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Q1KKS3 (PDE11_TAKRU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A

EC=3.1.4.17
EC=3.1.4.35
Alternative name(s):
cAMP and cGMP phosphodiesterase 11A
Gene names
Name:pde11a
OrganismTakifugu rubripes (Japanese pufferfish) (Fugu rubripes) [Reference proteome]
Taxonomic identifier31033 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataPercomorphariaTetraodontiformesTetradontoideaTetraodontidaeTakifugu

Protein attributes

Sequence length903 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively By similarity.

Catalytic activity

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

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

Cofactor

Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions By similarity.

Enzyme regulation

Inhibited by 3-isobutyl-1-methylxanthine (IBMX), zaprinast and dipyridamole. cGMP acts as an allosteric activator By similarity.

Subcellular location

Cytoplasmcytosol By similarity.

Domain

The tandem GAF domains bind cGMP, and regulate enzyme activity. The binding of cGMP stimulates enzyme activity By similarity.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Contains 2 GAF domains.

Ontologies

Keywords
   Cellular componentCytoplasm
   DomainRepeat
   LigandcAMP
cGMP
Metal-binding
   Molecular functionHydrolase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processsignal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3',5'-cyclic-GMP phosphodiesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 903903Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
PRO_0000247043

Regions

Domain175 – 324150GAF 1
Domain356 – 512157GAF 2
Region594 – 859266Catalytic By similarity

Sites

Active site6181Proton donor By similarity
Metal binding6221Divalent metal cation 1 By similarity
Metal binding6581Divalent metal cation 1 By similarity
Metal binding6591Divalent metal cation 1 By similarity
Metal binding6591Divalent metal cation 2 By similarity
Metal binding6621Divalent metal cation 2 By similarity
Metal binding6881Divalent metal cation 2 By similarity
Metal binding7701Divalent metal cation 1 By similarity
Binding site8231cAMP or cGMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1KKS3 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 0B12D6E7897E2E26

FASTA903102,019
        10         20         30         40         50         60 
MAVPKMVFSD VESFLDSHPE LFEDYLNRKG SSSMVEKWLK NHQAGKSEAE PKEEKSSVCK 

        70         80         90        100        110        120 
DSWASKCDGL QRRASQKELR KTFARSKAIN VNRTYDEHVN SRAQEPLTSM RRRALLRKAS 

       130        140        150        160        170        180 
SLPPTTAHIL SALLESRVNI PQYPSTAVDF KYYLKEHNER EFFLELVKDI SNDLDLTSLS 

       190        200        210        220        230        240 
YKILVFVCIM VDADRCSLFL VEGTGNKKTL VSKFFDVHAG TTVLPSMNSG EVQVPWGKGI 

       250        260        270        280        290        300 
IGYVAEHGET VNIPDAYQDR RFSDEIDKLT GYKTKSLLCM PIQNSDGEII GVAQAINKSS 

       310        320        330        340        350        360 
SGELFTEDDE KVLQMYLPFC GIAISNAQLF AASRKEYDRS RALLEVVNDL FEEQTDLEKI 

       370        380        390        400        410        420 
VRKIMHRAQT LLKCERCSVQ LLEDIESPVV KFTKSFELLS PKCSADAESS FKDSMEKSSY 

       430        440        450        460        470        480 
SDWLINNSIA ELVASTGLPV NISDAYQDPR FDAEADQFSD FHIRSVLCVP IWNSNHQIIG 

       490        500        510        520        530        540 
VAQVLNRLDG KPFDDADQRL FEAFVIFCGL GINNTIMYDQ VKKSWAKQSV ALDVLSYHAT 

       550        560        570        580        590        600 
CSKTEVDKFK AANIPLVCEL GIDKLSFDDF SLDVDAMITA ALRMFIELGM VQKFKIDYET 

       610        620        630        640        650        660 
LCRWLLTVRK NYRMVLYHNW RHAFNVCQCM FAMLTTAGFQ ETLTDVEILA LIVGCVCHDL 

       670        680        690        700        710        720 
DHRGTNNAFQ AKTGSALSLL YGTSATLEHH HFNHAVMILQ SEGHNIFCNL SSTEYSDLMQ 

       730        740        750        760        770        780 
LLKQSILATD LTLYFENRNS FFELVSIGEY NWNVKTHRDM CRSMMMTACD LGAVTKPWDI 

       790        800        810        820        830        840 
SRKVAELVTS EFFEQGDRER SELKLTPSAI FDRNRKDELP GLQLEWIDGI CAPLYETLVK 

       850        860        870        880        890        900 
LNPKLQPMVD MINANRVKWE ELDKKRQHDH GASVPASPCS AAEGSETGGV PCCSNNTPPT 


HVS 

« Hide

References

[1]"Highly conserved syntenic blocks at the vertebrate Hox loci and conserved regulatory elements within and outside Hox gene clusters."
Lee A.P., Koh E.G.L., Tay A., Brenner S., Venkatesh B.
Proc. Natl. Acad. Sci. U.S.A. 103:6994-6999(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ481668 Genomic DNA. Translation: ABF22471.1.

3D structure databases

ProteinModelPortalQ1KKS3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING31033.ENSTRUP00000044767.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG270709.
InParanoidQ1KKS3.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMSSF55781. SSF55781. 2 hits.
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDE11_TAKRU
AccessionPrimary (citable) accession number: Q1KKS3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: May 30, 2006
Last modified: June 11, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families