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Protein

Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A

Gene

Pde11a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

a divalent metal cationBy similarityNote: 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 regulationi

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

Kineticsi

  1. KM=3.9 µM for cAMP (isoform 1)1 Publication
  2. KM=1.6 µM for cGMP (isoform 1)1 Publication
  3. KM=4.0 µM for cAMP (isoform 2)1 Publication
  4. KM=1.6 µM for cGMP (isoform 2)1 Publication
  5. KM=2.2 µM for cAMP (isoform 3)1 Publication
  6. KM=1.3 µM for cGMP (isoform 3)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei664 – 6641Proton donorBy similarity
Metal bindingi668 – 6681Divalent metal cation 1By similarity
Metal bindingi704 – 7041Divalent metal cation 1By similarity
Metal bindingi705 – 7051Divalent metal cation 1By similarity
Metal bindingi705 – 7051Divalent metal cation 2By similarity
Metal bindingi708 – 7081Divalent metal cation 2By similarity
Metal bindingi734 – 7341Divalent metal cation 2By similarity
Metal bindingi816 – 8161Divalent metal cation 1By similarity
Binding sitei869 – 8691cAMP or cGMPBy similarity

GO - Molecular functioni

  1. 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB-EC
  2. cAMP binding Source: RGD
  3. cGMP binding Source: RGD
  4. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  5. cyclic-nucleotide phosphodiesterase activity Source: RGD
  6. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cAMP catabolic process Source: RGD
  2. cGMP catabolic process Source: RGD
  3. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, cGMP, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_287445. G alpha (s) signalling events.
REACT_349609. cGMP effects.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Pde11a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi621793. Pde11a.

Subcellular locationi

Cytoplasmcytosol By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. perikaryon Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 935935Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11APRO_0000247042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei239 – 2391PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ8VID6.

PTM databases

PhosphoSiteiQ8VID6.

Expressioni

Tissue specificityi

Isoform 1 is expressed in brain, heart, kidney and liver, but not in prostate. Isoform 2 is specifically expressed in testis. Isoform 3 is expressed in various tissues including brain, lung, skeletal muscle, spleen, testis and prostate.1 Publication

Gene expression databases

ExpressionAtlasiQ8VID6. baseline and differential.
GenevestigatoriQ8VID6.

Structurei

3D structure databases

ProteinModelPortaliQ8VID6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini217 – 370154GAF 1Add
BLAST
Domaini402 – 558157GAF 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni640 – 905266CatalyticBy similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 2 GAF domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00760000119066.
HOGENOMiHOG000007068.
HOVERGENiHBG101207.
InParanoidiQ8VID6.
KOiK13298.
PhylomeDBiQ8VID6.
TreeFamiTF316499.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 2 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VID6-1) [UniParc]FASTAAdd to basket

Also known as: PDE11A4

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAASRLDFGE VETFLDRHPE LFEDYLMRKG KQELVDKWLQ RHSSGQGASD
60 70 80 90 100
LRPALAGASS LAQSSARGST GIGGGAGPQG SANSHPASGG GESAGVPLSP
110 120 130 140 150
SWASGSRGDG NLQRRASQKE LRKSFARSKA IHVNRTYDEQ VTSRAQEPLS
160 170 180 190 200
SVRRRALLRK ASSLPPTTAH ILSALLESRV NLPQYPPTAI DYKCHLKKHN
210 220 230 240 250
ERQFFLELVK DISNDLDLTS LSYKILIFVC LMVDADRCSL FLVEGAAAGK
260 270 280 290 300
KTLVSKFFDV HAGTPLLPCS TTENSNEVQV PWGKGIIGYV GEHGETVNIP
310 320 330 340 350
DAYQDRRFND EIDKLTGYKT KSLLCMPIRN SDGEIIGVAQ AINKVPEGAP
360 370 380 390 400
FTEDDEKVMQ MYLPFCGIAI SNAQLFAASR KEYERSRALL EVVNDLFEEQ
410 420 430 440 450
TDLEKIVKKI MHRAQTLLKC ERCSVLLLED IESPVVKFTK SFELMSPKCS
460 470 480 490 500
ADAENSFKES VEKSSYSDWL INNSIAELVA STGLPVNVSD AYQDPRFDAE
510 520 530 540 550
ADQISGFHIR SVLCVPIWNS NHQIIGVAQV LNRLDGKPFD DADQRLFEAF
560 570 580 590 600
VIFCGLGINN TIMYDQVKKS WAKQSVALDV LSYHATCSKA EVDKFKAANI
610 620 630 640 650
PLVSELAIDD IHFDDFSLDV DAMITAALRM FMELGMVQKF KIDYETLCRW
660 670 680 690 700
LLTVRKNYRM VLYHNWRHAF NVCQLMFAML TTAGFQEILT EVEILAVIVG
710 720 730 740 750
CLCHDLDHRG TNNAFQAKSD SALAQLYGTS ATLEHHHFNH AVMILQSEGH
760 770 780 790 800
NIFANLSSKE YSDLMQLLKQ SILATDLTLY FERRTEFFEL VSKGAYDWSI
810 820 830 840 850
TSHRDVFRSM LMTACDLGAV TKPWEISRQV AELVTSEFFE QGDRERSELK
860 870 880 890 900
LTPSAIFDRN RKDELPRLQL EWIDSICMPL YQALVKVNAK LKPMLDSVAA
910 920 930
NRRKWEELHQ KRLQVSAASP VPSSPSPAVA GEDRL
Length:935
Mass (Da):104,571
Last modified:March 1, 2002 - v1
Checksum:iE80F1039770F8276
GO
Isoform 2 (identifier: Q8VID6-2) [UniParc]FASTAAdd to basket

Also known as: PDE11A3

The sequence of this isoform differs from the canonical sequence as follows:
     1-250: Missing.
     251-304: KTLVSKFFDV...ETVNIPDAYQ → MLKQARRFSF...FLTRMQTRTK

Show »
Length:685
Mass (Da):78,067
Checksum:i505E8748E9A6C21F
GO
Isoform 3 (identifier: Q8VID6-3) [UniParc]FASTAAdd to basket

Also known as: PDE11A2

The sequence of this isoform differs from the canonical sequence as follows:
     1-354: Missing.
     355-357: DEK → MSW

Show »
Length:581
Mass (Da):66,142
Checksum:i2CA7C2F5DDB37D00
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 354354Missing in isoform 3. 1 PublicationVSP_019902Add
BLAST
Alternative sequencei1 – 250250Missing in isoform 2. 1 PublicationVSP_019903Add
BLAST
Alternative sequencei251 – 30454KTLVS…PDAYQ → MLKQARRFSFRNVRSATQWR KVGSTRQGQISGAFLAERLD KHQDFLTRMQTRTK in isoform 2. 1 PublicationVSP_019904Add
BLAST
Alternative sequencei355 – 3573DEK → MSW in isoform 3. 1 PublicationVSP_019905

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB059360 mRNA. Translation: BAB79627.1.
AB059361 mRNA. Translation: BAB79628.1.
AB059362 mRNA. Translation: BAB79629.1.
RefSeqiNP_001120952.1. NM_001127480.1. [Q8VID6-2]
NP_001120953.1. NM_001127481.2. [Q8VID6-3]
NP_543169.1. NM_080893.1. [Q8VID6-1]
UniGeneiRn.88630.

Genome annotation databases

EnsembliENSRNOT00000008301; ENSRNOP00000008300; ENSRNOG00000024457. [Q8VID6-1]
ENSRNOT00000050355; ENSRNOP00000051289; ENSRNOG00000024457. [Q8VID6-2]
GeneIDi140928.
KEGGirno:140928.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB059360 mRNA. Translation: BAB79627.1.
AB059361 mRNA. Translation: BAB79628.1.
AB059362 mRNA. Translation: BAB79629.1.
RefSeqiNP_001120952.1. NM_001127480.1. [Q8VID6-2]
NP_001120953.1. NM_001127481.2. [Q8VID6-3]
NP_543169.1. NM_080893.1. [Q8VID6-1]
UniGeneiRn.88630.

3D structure databases

ProteinModelPortaliQ8VID6.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ8VID6.

Proteomic databases

PRIDEiQ8VID6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000008301; ENSRNOP00000008300; ENSRNOG00000024457. [Q8VID6-1]
ENSRNOT00000050355; ENSRNOP00000051289; ENSRNOG00000024457. [Q8VID6-2]
GeneIDi140928.
KEGGirno:140928.

Organism-specific databases

CTDi50940.
RGDi621793. Pde11a.

Phylogenomic databases

GeneTreeiENSGT00760000119066.
HOGENOMiHOG000007068.
HOVERGENiHBG101207.
InParanoidiQ8VID6.
KOiK13298.
PhylomeDBiQ8VID6.
TreeFamiTF316499.

Enzyme and pathway databases

ReactomeiREACT_287445. G alpha (s) signalling events.
REACT_349609. cGMP effects.

Miscellaneous databases

NextBioi620787.
PROiQ8VID6.

Gene expression databases

ExpressionAtlasiQ8VID6. baseline and differential.
GenevestigatoriQ8VID6.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 2 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of rat cyclic nucleotide phosphodiesterase 11A (PDE11A): comparison of rat and human PDE11A splicing variants."
    Yuasa K., Ohgaru T., Asahina M., Omori K.
    Eur. J. Biochem. 268:4440-4448(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPDE11_RAT
AccessioniPrimary (citable) accession number: Q8VID6
Secondary accession number(s): Q8VID7, Q8VID8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2002
Last modified: April 1, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. 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.