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Q9QYJ6

- PDE10_RAT

UniProt

Q9QYJ6 - PDE10_RAT

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
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    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

    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

    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 – 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.
    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.
    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. 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 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

    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 1, 2014
    This is version 80 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