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P0C1Q2 (PDE11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length933 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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. Ref.2

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.

Tissue specificity

Expressed in testis and developing spermatoza. Ref.2

Domain

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

Disruption phenotype

Mice live well and have no impaired fertility. They do however display reduced sperm concentration, rate of forward progression and percentage of live spermatozoa. Pre-ejaculated sperm display increased premature/spontaneous capacitance. Ref.2

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Contains 2 GAF domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 933933Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
PRO_0000247041

Regions

Domain217 – 370154GAF 1
Domain402 – 558157GAF 2
Region640 – 905266Catalytic By similarity

Sites

Active site6641Proton donor By similarity
Metal binding6681Divalent metal cation 1 By similarity
Metal binding7041Divalent metal cation 1 By similarity
Metal binding7051Divalent metal cation 1 By similarity
Metal binding7051Divalent metal cation 2 By similarity
Metal binding7081Divalent metal cation 2 By similarity
Metal binding7341Divalent metal cation 2 By similarity
Metal binding8161Divalent metal cation 1 By similarity
Binding site8691cAMP or cGMP By similarity

Amino acid modifications

Modified residue2391Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C1Q2 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 07B7CA1E4F905755

FASTA933104,563
        10         20         30         40         50         60 
MAASRLDFGE VETFLDRHPE LFEDYLMRKG KQELVDKWLQ RHTSGQGASS LRPALAGASS 

        70         80         90        100        110        120 
LAQSNAKGSP GIGGGAGPQG SAHSHPTPGG GESAGVPLSP SWASGSRGDG SLQRRASQKE 

       130        140        150        160        170        180 
LRKSFARSKA IHVNRTYDEQ VTSRAQEPLS SVRRRALLRK ASSLPPTTAH ILSALLESRV 

       190        200        210        220        230        240 
NLPQYPPTAI DYKCHLKKHN ERQFFLELVK DISNDLDLTS LSYKILIFVC LMVDADRCSL 

       250        260        270        280        290        300 
FLVEGAAAGK KTLVSKFFDV HAGTPLLPCS STENSNEVQV PWGKGIIGYV GEHGETVNIP 

       310        320        330        340        350        360 
DAYQDRRFND EIDKLTGYKT KSLLCMPIRN SDGEIIGVAQ AINKVPEGAP FTEDDEKVMQ 

       370        380        390        400        410        420 
MYLPFCGIAI SNAQLFAASR KEYERSRALL EVVNDLFEEQ TDLEKIVKKI MHRAQTLLKC 

       430        440        450        460        470        480 
ERCSVLLLED IESPVVKFTK SFELMSPKCS ADAENSFKES VEKSSYSDWL INNSIAELVA 

       490        500        510        520        530        540 
STGLPVNVSD AYQDPRFDAE ADQISGFHIR SVLCVPIWNS NHQIIGVAQV LNRLDGKPFD 

       550        560        570        580        590        600 
DADQRLFEAF VIFCGLGINN TIMYDQVKKS WAKQSVALDV LSYHATCSKA EVDKFKAANI 

       610        620        630        640        650        660 
PLVSELAIDD IHFDDFSLDV DAMITAALRM FMELGMVQKF KIDYETLCRW LLTVRKNYRM 

       670        680        690        700        710        720 
VLYHNWRHAF NVCQLMFAML TTAGFQEILT EVEILAVIVG CLCHDLDHRG TNNAFQAKSD 

       730        740        750        760        770        780 
SALAQLYGTS ATLEHHHFNH AVMILQSEGH NIFANLSSKE YSDLMQLLKQ SILATDLTLY 

       790        800        810        820        830        840 
FERRTEFFEL VRKGDYDWSI TSHRDVFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE 

       850        860        870        880        890        900 
QGDRERSELK LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNAK LKPMLDSVAA 

       910        920        930 
NRRKWEELHQ KRLQVSAASP DPASPMVAGE DRL 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL772341, AL845373, AL929133 Genomic DNA. Translation: CAM16587.1.
AL845373, AL772341, AL929133 Genomic DNA. Translation: CAM17618.1.
AL929133, AL772341, AL845373 Genomic DNA. Translation: CAM23980.1.
AL929589 Genomic DNA. No translation available.
CCDSCCDS38152.1.
RefSeqNP_001074502.1. NM_001081033.1.
UniGeneMm.246613.

3D structure databases

ProteinModelPortalP0C1Q2.
SMRP0C1Q2. Positions 205-911.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP0C1Q2.

Proteomic databases

PRIDEP0C1Q2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000099992; ENSMUSP00000097572; ENSMUSG00000075270.
GeneID241489.
KEGGmmu:241489.
UCSCuc008kex.1. mouse.

Organism-specific databases

CTD50940.
MGIMGI:3036251. Pde11a.

Phylogenomic databases

eggNOGNOG270709.
GeneTreeENSGT00750000117253.
HOGENOMHOG000007068.
HOVERGENHBG101207.
InParanoidP0C1Q2.
KOK13298.
OMADYSDLMQ.
OrthoDBEOG7RRF69.
PhylomeDBP0C1Q2.
TreeFamTF316499.

Gene expression databases

BgeeP0C1Q2.
CleanExMM_PDE11A.
GenevestigatorP0C1Q2.

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...

Other

NextBio385015.
PROP0C1Q2.
SOURCESearch...

Entry information

Entry namePDE11_MOUSE
AccessionPrimary (citable) accession number: P0C1Q2
Secondary accession number(s): A2AKR2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: July 9, 2014
This is version 66 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot