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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 cGMP1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei374 – 3741Allosteric effectorBy similarity
Binding sitei393 – 3931Allosteric effectorBy similarity
Active sitei525 – 5251Proton donorBy similarity
Binding sitei525 – 5251SubstrateBy 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 – 7261SubstrateBy 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-KW
  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 10APRO_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.1 Publication

Gene expression databases

ExpressionAtlasiQ9QYJ6. baseline.
GenevestigatoriQ9QYJ6.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

Secondary structure

1
794
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi466 – 4716Combined sources
Helixi483 – 4853Combined sources
Helixi486 – 49813Combined sources
Helixi500 – 5023Combined sources
Helixi505 – 51713Combined sources
Beta strandi523 – 5264Combined sources
Helixi527 – 54216Combined sources
Turni545 – 5473Combined sources
Helixi550 – 56213Combined sources
Turni563 – 5664Combined sources
Helixi572 – 5787Combined sources
Helixi581 – 5855Combined sources
Beta strandi587 – 5893Combined sources
Helixi590 – 60314Combined sources
Turni610 – 6134Combined sources
Helixi616 – 63217Combined sources
Helixi635 – 65016Combined sources
Helixi659 – 67416Combined sources
Helixi676 – 6794Combined sources
Helixi682 – 70524Combined sources
Helixi712 – 7143Combined sources
Helixi716 – 7216Combined sources
Helixi722 – 73211Combined sources
Helixi734 – 74411Combined sources
Helixi746 – 7483Combined sources
Helixi749 – 76618Combined sources

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QYJ6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni296 – 2972Allosteric effector bindingBy similarity
Regioni340 – 3412Allosteric effector bindingBy 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.
GeneTreeiENSGT00760000119066.
HOGENOMiHOG000007068.
HOVERGENiHBG082113.
InParanoidiQ9QYJ6.
KOiK18438.
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) [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

        10         20         30         40         50
MEDGPSNNAS CFRRLTECFL SPSLTDEKVK AYLSLHPQVL DEFVSESVSA
60 70 80 90 100
ETVEKWLKRK NNKAEDEPSP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG
110 120 130 140 150
DNHLLLYELS SIIRIATKAD GFALYFLGEC NNSLCVFTPP GMKEGQPRLI
160 170 180 190 200
PAGPITQGTT ISAYVAKSRK TLLVEDILGD ERFPRGTGLE SGTRIQSVLC
210 220 230 240 250
LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA SVAIHQVQVC
260 270 280 290 300
RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF
310 320 330 340 350
QVDHKNKELY SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV
360 370 380 390 400
LNIPDAYADP RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG
410 420 430 440 450
SAFSKTDENN FKMFAVFCAL ALHCANMYHR IRHSECIYRV TMEKLSYHSI
460 470 480 490 500
CTSEEWQGLM HFNLPARICR DIELFHFDIG PFENMWPGIF VYMIHRSCGT
510 520 530 540 550
SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI LQNNNGLFTD
560 570 580 590 600
LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV
610 620 630 640 650
SILQLEGHNI FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ
660 670 680 690 700
TGSLNLHNQS HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG
710 720 730 740 750
DEMKKLGIQP IPMMDRDKRD EVPQGQLGFY NAVAIPCYTT LTQILPPTEP
760 770 780 790
LLKACRDNLN QWEKVIRGEE TAMWISGPAT SKSTSEKPTR KVDD
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. 1 PublicationVSP_035919Add
BLAST
Alternative sequencei1 – 8080Missing in isoform 5. 1 PublicationVSP_035920Add
BLAST
Alternative sequencei1 – 2323MEDGP…FLSPS → MSNDSPEGAVGSCNATG in isoform 2. 2 PublicationsVSP_035921Add
BLAST
Alternative sequencei1 – 2323MEDGP…FLSPS → MSKKRKALEGGGGGGEPQLP EEEPTAWFGGSSEEPAGCLP ITFKGGSKGPALLALRNRTD SRGQMSNDSPEGAVGSCNAT G in isoform 3. 1 PublicationVSP_035922Add
BLAST
Alternative sequencei1 – 2323MEDGP…FLSPS → MSKKRKALEGGGGGGEPQLP EEEPTAWFGGSSEEPAGCLP ITFKGGSKGPALLALRNRTD SRGQMSNDSPEGAVGSCNAT GSTGSTGELGKEFHTPPRRK SASDSRLALCMG in isoform 4. 1 PublicationVSP_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 ENSGT00760000119066.
HOGENOMi HOG000007068.
HOVERGENi HBG082113.
InParanoidi Q9QYJ6.
KOi K18438.
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

ExpressionAtlasi Q9QYJ6. baseline.
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: October 29, 2014
This is version 81 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