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Q9QYJ6

- PDE10_RAT

UniProt

Q9QYJ6 - PDE10_RAT

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Protein
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Gene
Pde10a
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate.1 Publication

Catalytic activityi

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.1 Publication
Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.1 Publication

Cofactori

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.

Enzyme regulationi

Inhibited by dipyridamole and moderately by IBMX, zaprinast and rolipram.1 Publication

Kineticsi

  1. KM=0.26 µM for cAMP1 Publication
  2. KM=9.3 µM for cGMP

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei374 – 3741Allosteric effector By similarity
Binding sitei393 – 3931Allosteric effector By similarity
Active sitei525 – 5251Proton donor By similarity
Binding sitei525 – 5251Substrate By similarity
Metal bindingi529 – 5291Divalent metal cation 1
Metal bindingi563 – 5631Divalent metal cation 1
Metal bindingi564 – 5641Divalent metal cation 1
Metal bindingi564 – 5641Divalent metal cation 2
Metal bindingi674 – 6741Divalent metal cation 1
Binding sitei726 – 7261Substrate By 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. drug binding Source: RGD
  7. 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, cAMP-binding, cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00762; UER00747.
UPA00763; UER00748.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC:3.1.4.17, EC:3.1.4.35)
Gene namesi
Name:Pde10a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi68434. Pde10a.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. membrane Source: RGD
  3. neuronal cell body Source: RGD
  4. perikaryon Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 794794cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
PRO_0000355559Add
BLAST

Proteomic databases

PaxDbiQ9QYJ6.
PRIDEiQ9QYJ6.

Miscellaneous databases

PMAP-CutDBQ9QYJ6.

Expressioni

Tissue specificityi

Detected in striatum and testis (at protein level). Detected in whole brain, hippocampus, olfactory bulb, striatum neurons and testis.2 Publications

Inductioni

Up-regulated in brain after seizures. Up-regulated in the hippocampus one hour after induction of long-term potentiation.2 Publications

Gene expression databases

GenevestigatoriQ9QYJ6.

Interactioni

Subunit structurei

Homodimer By similarity.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi466 – 4716
Helixi483 – 4853
Helixi486 – 49813
Helixi500 – 5023
Helixi505 – 51713
Beta strandi523 – 5264
Helixi527 – 54216
Turni545 – 5473
Helixi550 – 56213
Turni563 – 5664
Helixi572 – 5787
Helixi581 – 5855
Beta strandi587 – 5893
Helixi590 – 60314
Turni610 – 6134
Helixi616 – 63217
Helixi635 – 65016
Helixi659 – 67416
Helixi676 – 6794
Helixi682 – 70524
Helixi712 – 7143
Helixi716 – 7216
Helixi722 – 73211
Helixi734 – 74411
Helixi746 – 7483
Helixi749 – 76618

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O8HX-ray1.80A452-794[»]
2OVVX-ray2.00A452-794[»]
2OVYX-ray1.80A452-794[»]
3HQWX-ray1.70A452-794[»]
3HQYX-ray2.00A452-794[»]
3HQZX-ray1.70A452-794[»]
3HR1X-ray1.53A452-794[»]
3LXGX-ray2.30A463-770[»]
3QPNX-ray2.00A452-794[»]
3QPOX-ray1.80A452-794[»]
3QPPX-ray1.80A452-794[»]
ProteinModelPortaliQ9QYJ6.
SMRiQ9QYJ6. Positions 256-432, 464-770.

Miscellaneous databases

EvolutionaryTraceiQ9QYJ6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni296 – 2972Allosteric effector binding By similarity
Regioni340 – 3412Allosteric effector binding By similarity

Domaini

The tandem GAF domains bind cAMP, and regulate enzyme activity. The binding of cAMP stimulates enzyme activity.
Composed of a C-terminal catalytic domain containing two divalent metal sites and an N-terminal regulatory domain which contains one cyclic nucleotide-binding region.

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270709.
GeneTreeiENSGT00750000117253.
HOGENOMiHOG000007068.
HOVERGENiHBG082113.
InParanoidiQ6S9E8.
KOiK01120.
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 (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9QYJ6-1) [UniParc]FASTAAdd to Basket

Also known as: PDE10A2

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

MEDGPSNNAS CFRRLTECFL SPSLTDEKVK AYLSLHPQVL DEFVSESVSA    50
ETVEKWLKRK NNKAEDEPSP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG 100
DNHLLLYELS SIIRIATKAD GFALYFLGEC NNSLCVFTPP GMKEGQPRLI 150
PAGPITQGTT ISAYVAKSRK TLLVEDILGD ERFPRGTGLE SGTRIQSVLC 200
LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA SVAIHQVQVC 250
RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF 300
QVDHKNKELY SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV 350
LNIPDAYADP RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG 400
SAFSKTDENN FKMFAVFCAL ALHCANMYHR IRHSECIYRV TMEKLSYHSI 450
CTSEEWQGLM HFNLPARICR DIELFHFDIG PFENMWPGIF VYMIHRSCGT 500
SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI LQNNNGLFTD 550
LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV 600
SILQLEGHNI FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ 650
TGSLNLHNQS HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG 700
DEMKKLGIQP IPMMDRDKRD EVPQGQLGFY NAVAIPCYTT LTQILPPTEP 750
LLKACRDNLN QWEKVIRGEE TAMWISGPAT SKSTSEKPTR KVDD 794
Length:794
Mass (Da):90,161
Last modified:May 1, 2000 - v1
Checksum:iA36C4678B385846E
GO
Isoform 2 (identifier: Q9QYJ6-2) [UniParc]FASTAAdd to Basket

Also known as: PDE10A3

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MEDGPSNNASCFRRLTECFLSPS → MSNDSPEGAVGSCNATG

Show »
Length:788
Mass (Da):89,196
Checksum:i44F421DF1CC8FBA0
GO
Isoform 3 (identifier: Q9QYJ6-3) [UniParc]FASTAAdd to Basket

Also known as: PDE10A11

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MEDGPSNNASCFRRLTECFLSPS → MSKKRKALEG...GAVGSCNATG

Show »
Length:852
Mass (Da):95,777
Checksum:i31F6E5D4DDB8F60B
GO
Isoform 4 (identifier: Q9QYJ6-4) [UniParc]FASTAAdd to Basket

Also known as: PDE10A12

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MEDGPSNNASCFRRLTECFLSPS → MSKKRKALEG...SDSRLALCMG

Show »
Length:883
Mass (Da):99,036
Checksum:i86527DFF337E4B4F
GO
Isoform 5 (identifier: Q9QYJ6-5) [UniParc]FASTAAdd to Basket

Also known as: PDE10A13

The sequence of this isoform differs from the canonical sequence as follows:
     1-80: Missing.

Show »
Length:714
Mass (Da):81,028
Checksum:i5AFBCD366955F8F6
GO
Isoform 6 (identifier: Q9QYJ6-6) [UniParc]FASTAAdd to Basket

Also known as: PDE10A14

The sequence of this isoform differs from the canonical sequence as follows:
     1-141: Missing.

Show »
Length:653
Mass (Da):74,275
Checksum:iC712183FC1CFA76F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 141141Missing in isoform 6.
VSP_035919Add
BLAST
Alternative sequencei1 – 8080Missing in isoform 5.
VSP_035920Add
BLAST
Alternative sequencei1 – 2323MEDGP…FLSPS → MSNDSPEGAVGSCNATG in isoform 2.
VSP_035921Add
BLAST
Alternative sequencei1 – 2323MEDGP…FLSPS → MSKKRKALEGGGGGGEPQLP EEEPTAWFGGSSEEPAGCLP ITFKGGSKGPALLALRNRTD SRGQMSNDSPEGAVGSCNAT G in isoform 3.
VSP_035922Add
BLAST
Alternative sequencei1 – 2323MEDGP…FLSPS → MSKKRKALEGGGGGGEPQLP EEEPTAWFGGSSEEPAGCLP ITFKGGSKGPALLALRNRTD SRGQMSNDSPEGAVGSCNAT GSTGSTGELGKEFHTPPRRK SASDSRLALCMG in isoform 4.
VSP_035923Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB027155 mRNA. Translation: BAA88996.1.
AB027156 mRNA. Translation: BAA88997.1.
AY462091 mRNA. Translation: AAS21243.1.
AY462092 mRNA. Translation: AAS21244.1.
AY462093 mRNA. Translation: AAS21245.1.
AY462094 mRNA. Translation: AAS21246.1.
AY462095 mRNA. Translation: AAS21247.1.
CH474059 Genomic DNA. Translation: EDL83106.1.
RefSeqiNP_071572.1. NM_022236.1. [Q9QYJ6-1]
UniGeneiRn.44869.

Genome annotation databases

EnsembliENSRNOT00000043474; ENSRNOP00000042134; ENSRNOG00000011310. [Q9QYJ6-1]
GeneIDi63885.
KEGGirno:63885.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB027155 mRNA. Translation: BAA88996.1 .
AB027156 mRNA. Translation: BAA88997.1 .
AY462091 mRNA. Translation: AAS21243.1 .
AY462092 mRNA. Translation: AAS21244.1 .
AY462093 mRNA. Translation: AAS21245.1 .
AY462094 mRNA. Translation: AAS21246.1 .
AY462095 mRNA. Translation: AAS21247.1 .
CH474059 Genomic DNA. Translation: EDL83106.1 .
RefSeqi NP_071572.1. NM_022236.1. [Q9QYJ6-1 ]
UniGenei Rn.44869.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2O8H X-ray 1.80 A 452-794 [» ]
2OVV X-ray 2.00 A 452-794 [» ]
2OVY X-ray 1.80 A 452-794 [» ]
3HQW X-ray 1.70 A 452-794 [» ]
3HQY X-ray 2.00 A 452-794 [» ]
3HQZ X-ray 1.70 A 452-794 [» ]
3HR1 X-ray 1.53 A 452-794 [» ]
3LXG X-ray 2.30 A 463-770 [» ]
3QPN X-ray 2.00 A 452-794 [» ]
3QPO X-ray 1.80 A 452-794 [» ]
3QPP X-ray 1.80 A 452-794 [» ]
ProteinModelPortali Q9QYJ6.
SMRi Q9QYJ6. Positions 256-432, 464-770.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q9QYJ6.
ChEMBLi CHEMBL6140.

Proteomic databases

PaxDbi Q9QYJ6.
PRIDEi Q9QYJ6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000043474 ; ENSRNOP00000042134 ; ENSRNOG00000011310 . [Q9QYJ6-1 ]
GeneIDi 63885.
KEGGi rno:63885.

Organism-specific databases

CTDi 10846.
RGDi 68434. Pde10a.

Phylogenomic databases

eggNOGi NOG270709.
GeneTreei ENSGT00750000117253.
HOGENOMi HOG000007068.
HOVERGENi HBG082113.
InParanoidi Q6S9E8.
KOi K01120.
TreeFami TF316499.

Enzyme and pathway databases

UniPathwayi UPA00762 ; UER00747 .
UPA00763 ; UER00748 .

Miscellaneous databases

EvolutionaryTracei Q9QYJ6.
NextBioi 612518.
PMAP-CutDB Q9QYJ6.
PROi Q9QYJ6.

Gene expression databases

Genevestigatori Q9QYJ6.

Family and domain databases

Gene3Di 1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProi IPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view ]
SUPFAMi SSF55781. SSF55781. 2 hits.
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Striatum- and testis-specific phosphodiesterase PDE10A isolation and characterization of a rat PDE10A."
    Fujishige K., Kotera J., Omori K.
    Eur. J. Biochem. 266:1118-1127(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "Differential amplification of intron-containing transcripts reveals long term potentiation-associated up-regulation of specific Pde10A phosphodiesterase splice variants."
    O'Connor V., Genin A., Davis S., Karishma K.K., Doyere V., De Zeeuw C.I., Sanger G., Hunt S.P., Richter-Levin G., Mallet J., Laroche S., Bliss T.V.P., French P.J.
    J. Biol. Chem. 279:15841-15849(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, INDUCTION.
    Strain: Wistar.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 452-794 IN COMPLEXES WITH ZINC; MAGNESIUM AND A SYNTHETIC INHIBITOR.

Entry informationi

Entry nameiPDE10_RAT
AccessioniPrimary (citable) accession number: Q9QYJ6
Secondary accession number(s): Q6S9E6
, Q6S9E7, Q6S9E8, Q6S9E9, Q9QYJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 79 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

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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