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Q8CA95

- PDE10_MOUSE

UniProt

Q8CA95 - PDE10_MOUSE

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Protein
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Gene
Pde10a
Organism
Mus musculus (Mouse)
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. May play a critical role in regulating cAMP and cGMP levels in the striatum, a region of the brain that contributes to the control of movement and cognition.1 Publication

Catalytic activityi

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

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 By similarity.

Kineticsi

  1. KM=0.05 µM for cAMP1 Publication
  2. KM=3 µM for cGMP

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei368 – 3681Allosteric effector By similarity
Binding sitei387 – 3871Allosteric effector By similarity
Active sitei519 – 5191Proton donor By similarity
Binding sitei519 – 5191Substrate By similarity
Metal bindingi523 – 5231Divalent metal cation 1 By similarity
Metal bindingi557 – 5571Divalent metal cation 1 By similarity
Metal bindingi558 – 5581Divalent metal cation 1 By similarity
Metal bindingi558 – 5581Divalent metal cation 2 By similarity
Metal bindingi668 – 6681Divalent metal cation 1 By similarity
Binding sitei720 – 7201Substrate By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cAMP catabolic process Source: UniProtKB-UniPathway
  2. cGMP catabolic process Source: UniProtKB-UniPathway
  3. regulation of cAMP-mediated signaling Source: MGI
  4. regulation of protein kinase A signaling Source: MGI
  5. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1345143. Pde10a.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 790790cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
PRO_0000355558Add
BLAST

Proteomic databases

PaxDbiQ8CA95.
PRIDEiQ8CA95.

PTM databases

PhosphoSiteiQ8CA95.

Expressioni

Tissue specificityi

Detected in striatum (at protein level). Detected in testis and brain.2 Publications

Inductioni

Down-regulated by the expression of a huntingtin (HD) gene with an expanded polyglutamine repeat prior to the onset of neurological symptoms related to Huntington disease.1 Publication

Gene expression databases

BgeeiQ8CA95.
GenevestigatoriQ8CA95.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi204836. 3 interactions.
IntActiQ8CA95. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ8CA95.
SMRiQ8CA95. Positions 159-761.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 2912Allosteric effector binding By similarity
Regioni334 – 3352Allosteric effector binding By similarity

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270709.
GeneTreeiENSGT00750000117253.
HOGENOMiHOG000007068.
HOVERGENiHBG082113.
InParanoidiQ3TLU6.
KOiK01120.
OMAiCRFTMSV.
OrthoDBiEOG7WQ7RN.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8CA95-1) [UniParc]FASTAAdd to Basket

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

MSNDSTEGTV GSCNATGLTD EKVKAYLSLH PQVLDEFVSE SVSAETVEKW    50
LKRKTNKAKD EPSPKEVSRY QDTNMQGVVY ELNSYIEQRL DTGGDNHLLL 100
YELSSIIRIA TKADGFALYF LGECNNSLCV FIPPGMKEGQ PRLIPAGPIT 150
QGTTISAYVA KSRKTLLVED ILGDERFPRG TGLESGTRIQ SVLCLPIVTA 200
IGDLIGILEL YRHWGKEAFC LSHQEVATAN LAWASVAIHQ VQVCRGLAKQ 250
TELNDFLLDV SKTYFDNIVA IDSLLEHIMI YAKNLVNADR CALFQVDHKN 300
KELYSDLFDI GEEKEGKPIF KKTKEIRFSI EKGIAGQVAR TGEVLNIPDA 350
YADPRFNREV DLYTGYTTRN ILCMPIVSRG SVIGVVQMVN KISGSAFSKT 400
DENNFKMFAV FCALALHCAN MYHRIRHSEC IYRVTMEKLS YHSICTSEEW 450
QGLMRFNLPA RICRDIELFH FDIGPFENMW PGIFVYMIHR SCGTSCFELE 500
KLCRFIMSVK KNYRRVPYHN WKHAVTVAHC MYAILQNNNG LFTDLERKGL 550
LIACLCHDLD HRGFSNSYLQ KFDHPLAALY STSTMEQHHF SQTVSILQLE 600
GHNIFSTLSS SEYEQVLEII RKAIIATDLA LYFGNRKQLE EMYQTGSLNL 650
HNQSHRDRVI GLMMTACDLC SVTKLWPVTK LTANDIYAEF WAEGDEMKKL 700
GIQPIPMMDR DKRDEVPQGQ LGFYNAVAIP CYTTLTQILP PTEPLLKACR 750
DNLNQWEKVI RGEETAMWIS GPGPAPSKST PEKLNVKVED 790
Length:790
Mass (Da):89,408
Last modified:December 16, 2008 - v2
Checksum:i1B1D8111A5AD7B92
GO
Isoform 2 (identifier: Q8CA95-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: MSNDSTEGTVGSCNAT → MEKLY

Show »
Length:779
Mass (Da):88,517
Checksum:i83691B72F0D0EEAB
GO
Isoform 3 (identifier: Q8CA95-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: MSNDSTEGTVGSCNATG → MEDGPSNNASCFRRLTECFLSPS

Show »
Length:796
Mass (Da):90,339
Checksum:i4662D791B45E9EBA
GO
Isoform 4 (identifier: Q8CA95-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.
     61-69: EPSPKEVSR → MPGPGQ

Show »
Length:727
Mass (Da):82,409
Checksum:i703F98A68850E67E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6060Missing in isoform 4.
VSP_035915Add
BLAST
Alternative sequencei1 – 1717MSNDS…CNATG → MEDGPSNNASCFRRLTECFL SPS in isoform 3.
VSP_035916Add
BLAST
Alternative sequencei1 – 1616MSNDS…SCNAT → MEKLY in isoform 2.
VSP_035917Add
BLAST
Alternative sequencei61 – 699EPSPKEVSR → MPGPGQ in isoform 4.
VSP_035918

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti774 – 7741P → Q in BAC30292. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF110507 mRNA. Translation: AAD31544.1.
AY360383 mRNA. Translation: AAR12579.1.
AK039249 mRNA. Translation: BAC30292.1.
AK162804 mRNA. Translation: BAE37063.1.
AK166310 mRNA. Translation: BAE38696.1.
CH466619 Genomic DNA. Translation: EDL02097.1.
CH466619 Genomic DNA. Translation: EDL02099.1.
BC113201 mRNA. Translation: AAI13202.1.
CCDSiCCDS28384.1. [Q8CA95-3]
RefSeqiNP_001277636.1. NM_001290707.1.
NP_035996.2. NM_011866.2. [Q8CA95-3]
XP_006523385.1. XM_006523322.1. [Q8CA95-2]
UniGeneiMm.87161.

Genome annotation databases

EnsembliENSMUST00000089085; ENSMUSP00000086485; ENSMUSG00000023868. [Q8CA95-3]
ENSMUST00000115720; ENSMUSP00000111385; ENSMUSG00000023868. [Q8CA95-2]
ENSMUST00000115724; ENSMUSP00000111389; ENSMUSG00000023868. [Q8CA95-1]
ENSMUST00000149440; ENSMUSP00000123216; ENSMUSG00000023868. [Q8CA95-4]
GeneIDi23984.
KEGGimmu:23984.
UCSCiuc008ajr.1. mouse. [Q8CA95-1]
uc008ajs.1. mouse. [Q8CA95-3]
uc008aju.1. mouse. [Q8CA95-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF110507 mRNA. Translation: AAD31544.1 .
AY360383 mRNA. Translation: AAR12579.1 .
AK039249 mRNA. Translation: BAC30292.1 .
AK162804 mRNA. Translation: BAE37063.1 .
AK166310 mRNA. Translation: BAE38696.1 .
CH466619 Genomic DNA. Translation: EDL02097.1 .
CH466619 Genomic DNA. Translation: EDL02099.1 .
BC113201 mRNA. Translation: AAI13202.1 .
CCDSi CCDS28384.1. [Q8CA95-3 ]
RefSeqi NP_001277636.1. NM_001290707.1.
NP_035996.2. NM_011866.2. [Q8CA95-3 ]
XP_006523385.1. XM_006523322.1. [Q8CA95-2 ]
UniGenei Mm.87161.

3D structure databases

ProteinModelPortali Q8CA95.
SMRi Q8CA95. Positions 159-761.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204836. 3 interactions.
IntActi Q8CA95. 1 interaction.

Chemistry

ChEMBLi CHEMBL1795126.

PTM databases

PhosphoSitei Q8CA95.

Proteomic databases

PaxDbi Q8CA95.
PRIDEi Q8CA95.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000089085 ; ENSMUSP00000086485 ; ENSMUSG00000023868 . [Q8CA95-3 ]
ENSMUST00000115720 ; ENSMUSP00000111385 ; ENSMUSG00000023868 . [Q8CA95-2 ]
ENSMUST00000115724 ; ENSMUSP00000111389 ; ENSMUSG00000023868 . [Q8CA95-1 ]
ENSMUST00000149440 ; ENSMUSP00000123216 ; ENSMUSG00000023868 . [Q8CA95-4 ]
GeneIDi 23984.
KEGGi mmu:23984.
UCSCi uc008ajr.1. mouse. [Q8CA95-1 ]
uc008ajs.1. mouse. [Q8CA95-3 ]
uc008aju.1. mouse. [Q8CA95-2 ]

Organism-specific databases

CTDi 10846.
MGIi MGI:1345143. Pde10a.

Phylogenomic databases

eggNOGi NOG270709.
GeneTreei ENSGT00750000117253.
HOGENOMi HOG000007068.
HOVERGENi HBG082113.
InParanoidi Q3TLU6.
KOi K01120.
OMAi CRFTMSV.
OrthoDBi EOG7WQ7RN.
TreeFami TF316499.

Enzyme and pathway databases

UniPathwayi UPA00762 ; UER00747 .
UPA00763 ; UER00748 .

Miscellaneous databases

ChiTaRSi PDE10A. mouse.
NextBioi 303873.
PROi Q8CA95.
SOURCEi Search...

Gene expression databases

Bgeei Q8CA95.
Genevestigatori Q8CA95.

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. "Isolation and characterization of a dual-substrate phosphodiesterase gene family: PDE10A."
    Soderling S.H., Bayuga S.J., Beavo J.A.
    Proc. Natl. Acad. Sci. U.S.A. 96:7071-7076(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "Striatal phosphodiesterase mRNA and protein levels are reduced in Huntington's disease transgenic mice prior to the onset of motor symptoms."
    Hebb A.L., Robertson H.A., Denovan-Wright E.M.
    Neuroscience 123:967-981(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INDUCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6 X CBA.
    Tissue: Corpus striatum.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Strain: C57BL/6J.
    Tissue: Mammary gland, Spinal cord and Thymus.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).

Entry informationi

Entry nameiPDE10_MOUSE
AccessioniPrimary (citable) accession number: Q8CA95
Secondary accession number(s): Q3TLU6
, Q3TRG6, Q69C21, Q9WVI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 85 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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