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cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC 3.1.4.17) (EC 3.1.4.35)

 PDE10_MOUSE             Reviewed;         790 AA.
Q8CA95; Q3TLU6; Q3TRG6; Q69C21; Q9WVI1;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
22-NOV-2017, entry version 109.
RecName: Full=cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A;
EC=3.1.4.17;
EC=3.1.4.35;
Name=Pde10a;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=10359840; DOI=10.1073/pnas.96.12.7071;
Soderling S.H., Bayuga S.J., Beavo J.A.;
"Isolation and characterization of a dual-substrate phosphodiesterase
gene family: PDE10A.";
Proc. Natl. Acad. Sci. U.S.A. 96:7071-7076(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INDUCTION, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6 X CBA; TISSUE=Corpus striatum;
PubMed=14751289; DOI=10.1016/j.neuroscience.2003.11.009;
Hebb A.L., Robertson H.A., Denovan-Wright E.M.;
"Striatal phosphodiesterase mRNA and protein levels are reduced in
Huntington's disease transgenic mice prior to the onset of motor
symptoms.";
Neuroscience 123:967-981(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
STRAIN=C57BL/6J; TISSUE=Mammary gland, Spinal cord, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION, AND MUTAGENESIS OF TYR-101.
PubMed=27058446; DOI=10.1016/j.ajhg.2016.03.015;
Diggle C.P., Sukoff Rizzo S.J., Popiolek M., Hinttala R.,
Schuelke J.P., Kurian M.A., Carr I.M., Markham A.F., Bonthron D.T.,
Watson C., Sharif S.M., Reinhart V., James L.C., Vanase-Frawley M.A.,
Charych E., Allen M., Harms J., Schmidt C.J., Ng J., Pysden K.,
Strick C., Vieira P., Mankinen K., Kokkonen H., Kallioinen M.,
Sormunen R., Rinne J.O., Johansson J., Alakurtti K., Huilaja L.,
Hurskainen T., Tasanen K., Anttila E., Marques T.R., Howes O.,
Politis M., Fahiminiya S., Nguyen K.Q., Majewski J., Uusimaa J.,
Sheridan E., Brandon N.J.;
"Biallelic mutations in PDE10A Lead to loss of striatal PDE10A and a
hyperkinetic movement disorder with onset in infancy.";
Am. J. Hum. Genet. 98:735-743(2016).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10359840, ECO:0000269|PubMed:27058446}.
-!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
nucleoside 5'-phosphate.
-!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
guanosine 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=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. {ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.05 uM for cAMP {ECO:0000269|PubMed:10359840};
KM=3 uM for cGMP {ECO:0000269|PubMed:10359840};
-!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
3',5'-cyclic AMP: step 1/1.
-!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
3',5'-cyclic GMP: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8CA95-1; Sequence=Displayed;
Name=2;
IsoId=Q8CA95-2; Sequence=VSP_035917;
Name=3;
IsoId=Q8CA95-3; Sequence=VSP_035916;
Name=4;
IsoId=Q8CA95-4; Sequence=VSP_035915, VSP_035918;
-!- TISSUE SPECIFICITY: Detected in striatum (at protein level).
Detected in testis and brain. {ECO:0000269|PubMed:10359840,
ECO:0000269|PubMed:14751289}.
-!- INDUCTION: 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.
{ECO:0000269|PubMed:14751289}.
-!- DOMAIN: The tandem GAF domains bind cAMP, and regulate enzyme
activity. The binding of cAMP stimulates enzyme activity (By
similarity). {ECO:0000250}.
-!- DOMAIN: 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. {ECO:0000250}.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF110507; AAD31544.1; -; mRNA.
EMBL; AY360383; AAR12579.1; -; mRNA.
EMBL; AK039249; BAC30292.1; -; mRNA.
EMBL; AK162804; BAE37063.1; -; mRNA.
EMBL; AK166310; BAE38696.1; -; mRNA.
EMBL; CH466619; EDL02097.1; -; Genomic_DNA.
EMBL; CH466619; EDL02099.1; -; Genomic_DNA.
EMBL; BC113201; AAI13202.1; -; mRNA.
CCDS; CCDS28384.1; -. [Q8CA95-3]
CCDS; CCDS84274.1; -. [Q8CA95-2]
RefSeq; NP_001277636.1; NM_001290707.1.
RefSeq; NP_001334250.1; NM_001347321.1. [Q8CA95-2]
RefSeq; NP_035996.2; NM_011866.2. [Q8CA95-3]
RefSeq; XP_017172950.1; XM_017317461.1. [Q8CA95-1]
UniGene; Mm.87161; -.
ProteinModelPortal; Q8CA95; -.
SMR; Q8CA95; -.
BioGrid; 204836; 3.
IntAct; Q8CA95; 1.
STRING; 10090.ENSMUSP00000086485; -.
BindingDB; Q8CA95; -.
ChEMBL; CHEMBL1795126; -.
iPTMnet; Q8CA95; -.
PhosphoSitePlus; Q8CA95; -.
SwissPalm; Q8CA95; -.
PaxDb; Q8CA95; -.
PeptideAtlas; Q8CA95; -.
PRIDE; Q8CA95; -.
Ensembl; ENSMUST00000089085; ENSMUSP00000086485; ENSMUSG00000023868. [Q8CA95-3]
Ensembl; ENSMUST00000115720; ENSMUSP00000111385; ENSMUSG00000023868. [Q8CA95-2]
Ensembl; ENSMUST00000115724; ENSMUSP00000111389; ENSMUSG00000023868. [Q8CA95-1]
Ensembl; ENSMUST00000149440; ENSMUSP00000123216; ENSMUSG00000023868. [Q8CA95-4]
GeneID; 23984; -.
KEGG; mmu:23984; -.
UCSC; uc008ajr.1; mouse. [Q8CA95-1]
UCSC; uc008ajs.1; mouse. [Q8CA95-3]
UCSC; uc008aju.1; mouse. [Q8CA95-2]
CTD; 10846; -.
MGI; MGI:1345143; Pde10a.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000119066; -.
HOGENOM; HOG000007068; -.
HOVERGEN; HBG082113; -.
InParanoid; Q8CA95; -.
KO; K18438; -.
OMA; CRFTMSV; -.
OrthoDB; EOG091G037C; -.
TreeFam; TF316499; -.
Reactome; R-MMU-418457; cGMP effects.
Reactome; R-MMU-418555; G alpha (s) signalling events.
SABIO-RK; Q8CA95; -.
UniPathway; UPA00762; UER00747.
UniPathway; UPA00763; UER00748.
ChiTaRS; Pde10a; mouse.
PRO; PR:Q8CA95; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000023868; -.
ExpressionAtlas; Q8CA95; baseline and differential.
Genevisible; Q8CA95; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC.
GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IDA:MGI.
GO; GO:0030552; F:cAMP binding; ISS:UniProtKB.
GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0046069; P:cGMP catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0043949; P:regulation of cAMP-mediated signaling; IMP:MGI.
GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:MGI.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
Gene3D; 3.30.450.40; -; 2.
InterPro; IPR003018; GAF.
InterPro; IPR029016; GAF-like_dom_sf.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
Pfam; PF01590; GAF; 2.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00065; GAF; 2.
SMART; SM00471; HDc; 1.
SUPFAM; SSF55781; SSF55781; 2.
PROSITE; PS00126; PDEASE_I; 1.
1: Evidence at protein level;
Allosteric enzyme; Alternative splicing; cAMP; cAMP-binding; cGMP;
cGMP-binding; Complete proteome; Cytoplasm; Hydrolase; Metal-binding;
Nucleotide-binding; Reference proteome; Repeat.
CHAIN 1 790 cAMP and cAMP-inhibited cGMP 3',5'-cyclic
phosphodiesterase 10A.
/FTId=PRO_0000355558.
REGION 290 291 Allosteric effector binding.
{ECO:0000250}.
REGION 334 335 Allosteric effector binding.
{ECO:0000250}.
ACT_SITE 519 519 Proton donor. {ECO:0000250}.
METAL 523 523 Divalent metal cation 1. {ECO:0000250}.
METAL 557 557 Divalent metal cation 1. {ECO:0000250}.
METAL 558 558 Divalent metal cation 1. {ECO:0000250}.
METAL 558 558 Divalent metal cation 2. {ECO:0000250}.
METAL 668 668 Divalent metal cation 1. {ECO:0000250}.
BINDING 368 368 Allosteric effector. {ECO:0000250}.
BINDING 387 387 Allosteric effector. {ECO:0000250}.
BINDING 519 519 Substrate. {ECO:0000250}.
BINDING 720 720 Substrate. {ECO:0000250}.
VAR_SEQ 1 60 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_035915.
VAR_SEQ 1 17 MSNDSTEGTVGSCNATG -> MEDGPSNNASCFRRLTECFL
SPS (in isoform 3).
{ECO:0000303|PubMed:14751289}.
/FTId=VSP_035916.
VAR_SEQ 1 16 MSNDSTEGTVGSCNAT -> MEKLY (in isoform 2).
{ECO:0000303|PubMed:10359840}.
/FTId=VSP_035917.
VAR_SEQ 61 69 EPSPKEVSR -> MPGPGQ (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_035918.
MUTAGEN 101 101 Y->C: Decreased protein abundance;
decreased 3',5'-cyclic-nucleotide
phosphodiesterase activity.
{ECO:0000269|PubMed:27058446}.
CONFLICT 774 774 P -> Q (in Ref. 3; BAC30292).
{ECO:0000305}.
SEQUENCE 790 AA; 89408 MW; 1B1D8111A5AD7B92 CRC64;
MSNDSTEGTV GSCNATGLTD EKVKAYLSLH PQVLDEFVSE SVSAETVEKW LKRKTNKAKD
EPSPKEVSRY QDTNMQGVVY ELNSYIEQRL DTGGDNHLLL YELSSIIRIA TKADGFALYF
LGECNNSLCV FIPPGMKEGQ PRLIPAGPIT QGTTISAYVA KSRKTLLVED ILGDERFPRG
TGLESGTRIQ SVLCLPIVTA IGDLIGILEL YRHWGKEAFC LSHQEVATAN LAWASVAIHQ
VQVCRGLAKQ TELNDFLLDV SKTYFDNIVA IDSLLEHIMI YAKNLVNADR CALFQVDHKN
KELYSDLFDI GEEKEGKPIF KKTKEIRFSI EKGIAGQVAR TGEVLNIPDA YADPRFNREV
DLYTGYTTRN ILCMPIVSRG SVIGVVQMVN KISGSAFSKT DENNFKMFAV FCALALHCAN
MYHRIRHSEC IYRVTMEKLS YHSICTSEEW QGLMRFNLPA RICRDIELFH FDIGPFENMW
PGIFVYMIHR SCGTSCFELE KLCRFIMSVK KNYRRVPYHN WKHAVTVAHC MYAILQNNNG
LFTDLERKGL LIACLCHDLD HRGFSNSYLQ KFDHPLAALY STSTMEQHHF SQTVSILQLE
GHNIFSTLSS SEYEQVLEII RKAIIATDLA LYFGNRKQLE EMYQTGSLNL HNQSHRDRVI
GLMMTACDLC SVTKLWPVTK LTANDIYAEF WAEGDEMKKL GIQPIPMMDR DKRDEVPQGQ
LGFYNAVAIP CYTTLTQILP PTEPLLKACR DNLNQWEKVI RGEETAMWIS GPGPAPSKST
PEKLNVKVED


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