILILIF FIEINNGSRL INSGNLFSEL KDYYIPENLN YYSGGYSEQH
60 70 80 90 100
CKDSSYITIP LGVTGGLDEG SLSSFLLTKK GSSLFIGLDA GTVWQGVRRL
110 120 130 140 150
TMLQDFNSVF NITYPPWATL PEQRATWFIK NHIQGYLIGH SHLDHVGGLI
160 170 180 190 200
VESAEDQLSP KKNELEVSQP EIYRGCIEMI HKMGYVSDFP NITSIPDQKK
210 220 230 240 250
PIIGINETLY SMATDLFNGF VWPSLPNYGR YSYYYLGNGN QYSFKDLTPY
260 270 280 290 300
ANKYVTKVQN DFPFNHLVKS FEICHDSLTS TAFILTDSQS GEQIVFFSDT
310 320 330 340 350
GISTTKCDWE FKILQVWRNI KIDKLKAVYI ESSFTNEVAD NVLFGHLRPK
360 370 380 390 400
DIMKLMDSLL ENSIQTSPPK TNLKHVKLII EHIKPQVGMN QYYLTSQRMV
410 420
YQQLQEINNH GVKVIIPNQG VPICL
Length:425
Mass (Da):48,505
Last modified:May 24, 2005 - v1
Checksum:iADE7F8A5D17D3713
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000130 Genomic DNA. Translation: EAL62880.1.
RefSeqiXP_636383.1. XM_631291.1.

Genome annotation databases

EnsemblProtistsiDDB0238626; DDB0238626; DDB_G0289145.
GeneIDi8626984.
KEGGiddi:DDB_G0289145.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000130 Genomic DNA. Translation: EAL62880.1.
RefSeqiXP_636383.1. XM_631291.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDBDRAFT_0188281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0238626; DDB0238626; DDB_G0289145.
GeneIDi8626984.
KEGGiddi:DDB_G0289145.

Organism-specific databases

dictyBaseiDDB_G0289145. pde7.

Phylogenomic databases

eggNOGiCOG5212.
InParanoidiQ54HY0.
OMAiDIMKLMD.
PhylomeDBiQ54HY0.

Family and domain databases

Gene3Di3.60.15.10. 3 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. "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.
  2. "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: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION.
  3. "Genome-wide transcriptional changes induced by phagocytosis or growth on bacteria in Dictyostelium."
    Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B., Skelton J., Ivens A., Bozzaro S.
    BMC Genomics 9:291-291(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDE7_DICDI
AccessioniPrimary (citable) accession number: Q54HY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: May 24, 2005
Last modified: January 7, 2015
This is version 51 of the entry and version 1 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.