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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_HUMAN             Reviewed;         779 AA.
Q9Y233; Q6FHX1; Q9HCP9; Q9NTV4; Q9ULW9; Q9Y5T1;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-APR-2018, entry version 176.
RecName: Full=cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A;
EC=3.1.4.17;
EC=3.1.4.35;
Name=PDE10A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE10A2), AND PHOSPHORYLATION AT
THR-16 (ISOFORM PDE10A2) BY PKA.
TISSUE=Fetal lung;
PubMed=10441464; DOI=10.1006/bbrc.1999.1013;
Kotera J., Fujishige K., Yuasa K., Omori K.;
"Characterization and phosphorylation of PDE10A2, a novel alternative
splice variant of human phosphodiesterase that hydrolyzes cAMP and
cGMP.";
Biochem. Biophys. Res. Commun. 261:551-557(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE10A1).
TISSUE=Fetal lung;
PubMed=10373451; DOI=10.1074/jbc.274.26.18438;
Fujishige K., Kotera J., Michibata H., Yuasa K., Takebayashi S.,
Okumura K., Omori K.;
"Cloning and characterization of a novel human phosphodiesterase that
hydrolyzes both cAMP and cGMP (PDE10A).";
J. Biol. Chem. 274:18438-18445(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE10A1 AND PDE10A2).
TISSUE=Fetal brain;
PubMed=10393245; DOI=10.1016/S0378-1119(99)00171-7;
Loughney K., Snyder P.B., Uher L., Rosman G.J., Ferguson K.,
Florio V.A.;
"Isolation and characterization of PDE10A, a novel human 3',5'-cyclic
nucleotide phosphodiesterase.";
Gene 234:109-117(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE10A1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE10A1).
TISSUE=Colon;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-779, AND ALTERNATIVE SPLICING.
PubMed=10998054; DOI=10.1046/j.1432-1327.2000.01661.x;
Fujishige K., Kotera J., Yuasa K., Omori K.;
"The human phosphodiesterase PDE10A gene genomic organization and
evolutionary relatedness with other PDEs containing GAF domains.";
Eur. J. Biochem. 267:5943-5951(2000).
[8]
DOMAIN, AND ENZYME REGULATION.
PubMed=16330539; DOI=10.1074/jbc.M511468200;
Gross-Langenhoff M., Hofbauer K., Weber J., Schultz A., Schultz J.E.;
"cAMP is a ligand for the tandem GAF domain of human phosphodiesterase
10 and cGMP for the tandem GAF domain of phosphodiesterase 11.";
J. Biol. Chem. 281:2841-2846(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[11]
INVOLVEMENT IN IOLOD, VARIANTS IOLOD CYS-97 AND PRO-106, AND
CHARACTERIZATION OF VARIANTS IOLOD CYS-97 AND PRO-106.
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).
[12]
TISSUE SPECIFICITY, INVOLVEMENT IN ADSD2, VARIANTS ADSD2 LEU-290 AND
LEU-324, AND CHARACTERIZATION OF VARIANTS ADSD2 LEU-290 AND LEU-324.
PubMed=27058447; DOI=10.1016/j.ajhg.2016.02.015;
Mencacci N.E., Kamsteeg E.J., Nakashima K., R'Bibo L., Lynch D.S.,
Balint B., Willemsen M.A., Adams M.E., Wiethoff S., Suzuki K.,
Davies C.H., Ng J., Meyer E., Veneziano L., Giunti P., Hughes D.,
Raymond F.L., Carecchio M., Zorzi G., Nardocci N., Barzaghi C.,
Garavaglia B., Salpietro V., Hardy J., Pittman A.M., Houlden H.,
Kurian M.A., Kimura H., Vissers L.E., Wood N.W., Bhatia K.P.;
"De novo mutations in PDE10A cause childhood-onset chorea with
bilateral striatal lesions.";
Am. J. Hum. Genet. 98:763-771(2016).
[13]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 436-766 IN COMPLEXES WITH
AMP; CAMP; GMP; CGMP AND MAGNESIUM, MUTAGENESIS OF ASP-554, FUNCTION,
COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=17389385; DOI=10.1073/pnas.0700279104;
Wang H., Liu Y., Hou J., Zheng M., Robinson H., Ke H.;
"Structural insight into substrate specificity of phosphodiesterase
10.";
Proc. Natl. Acad. Sci. U.S.A. 104:5782-5787(2007).
[14]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 242-427 IN COMPLEX WITH CAMP,
DOMAIN, AND SUBUNIT.
PubMed=18477562; DOI=10.1074/jbc.M800595200;
Handa N., Mizohata E., Kishishita S., Toyama M., Morita S.,
Uchikubo-Kamo T., Akasaka R., Omori K., Kotera J., Terada T.,
Shirouzu M., Yokoyama S.;
"Crystal structure of the GAF-B domain from human phosphodiesterase
10A complexed with its ligand, cAMP.";
J. Biol. Chem. 283:19657-19664(2008).
-!- 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:0000250|UniProtKB:Q8CA95, ECO:0000269|PubMed:17389385}.
-!- 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:0000269|PubMed:17389385};
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:0000269|PubMed:17389385};
-!- ENZYME REGULATION: Inhibited by dipyridamole and moderately by
IBMX. cAMP acts as an allosteric activator.
{ECO:0000269|PubMed:16330539}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=56 nM for cAMP {ECO:0000269|PubMed:17389385};
KM=4.4 uM for cGMP {ECO:0000269|PubMed:17389385};
Vmax=507 nmol/min/mg enzyme for cAMP
{ECO:0000269|PubMed:17389385};
Vmax=1860 nmol/min/mg enzyme for cGMP
{ECO:0000269|PubMed:17389385};
-!- 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:0000269|PubMed:18477562}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Note=Located mostly to soluble
cellular fractions.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Isoforms differ in their N-terminal region.;
Name=PDE10A1;
IsoId=Q9Y233-1; Sequence=Displayed;
Name=PDE10A2;
IsoId=Q9Y233-2; Sequence=VSP_004601;
Note=Contains a phosphothreonine at position 16.
{ECO:0000269|PubMed:10441464};
-!- TISSUE SPECIFICITY: Abundant in the putamen and caudate nucleus
regions of brain and testis, moderately expressed in the thyroid
gland, pituitary gland, thalamus and cerebellum.
{ECO:0000269|PubMed:10373451, ECO:0000269|PubMed:27058447}.
-!- DOMAIN: The tandem GAF domains bind cAMP, and regulate enzyme
activity. The binding of cAMP stimulates enzyme activity.
-!- 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.
-!- PTM: Isoform PDE10A2: Phosphorylated on Thr-16.
{ECO:0000269|PubMed:10441464}.
-!- DISEASE: Dyskinesia, limb and orofacial, infantile-onset (IOLOD)
[MIM:616921]: An autosomal recessive, early-onset hyperkinetic
movement disorder characterized by axial hypotonia, dyskinesia of
the limbs and trunk, orofacial dyskinesia, drooling, and
dysarthria. The severity of the hyperkinesis is variable.
{ECO:0000269|PubMed:27058446}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Striatal degeneration, autosomal dominant 2 (ADSD2)
[MIM:616922]: An autosomal dominant disorder characterized by
striatal degeneration and dysfunction of basal ganglia, resulting
in hyperkinesis. {ECO:0000269|PubMed:27058447}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD32596.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB026816; BAA84467.1; -; mRNA.
EMBL; AB020593; BAA78034.1; -; mRNA.
EMBL; AF127479; AAD32595.1; -; mRNA.
EMBL; AF127480; AAD32596.1; ALT_INIT; mRNA.
EMBL; CR536567; CAG38804.1; -; mRNA.
EMBL; AL117345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL136130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL160160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC104858; AAI04859.1; -; mRNA.
EMBL; BC104860; AAI04861.1; -; mRNA.
EMBL; AB041798; BAB16383.1; -; Genomic_DNA.
CCDS; CCDS47513.1; -. [Q9Y233-2]
CCDS; CCDS5289.1; -. [Q9Y233-1]
RefSeq; NP_001124162.1; NM_001130690.2. [Q9Y233-2]
RefSeq; NP_006652.1; NM_006661.3. [Q9Y233-1]
RefSeq; XP_011533690.1; XM_011535388.2. [Q9Y233-1]
UniGene; Hs.348762; -.
PDB; 1LRB; Model; -; A=501-757.
PDB; 2OUN; X-ray; 1.56 A; A/B=439-766.
PDB; 2OUP; X-ray; 1.56 A; A/B=439-766.
PDB; 2OUQ; X-ray; 1.90 A; A/B=439-766.
PDB; 2OUR; X-ray; 1.45 A; A/B=439-766.
PDB; 2OUS; X-ray; 1.45 A; A/B=439-766.
PDB; 2OUU; X-ray; 1.52 A; A/B=439-766.
PDB; 2OUV; X-ray; 1.56 A; A/B=439-766.
PDB; 2OUY; X-ray; 1.90 A; A/B=439-766.
PDB; 2WEY; X-ray; 2.80 A; A/B=439-779.
PDB; 2Y0J; X-ray; 2.43 A; A/B=432-764.
PDB; 2ZMF; X-ray; 2.10 A; A/B=246-427.
PDB; 3SN7; X-ray; 1.82 A; A/B=439-779.
PDB; 3SNI; X-ray; 1.90 A; A/B=439-779.
PDB; 3SNL; X-ray; 2.40 A; A/B=439-779.
PDB; 3UI7; X-ray; 2.28 A; A/B=432-760.
PDB; 3UUO; X-ray; 2.11 A; A/B=432-760.
PDB; 3WI2; X-ray; 2.26 A; A/B=439-779.
PDB; 3WS8; X-ray; 2.60 A; A/B=439-779.
PDB; 3WS9; X-ray; 2.99 A; A/B=439-779.
PDB; 3WYK; X-ray; 2.50 A; A/B=442-779.
PDB; 3WYL; X-ray; 2.68 A; A/B=442-779.
PDB; 3WYM; X-ray; 2.00 A; A/B=442-779.
PDB; 4AEL; X-ray; 2.20 A; A/B=439-779.
PDB; 4AJD; X-ray; 2.30 A; A/D=439-764.
PDB; 4AJF; X-ray; 1.90 A; A/D=439-764.
PDB; 4AJG; X-ray; 2.30 A; A/D=439-764.
PDB; 4AJM; X-ray; 2.40 A; A/D=439-764.
PDB; 4BBX; X-ray; 2.50 A; A/B=443-769.
PDB; 4DDL; X-ray; 2.07 A; A/B=442-779.
PDB; 4DFF; X-ray; 2.11 A; A/B=432-779.
PDB; 4FCB; X-ray; 2.10 A; A/B=439-779.
PDB; 4FCD; X-ray; 2.02 A; A/B=439-779.
PDB; 4HEU; X-ray; 2.00 A; A/B=442-759.
PDB; 4HF4; X-ray; 2.00 A; A/B=442-759.
PDB; 4LKQ; X-ray; 1.62 A; A/B=439-779.
PDB; 4LLJ; X-ray; 1.56 A; A/B=439-779.
PDB; 4LLK; X-ray; 1.55 A; A/B=439-779.
PDB; 4LLP; X-ray; 1.75 A; A/B=439-779.
PDB; 4LLX; X-ray; 1.75 A; A/B=439-779.
PDB; 4LM0; X-ray; 1.66 A; A/B=439-779.
PDB; 4LM1; X-ray; 1.60 A; A/B=439-779.
PDB; 4LM2; X-ray; 1.55 A; A/B=439-779.
PDB; 4LM3; X-ray; 1.49 A; A/B=439-779.
PDB; 4LM4; X-ray; 1.48 A; A/B=439-779.
PDB; 4MRW; X-ray; 1.96 A; A/B=439-779.
PDB; 4MRZ; X-ray; 1.58 A; A/B=439-779.
PDB; 4MS0; X-ray; 1.79 A; A/B=439-779.
PDB; 4MSA; X-ray; 1.62 A; A/B=439-779.
PDB; 4MSC; X-ray; 2.47 A; A/B=439-779.
PDB; 4MSE; X-ray; 2.81 A; A/B=439-779.
PDB; 4MSH; X-ray; 2.30 A; A/B=439-779.
PDB; 4MSN; X-ray; 2.30 A; A/B=439-779.
PDB; 4MUW; X-ray; 2.64 A; A/B=442-779.
PDB; 4MVH; X-ray; 2.50 A; A/B=442-779.
PDB; 4P0N; X-ray; 2.08 A; A/B=442-779.
PDB; 4P1R; X-ray; 2.24 A; A/B=442-779.
PDB; 4PHW; X-ray; 2.50 A; A/B=442-779.
PDB; 4TPM; X-ray; 2.77 A; A/B=442-779.
PDB; 4TPP; X-ray; 2.65 A; A/B=442-779.
PDB; 4WN1; X-ray; 3.13 A; A/B=439-779.
PDB; 4XY2; X-ray; 2.03 A; A/B=439-779.
PDB; 4YQH; X-ray; 2.31 A; A/B=439-759.
PDB; 4YS7; X-ray; 2.50 A; A/B=439-759.
PDB; 4ZO5; X-ray; 2.50 A; A/B=439-759.
PDB; 5AXP; X-ray; 1.95 A; A/B=442-779.
PDB; 5AXQ; X-ray; 1.77 A; A/B=442-779.
PDB; 5B4K; X-ray; 2.90 A; A/B=442-779.
PDB; 5B4L; X-ray; 2.40 A; A/B=442-779.
PDB; 5C1W; X-ray; 1.70 A; A/B=439-779.
PDB; 5C28; X-ray; 1.56 A; A/B=439-779.
PDB; 5C29; X-ray; 2.05 A; A/B=439-779.
PDB; 5C2A; X-ray; 2.00 A; A/B=439-779.
PDB; 5C2E; X-ray; 2.10 A; A/B=439-779.
PDB; 5C2H; X-ray; 2.09 A; A/B=439-779.
PDB; 5DH4; X-ray; 2.20 A; A/B=439-779.
PDB; 5DH5; X-ray; 2.00 A; A/B=439-779.
PDB; 5EDE; X-ray; 2.20 A; A/C/D=447-760, B=448-760.
PDB; 5EDG; X-ray; 2.30 A; A/B/C/D=447-760.
PDB; 5EDH; X-ray; 2.03 A; A/B/C/D=448-760.
PDB; 5EDI; X-ray; 2.20 A; A/B/C/D=442-760.
PDB; 5I2R; X-ray; 2.50 A; A/B/C/D=447-763.
PDB; 5K9R; X-ray; 2.70 A; A/B=448-759.
PDB; 5UWF; X-ray; 1.87 A; C/D=439-779.
PDB; 5XUI; X-ray; 2.77 A; A/B=439-779.
PDB; 5XUJ; X-ray; 2.44 A; A/B=439-779.
PDBsum; 1LRB; -.
PDBsum; 2OUN; -.
PDBsum; 2OUP; -.
PDBsum; 2OUQ; -.
PDBsum; 2OUR; -.
PDBsum; 2OUS; -.
PDBsum; 2OUU; -.
PDBsum; 2OUV; -.
PDBsum; 2OUY; -.
PDBsum; 2WEY; -.
PDBsum; 2Y0J; -.
PDBsum; 2ZMF; -.
PDBsum; 3SN7; -.
PDBsum; 3SNI; -.
PDBsum; 3SNL; -.
PDBsum; 3UI7; -.
PDBsum; 3UUO; -.
PDBsum; 3WI2; -.
PDBsum; 3WS8; -.
PDBsum; 3WS9; -.
PDBsum; 3WYK; -.
PDBsum; 3WYL; -.
PDBsum; 3WYM; -.
PDBsum; 4AEL; -.
PDBsum; 4AJD; -.
PDBsum; 4AJF; -.
PDBsum; 4AJG; -.
PDBsum; 4AJM; -.
PDBsum; 4BBX; -.
PDBsum; 4DDL; -.
PDBsum; 4DFF; -.
PDBsum; 4FCB; -.
PDBsum; 4FCD; -.
PDBsum; 4HEU; -.
PDBsum; 4HF4; -.
PDBsum; 4LKQ; -.
PDBsum; 4LLJ; -.
PDBsum; 4LLK; -.
PDBsum; 4LLP; -.
PDBsum; 4LLX; -.
PDBsum; 4LM0; -.
PDBsum; 4LM1; -.
PDBsum; 4LM2; -.
PDBsum; 4LM3; -.
PDBsum; 4LM4; -.
PDBsum; 4MRW; -.
PDBsum; 4MRZ; -.
PDBsum; 4MS0; -.
PDBsum; 4MSA; -.
PDBsum; 4MSC; -.
PDBsum; 4MSE; -.
PDBsum; 4MSH; -.
PDBsum; 4MSN; -.
PDBsum; 4MUW; -.
PDBsum; 4MVH; -.
PDBsum; 4P0N; -.
PDBsum; 4P1R; -.
PDBsum; 4PHW; -.
PDBsum; 4TPM; -.
PDBsum; 4TPP; -.
PDBsum; 4WN1; -.
PDBsum; 4XY2; -.
PDBsum; 4YQH; -.
PDBsum; 4YS7; -.
PDBsum; 4ZO5; -.
PDBsum; 5AXP; -.
PDBsum; 5AXQ; -.
PDBsum; 5B4K; -.
PDBsum; 5B4L; -.
PDBsum; 5C1W; -.
PDBsum; 5C28; -.
PDBsum; 5C29; -.
PDBsum; 5C2A; -.
PDBsum; 5C2E; -.
PDBsum; 5C2H; -.
PDBsum; 5DH4; -.
PDBsum; 5DH5; -.
PDBsum; 5EDE; -.
PDBsum; 5EDG; -.
PDBsum; 5EDH; -.
PDBsum; 5EDI; -.
PDBsum; 5I2R; -.
PDBsum; 5K9R; -.
PDBsum; 5UWF; -.
PDBsum; 5XUI; -.
PDBsum; 5XUJ; -.
ProteinModelPortal; Q9Y233; -.
SMR; Q9Y233; -.
BioGrid; 116057; 2.
IntAct; Q9Y233; 1.
STRING; 9606.ENSP00000438284; -.
BindingDB; Q9Y233; -.
ChEMBL; CHEMBL4409; -.
DrugBank; DB08384; 2-({4-[4-(pyridin-4-ylmethyl)-1H-pyrazol-3-yl]phenoxy}methyl)quinoline.
DrugBank; DB08387; 2-{[4-(1-methyl-4-pyridin-4-yl-1H-pyrazol-3-yl)phenoxy]methyl}quinoline.
DrugBank; DB08386; 2-{[4-(4-pyridin-4-yl-1H-pyrazol-3-yl)phenoxy]methyl}quinoline.
DrugBank; DB00201; Caffeine.
DrugBank; DB00975; Dipyridamole.
DrugBank; DB01113; Papaverine.
DrugBank; DB08811; Tofisopam.
DrugBank; DB08814; Triflusal.
GuidetoPHARMACOLOGY; 1310; -.
iPTMnet; Q9Y233; -.
PhosphoSitePlus; Q9Y233; -.
SwissPalm; Q9Y233; -.
BioMuta; PDE10A; -.
DMDM; 7993747; -.
PaxDb; Q9Y233; -.
PeptideAtlas; Q9Y233; -.
PRIDE; Q9Y233; -.
Ensembl; ENST00000366882; ENSP00000355847; ENSG00000112541. [Q9Y233-1]
Ensembl; ENST00000539869; ENSP00000438284; ENSG00000112541. [Q9Y233-2]
GeneID; 10846; -.
KEGG; hsa:10846; -.
UCSC; uc003quo.4; human. [Q9Y233-1]
CTD; 10846; -.
DisGeNET; 10846; -.
EuPathDB; HostDB:ENSG00000112541.13; -.
GeneCards; PDE10A; -.
HGNC; HGNC:8772; PDE10A.
HPA; CAB045998; -.
HPA; HPA047200; -.
MalaCards; PDE10A; -.
MIM; 610652; gene.
MIM; 616921; phenotype.
MIM; 616922; phenotype.
neXtProt; NX_Q9Y233; -.
OpenTargets; ENSG00000112541; -.
PharmGKB; PA33120; -.
eggNOG; KOG3689; Eukaryota.
eggNOG; ENOG410XRI7; LUCA.
GeneTree; ENSGT00760000119066; -.
HOGENOM; HOG000007068; -.
HOVERGEN; HBG082113; -.
KO; K18438; -.
OMA; LKACRNN; -.
OrthoDB; EOG091G037C; -.
PhylomeDB; Q9Y233; -.
TreeFam; TF316499; -.
BRENDA; 3.1.4.17; 2681.
Reactome; R-HSA-418457; cGMP effects.
Reactome; R-HSA-418555; G alpha (s) signalling events.
SABIO-RK; Q9Y233; -.
SIGNOR; Q9Y233; -.
UniPathway; UPA00762; UER00747.
UniPathway; UPA00763; UER00748.
ChiTaRS; PDE10A; human.
EvolutionaryTrace; Q9Y233; -.
GeneWiki; PDE10A; -.
GenomeRNAi; 10846; -.
PRO; PR:Q9Y233; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112541; -.
CleanEx; HS_PDE10A; -.
ExpressionAtlas; Q9Y233; baseline and differential.
Genevisible; Q9Y233; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; TAS:ProtInc.
GO; GO:0030552; F:cAMP binding; IDA:UniProtKB.
GO; GO:0030553; F:cGMP binding; NAS:UniProtKB.
GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IDA: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:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0043949; P:regulation of cAMP-mediated signaling; IEA:Ensembl.
GO; GO:0010738; P:regulation of protein kinase A signaling; IEA:Ensembl.
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.
PROSITE; PS00126; PDEASE_I_1; 1.
PROSITE; PS51845; PDEASE_I_2; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Alternative splicing; cAMP;
cAMP-binding; cGMP; cGMP-binding; Complete proteome; Cytoplasm;
Disease mutation; Hydrolase; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome; Repeat.
CHAIN 1 779 cAMP and cAMP-inhibited cGMP 3',5'-cyclic
phosphodiesterase 10A.
/FTId=PRO_0000198843.
DOMAIN 91 234 GAF 1.
DOMAIN 266 412 GAF 2.
DOMAIN 442 759 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
REGION 286 287 Allosteric effector binding.
REGION 330 331 Allosteric effector binding.
ACT_SITE 515 515 Proton donor. {ECO:0000250}.
METAL 519 519 Divalent metal cation 1.
METAL 553 553 Divalent metal cation 1.
METAL 554 554 Divalent metal cation 1.
METAL 554 554 Divalent metal cation 2.
METAL 664 664 Divalent metal cation 1.
BINDING 364 364 Allosteric effector.
BINDING 383 383 Allosteric effector.
BINDING 515 515 Substrate.
BINDING 716 716 Substrate.
VAR_SEQ 1 13 MRIEERKSQHLTG -> MEDGPSNNASCFRRLTECFLSPS
(in isoform PDE10A2).
{ECO:0000303|PubMed:10393245,
ECO:0000303|PubMed:10441464}.
/FTId=VSP_004601.
VARIANT 97 97 Y -> C (in IOLOD; decreased protein
abundance; dbSNP:rs778899140).
{ECO:0000269|PubMed:27058446}.
/FTId=VAR_076798.
VARIANT 106 106 A -> P (in IOLOD; decreased protein
abundance; dbSNP:rs875989839).
{ECO:0000269|PubMed:27058446}.
/FTId=VAR_076799.
VARIANT 290 290 F -> L (in ADSD2; no effect on basal
3',5'-cyclic-nucleotide phosphodiesterase
activity; the mutation severely disrupts
the stimulatory effect on the enzyme
activity mediated by cAMP binding;
dbSNP:rs875989841).
{ECO:0000269|PubMed:27058447}.
/FTId=VAR_076800.
VARIANT 303 303 L -> P.
/FTId=VAR_008797.
VARIANT 324 324 F -> L (in ADSD2; no effect on basal
3',5'-cyclic-nucleotide phosphodiesterase
activity; the mutation severely disrupts
the stimulatory effect on the enzyme
activity mediated by cAMP binding;
dbSNP:rs875989840).
{ECO:0000269|PubMed:27058447}.
/FTId=VAR_076801.
VARIANT 706 706 R -> K (in dbSNP:rs2224252).
/FTId=VAR_047822.
VARIANT 707 707 D -> N (in dbSNP:rs2860112).
/FTId=VAR_047823.
MUTAGEN 554 554 D->A: Loss of activity and of zinc
binding. {ECO:0000269|PubMed:17389385}.
MUTAGEN 554 554 D->N: Reduces activity 1000-fold.
{ECO:0000269|PubMed:17389385}.
CONFLICT 657 657 G -> S (in Ref. 4; CAG38804).
{ECO:0000305}.
HELIX 247 262 {ECO:0000244|PDB:2ZMF}.
HELIX 267 282 {ECO:0000244|PDB:2ZMF}.
STRAND 284 293 {ECO:0000244|PDB:2ZMF}.
TURN 294 297 {ECO:0000244|PDB:2ZMF}.
STRAND 298 304 {ECO:0000244|PDB:2ZMF}.
STRAND 323 325 {ECO:0000244|PDB:2ZMF}.
HELIX 329 337 {ECO:0000244|PDB:2ZMF}.
STRAND 341 344 {ECO:0000244|PDB:2ZMF}.
HELIX 346 348 {ECO:0000244|PDB:2ZMF}.
HELIX 355 360 {ECO:0000244|PDB:2ZMF}.
STRAND 367 374 {ECO:0000244|PDB:2ZMF}.
STRAND 377 387 {ECO:0000244|PDB:2ZMF}.
STRAND 390 392 {ECO:0000244|PDB:2ZMF}.
HELIX 395 419 {ECO:0000244|PDB:2ZMF}.
HELIX 443 449 {ECO:0000244|PDB:2OUR}.
HELIX 456 461 {ECO:0000244|PDB:2OUR}.
STRAND 464 466 {ECO:0000244|PDB:3UI7}.
HELIX 470 475 {ECO:0000244|PDB:2OUR}.
HELIX 476 488 {ECO:0000244|PDB:2OUR}.
TURN 490 492 {ECO:0000244|PDB:3SNI}.
HELIX 495 507 {ECO:0000244|PDB:2OUR}.
STRAND 513 516 {ECO:0000244|PDB:2OUR}.
HELIX 517 532 {ECO:0000244|PDB:2OUR}.
HELIX 533 537 {ECO:0000244|PDB:2OUR}.
HELIX 540 552 {ECO:0000244|PDB:2OUR}.
TURN 553 556 {ECO:0000244|PDB:2OUR}.
HELIX 562 567 {ECO:0000244|PDB:2OUR}.
HELIX 571 575 {ECO:0000244|PDB:2OUR}.
STRAND 577 579 {ECO:0000244|PDB:2OUS}.
HELIX 580 593 {ECO:0000244|PDB:2OUR}.
TURN 596 598 {ECO:0000244|PDB:3SN7}.
TURN 600 603 {ECO:0000244|PDB:2OUR}.
HELIX 606 622 {ECO:0000244|PDB:2OUR}.
HELIX 625 640 {ECO:0000244|PDB:2OUR}.
STRAND 646 648 {ECO:0000244|PDB:3WI2}.
HELIX 649 664 {ECO:0000244|PDB:2OUR}.
HELIX 666 669 {ECO:0000244|PDB:2OUR}.
HELIX 672 695 {ECO:0000244|PDB:2OUR}.
HELIX 702 704 {ECO:0000244|PDB:2OUR}.
HELIX 706 711 {ECO:0000244|PDB:2OUR}.
HELIX 712 722 {ECO:0000244|PDB:2OUR}.
HELIX 724 734 {ECO:0000244|PDB:2OUR}.
HELIX 736 738 {ECO:0000244|PDB:2OUR}.
HELIX 739 757 {ECO:0000244|PDB:2OUR}.
HELIX 762 765 {ECO:0000244|PDB:5C28}.
SEQUENCE 779 AA; 88412 MW; C5651BBB524A32B7 CRC64;
MRIEERKSQH LTGLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK NNKSEDESAP
KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNQLLLYELS SIIKIATKAD GFALYFLGEC
NNSLCIFTPP GIKEGKPRLI PAGPITQGTT VSAYVAKSRK TLLVEDILGD ERFPRGTGLE
SGTRIQSVLC LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA SVAIHQVQVC
RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF QVDHKNKELY
SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP RFNREVDLYT
GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN FKMFAVFCAL ALHCANMYHR
IRHSECIYRV TMEKLSYHSI CTSEEWQGLM QFTLPVRLCK EIELFHFDIG PFENMWPGIF
VYMVHRSCGT SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI LQNNHTLFTD
LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV SILQLEGHNI
FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLNNQS HRDRVIGLMM
TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP IPMMDRDKKD EVPQGQLGFY
NAVAIPCYTT LTQILPPTEP LLKACRDNLS QWEKVIRGEE TATWISSPSV AQKAAASED


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