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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: 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

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

Kineticsi

  1. KM=0.05 µM for cAMP1 Publication
  2. KM=3 µM for cGMP1 Publication

    Pathway: 3',5'-cyclic AMP degradation

    This protein is involved in step 1 of the subpathway that synthesizes AMP from 3',5'-cyclic AMP.
    Proteins known to be involved in this subpathway in this organism are:
    1. cAMP-specific 3',5'-cyclic phosphodiesterase 4A (Pde4a), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (Pde8b), cAMP-specific 3',5'-cyclic phosphodiesterase 4C (Pde4c), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A (Pde8a), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (Pde4d), High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (Pde7a), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (Pde10a), cAMP-specific 3',5'-cyclic phosphodiesterase 7B (Pde7b)
    This subpathway is part of the pathway 3',5'-cyclic AMP degradation, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from 3',5'-cyclic AMP, the pathway 3',5'-cyclic AMP degradation and in Purine metabolism.

    Pathway: 3',5'-cyclic GMP degradation

    This protein is involved in step 1 of the subpathway that synthesizes GMP from 3',5'-cyclic GMP.
    Proteins known to be involved in this subpathway in this organism are:
    1. cGMP-specific 3',5'-cyclic phosphodiesterase (Pde5a), High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (Pde9a), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (Pde10a)
    This subpathway is part of the pathway 3',5'-cyclic GMP degradation, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes GMP from 3',5'-cyclic GMP, the pathway 3',5'-cyclic GMP degradation and in Purine metabolism.

    Sites

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

    GO - Molecular functioni

    GO - Biological processi

    • cAMP catabolic process Source: UniProtKB-UniPathway
    • cGMP catabolic process Source: UniProtKB-UniPathway
    • regulation of cAMP-mediated signaling Source: MGI
    • regulation of protein kinase A signaling Source: MGI
    • 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

    ReactomeiREACT_311531. cGMP effects.
    REACT_313192. G alpha (s) signalling events.
    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 Componenti: Chromosome 17

    Organism-specific databases

    MGIiMGI:1345143. Pde10a.

    Subcellular locationi

    GO - Cellular componenti

    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 10APRO_0000355558Add
    BLAST

    Proteomic databases

    MaxQBiQ8CA95.
    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.
    ExpressionAtlasiQ8CA95. baseline and differential.
    GenevisibleiQ8CA95. MM.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi204836. 3 interactions.
    IntActiQ8CA95. 1 interaction.
    STRINGi10090.ENSMUSP00000086485.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CA95.
    SMRiQ8CA95. Positions 159-761.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

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

    Domaini

    The tandem GAF domains bind cAMP, and regulate enzyme activity. The binding of cAMP stimulates enzyme activity (By similarity).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.
    GeneTreeiENSGT00760000119066.
    HOGENOMiHOG000007068.
    HOVERGENiHBG082113.
    InParanoidiQ8CA95.
    KOiK18438.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MSNDSTEGTV GSCNATGLTD EKVKAYLSLH PQVLDEFVSE SVSAETVEKW
    60 70 80 90 100
    LKRKTNKAKD EPSPKEVSRY QDTNMQGVVY ELNSYIEQRL DTGGDNHLLL
    110 120 130 140 150
    YELSSIIRIA TKADGFALYF LGECNNSLCV FIPPGMKEGQ PRLIPAGPIT
    160 170 180 190 200
    QGTTISAYVA KSRKTLLVED ILGDERFPRG TGLESGTRIQ SVLCLPIVTA
    210 220 230 240 250
    IGDLIGILEL YRHWGKEAFC LSHQEVATAN LAWASVAIHQ VQVCRGLAKQ
    260 270 280 290 300
    TELNDFLLDV SKTYFDNIVA IDSLLEHIMI YAKNLVNADR CALFQVDHKN
    310 320 330 340 350
    KELYSDLFDI GEEKEGKPIF KKTKEIRFSI EKGIAGQVAR TGEVLNIPDA
    360 370 380 390 400
    YADPRFNREV DLYTGYTTRN ILCMPIVSRG SVIGVVQMVN KISGSAFSKT
    410 420 430 440 450
    DENNFKMFAV FCALALHCAN MYHRIRHSEC IYRVTMEKLS YHSICTSEEW
    460 470 480 490 500
    QGLMRFNLPA RICRDIELFH FDIGPFENMW PGIFVYMIHR SCGTSCFELE
    510 520 530 540 550
    KLCRFIMSVK KNYRRVPYHN WKHAVTVAHC MYAILQNNNG LFTDLERKGL
    560 570 580 590 600
    LIACLCHDLD HRGFSNSYLQ KFDHPLAALY STSTMEQHHF SQTVSILQLE
    610 620 630 640 650
    GHNIFSTLSS SEYEQVLEII RKAIIATDLA LYFGNRKQLE EMYQTGSLNL
    660 670 680 690 700
    HNQSHRDRVI GLMMTACDLC SVTKLWPVTK LTANDIYAEF WAEGDEMKKL
    710 720 730 740 750
    GIQPIPMMDR DKRDEVPQGQ LGFYNAVAIP CYTTLTQILP PTEPLLKACR
    760 770 780 790
    DNLNQWEKVI RGEETAMWIS GPGPAPSKST PEKLNVKVED
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti774 – 7741P → Q in BAC30292 (PubMed:16141072).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060Missing in isoform 4. 1 PublicationVSP_035915Add
    BLAST
    Alternative sequencei1 – 1717MSNDS…CNATG → MEDGPSNNASCFRRLTECFL SPS in isoform 3. 1 PublicationVSP_035916Add
    BLAST
    Alternative sequencei1 – 1616MSNDS…SCNAT → MEKLY in isoform 2. 1 PublicationVSP_035917Add
    BLAST
    Alternative sequencei61 – 699EPSPKEVSR → MPGPGQ in isoform 4. 1 PublicationVSP_035918

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    ProteinModelPortaliQ8CA95.
    SMRiQ8CA95. Positions 159-761.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi204836. 3 interactions.
    IntActiQ8CA95. 1 interaction.
    STRINGi10090.ENSMUSP00000086485.

    Chemistry

    BindingDBiQ8CA95.
    ChEMBLiCHEMBL1795126.

    PTM databases

    PhosphoSiteiQ8CA95.

    Proteomic databases

    MaxQBiQ8CA95.
    PaxDbiQ8CA95.
    PRIDEiQ8CA95.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    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]

    Organism-specific databases

    CTDi10846.
    MGIiMGI:1345143. Pde10a.

    Phylogenomic databases

    eggNOGiNOG270709.
    GeneTreeiENSGT00760000119066.
    HOGENOMiHOG000007068.
    HOVERGENiHBG082113.
    InParanoidiQ8CA95.
    KOiK18438.
    OMAiCRFTMSV.
    OrthoDBiEOG7WQ7RN.
    TreeFamiTF316499.

    Enzyme and pathway databases

    UniPathwayiUPA00762; UER00747.
    UPA00763; UER00748.
    ReactomeiREACT_311531. cGMP effects.
    REACT_313192. G alpha (s) signalling events.

    Miscellaneous databases

    ChiTaRSiPde10a. mouse.
    NextBioi303873.
    PROiQ8CA95.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8CA95.
    ExpressionAtlasiQ8CA95. baseline and differential.
    GenevisibleiQ8CA95. MM.

    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

    « 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: June 24, 2015
    This is version 92 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

    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.