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High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (HsPDE8B) (EC 3.1.4.53) (Cell proliferation-inducing gene 22 protein)

 PDE8B_HUMAN             Reviewed;         885 AA.
O95263; Q5J7V7; Q86XK8; Q8IUJ7; Q8IUJ8; Q8IUJ9; Q8IUK0; Q8N3T2;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
22-AUG-2003, sequence version 2.
20-JUN-2018, entry version 175.
RecName: Full=High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B;
Short=HsPDE8B;
EC=3.1.4.53 {ECO:0000269|PubMed:12681444};
AltName: Full=Cell proliferation-inducing gene 22 protein;
Name=PDE8B; ORFNames=PIG22;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 6), AND
TISSUE SPECIFICITY.
PubMed=12372422; DOI=10.1016/S0006-291X(02)02371-9;
Hayashi M., Shimada Y., Nishimura Y., Hama T., Tanaka T.;
"Genomic organization, chromosomal localization, and alternative
splicing of the human phosphodiesterase 8B gene.";
Biochem. Biophys. Res. Commun. 297:1253-1258(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), CATALYTIC
ACTIVITY, ENZYME REGULATION, AND TISSUE SPECIFICITY.
TISSUE=Thyroid;
PubMed=12681444; DOI=10.1016/S0898-6568(02)00146-8;
Gamanuma M., Yuasa K., Sasaki T., Sakurai N., Kotera J., Omori K.;
"Comparison of enzymatic characterization and gene organization of
cyclic nucleotide phosphodiesterase 8 family in humans.";
Cell. Signal. 15:565-574(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Kim J.W.;
"Identification of a human proliferation-inducing gene.";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Testis;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 227-885 (ISOFORM 1).
PubMed=9784418; DOI=10.1006/bbrc.1998.9379;
Hayashi M., Matsushima K., Ohashi H., Tsunoda H., Murase S.,
Kawarada Y., Tanaka T.;
"Molecular cloning and characterization of human PDE8B, a novel
thyroid-specific isozyme of 3',5'-cyclic nucleotide
phosphodiesterase.";
Biochem. Biophys. Res. Commun. 250:751-756(1998).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-885 (ISOFORM 1).
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
INVOLVEMENT IN ADSD1.
PubMed=20085714; DOI=10.1016/j.ajhg.2009.12.003;
Appenzeller S., Schirmacher A., Halfter H., Baumer S., Pendziwiat M.,
Timmerman V., De Jonghe P., Fekete K., Stogbauer F., Ludemann P.,
Hund M., Quabius E.S., Ringelstein E.B., Kuhlenbaumer G.;
"Autosomal-dominant striatal degeneration is caused by a mutation in
the phosphodiesterase 8B gene.";
Am. J. Hum. Genet. 86:83-87(2010).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
VARIANT PPNAD3 PRO-305, AND CHARACTERIZATION OF VARIANT PPNAD3
PRO-305.
PubMed=18431404; DOI=10.1038/ejhg.2008.85;
Horvath A., Giatzakis C., Tsang K., Greene E., Osorio P., Boikos S.,
Libe R., Patronas Y., Robinson-White A., Remmers E., Bertherat J.,
Nesterova M., Stratakis C.A.;
"A cAMP-specific phosphodiesterase (PDE8B) that is mutated in adrenal
hyperplasia is expressed widely in human and mouse tissues: a novel
PDE8B isoform in human adrenal cortex.";
Eur. J. Hum. Genet. 16:1245-1253(2008).
-!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
regulator of many important physiological processes. May be
involved in specific signaling in the thyroid gland.
-!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
adenosine 5'-phosphate. {ECO:0000269|PubMed:12681444}.
-!- 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};
-!- ENZYME REGULATION: Inhibited by dipyridimole. Insensitive to
selective PDE inhibitors including rolipram and milrinone as well
as to the non-selective inhibitor, IBMX. Unaffected by cGMP.
{ECO:0000269|PubMed:12681444}.
-!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
3',5'-cyclic AMP: step 1/1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=PDE8B1;
IsoId=O95263-1; Sequence=Displayed;
Note=Major isoform.;
Name=2; Synonyms=PDE8B2, PDE8B3;
IsoId=O95263-2; Sequence=VSP_008084;
Name=3; Synonyms=PDE8B3;
IsoId=O95263-3; Sequence=VSP_008085;
Name=4; Synonyms=PDE8B4;
IsoId=O95263-4; Sequence=VSP_008082;
Name=5;
IsoId=O95263-5; Sequence=VSP_008081;
Note=No experimental confirmation available.;
Name=6; Synonyms=PDE8B2;
IsoId=O95263-6; Sequence=VSP_008083;
-!- TISSUE SPECIFICITY: Abundantly expressed in the thyroid. Also very
weakly expressed in brain, spinal cord and placenta. In the
thyroid isoform 1 predominates, and isoforms 2 and 6 are also
highly expressed. In the placenta isoforms 1 and 2 are expressed
equally. In the brain isoform 2 predominates.
{ECO:0000269|PubMed:12372422, ECO:0000269|PubMed:12681444}.
-!- DOMAIN: Composed of a C-terminal catalytic domain containing two
putative divalent metal sites and an N-terminal regulatory domain.
-!- DISEASE: Striatal degeneration, autosomal dominant 1 (ADSD1)
[MIM:609161]: A movement disorder affecting the striatal part of
the basal ganglia and characterized by bradykinesia, dysarthria
and muscle rigidity. These symptoms resemble idiopathic Parkinson
disease, but tremor is not present. {ECO:0000269|PubMed:20085714}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Primary pigmented nodular adrenocortical disease 3
(PPNAD3) [MIM:614190]: A rare bilateral adrenal defect causing
ACTH-independent Cushing syndrome. Macroscopic appearance of the
adrenals is characteristic with small pigmented micronodules
observed in the cortex. Adrenal glands show overall normal size
and weight, and multiple small yellow-to-dark brown nodules
surrounded by a cortex with a uniform appearance. Microscopically,
there are moderate diffuse cortical hyperplasia with mostly
nonpigmented nodules, multiple capsular deficits and massive
circumscribed and infiltrating extra-adrenal cortical excrescences
with micronodules. Clinical manifestations of Cushing syndrome
include facial and truncal obesity, abdominal striae, muscular
weakness, osteoporosis, arterial hypertension, diabetes.
{ECO:0000269|PubMed:18431404}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE8 subfamily. {ECO:0000305}.
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EMBL; AY129948; AAN71723.1; -; mRNA.
EMBL; AY129949; AAN71724.1; -; mRNA.
EMBL; AY129950; AAN71725.1; -; Genomic_DNA.
EMBL; AY129950; AAN71726.1; -; Genomic_DNA.
EMBL; AY129950; AAN71727.1; -; Genomic_DNA.
EMBL; AB085824; BAC53762.1; -; mRNA.
EMBL; AB085825; BAC53763.1; -; mRNA.
EMBL; AB085826; BAC53764.1; -; mRNA.
EMBL; AB085827; BAC53765.1; -; mRNA.
EMBL; AY423729; AAS00492.1; -; mRNA.
EMBL; CH471084; EAW95803.1; -; Genomic_DNA.
EMBL; BC043209; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF079529; AAC69564.2; -; mRNA.
EMBL; AL831924; CAD38584.1; -; mRNA.
CCDS; CCDS34190.1; -. [O95263-3]
CCDS; CCDS34191.1; -. [O95263-6]
CCDS; CCDS34192.1; -. [O95263-2]
CCDS; CCDS34193.1; -. [O95263-4]
CCDS; CCDS4037.1; -. [O95263-1]
PIR; JE0293; JE0293.
RefSeq; NP_001025022.1; NM_001029851.2. [O95263-2]
RefSeq; NP_001025023.1; NM_001029852.2. [O95263-3]
RefSeq; NP_001025024.1; NM_001029853.2. [O95263-4]
RefSeq; NP_001025025.1; NM_001029854.2. [O95263-6]
RefSeq; NP_003710.1; NM_003719.3. [O95263-1]
UniGene; Hs.584830; -.
ProteinModelPortal; O95263; -.
SMR; O95263; -.
BioGrid; 114177; 1.
IntAct; O95263; 1.
STRING; 9606.ENSP00000264917; -.
BindingDB; O95263; -.
ChEMBL; CHEMBL4408; -.
DrugBank; DB00201; Caffeine.
GuidetoPHARMACOLOGY; 1308; -.
iPTMnet; O95263; -.
PhosphoSitePlus; O95263; -.
BioMuta; PDE8B; -.
UCD-2DPAGE; O95263; -.
MaxQB; O95263; -.
PaxDb; O95263; -.
PeptideAtlas; O95263; -.
PRIDE; O95263; -.
ProteomicsDB; 50759; -.
ProteomicsDB; 50760; -. [O95263-2]
ProteomicsDB; 50761; -. [O95263-3]
ProteomicsDB; 50762; -. [O95263-4]
ProteomicsDB; 50763; -. [O95263-5]
ProteomicsDB; 50764; -. [O95263-6]
DNASU; 8622; -.
Ensembl; ENST00000264917; ENSP00000264917; ENSG00000113231. [O95263-1]
Ensembl; ENST00000333194; ENSP00000331336; ENSG00000113231. [O95263-3]
Ensembl; ENST00000340978; ENSP00000345446; ENSG00000113231. [O95263-6]
Ensembl; ENST00000342343; ENSP00000345646; ENSG00000113231. [O95263-4]
Ensembl; ENST00000346042; ENSP00000330428; ENSG00000113231. [O95263-2]
Ensembl; ENST00000505283; ENSP00000423461; ENSG00000113231. [O95263-5]
GeneID; 8622; -.
KEGG; hsa:8622; -.
UCSC; uc003kfa.4; human. [O95263-1]
CTD; 8622; -.
DisGeNET; 8622; -.
EuPathDB; HostDB:ENSG00000113231.13; -.
GeneCards; PDE8B; -.
H-InvDB; HIX0004971; -.
HGNC; HGNC:8794; PDE8B.
HPA; HPA036911; -.
HPA; HPA036912; -.
MalaCards; PDE8B; -.
MIM; 603390; gene.
MIM; 609161; phenotype.
MIM; 614190; phenotype.
neXtProt; NX_O95263; -.
OpenTargets; ENSG00000113231; -.
Orphanet; 228169; Autosomal dominant striatal neurodegeneration.
Orphanet; 189439; Primary pigmented nodular adrenocortical disease.
PharmGKB; PA33142; -.
eggNOG; KOG1229; Eukaryota.
eggNOG; ENOG410XP9B; LUCA.
GeneTree; ENSGT00760000118889; -.
HOVERGEN; HBG053544; -.
KO; K18437; -.
OMA; PHSFRYK; -.
OrthoDB; EOG091G0337; -.
PhylomeDB; O95263; -.
TreeFam; TF314638; -.
BRENDA; 3.1.4.53; 2681.
Reactome; R-HSA-418555; G alpha (s) signalling events.
UniPathway; UPA00762; UER00747.
ChiTaRS; PDE8B; human.
GeneWiki; PDE8B; -.
GenomeRNAi; 8622; -.
PRO; PR:O95263; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113231; -.
CleanEx; HS_PDE8B; -.
ExpressionAtlas; O95263; baseline and differential.
Genevisible; O95263; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; TAS:Reactome.
GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0009187; P:cyclic nucleotide metabolic process; NAS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
CDD; cd00077; HDc; 1.
CDD; cd00130; PAS; 1.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
InterPro; IPR013938; PDEase_PDE8.
Pfam; PF13426; PAS_9; 1.
Pfam; PF08629; PDE8; 1.
Pfam; PF00233; PDEase_I; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00471; HDc; 1.
SMART; SM00091; PAS; 1.
SUPFAM; SSF55785; SSF55785; 1.
TIGRFAMs; TIGR00229; sensory_box; 1.
PROSITE; PS50112; PAS; 1.
PROSITE; PS00126; PDEASE_I_1; 1.
PROSITE; PS51845; PDEASE_I_2; 1.
1: Evidence at protein level;
Alternative splicing; cAMP; Complete proteome; Cushing syndrome;
Disease mutation; Hydrolase; Metal-binding; Phosphoprotein;
Reference proteome.
CHAIN 1 885 High affinity cAMP-specific and IBMX-
insensitive 3',5'-cyclic
phosphodiesterase 8B.
/FTId=PRO_0000198840.
DOMAIN 267 338 PAS. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 539 875 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
ACT_SITE 615 615 Proton donor.
{ECO:0000250|UniProtKB:O76083}.
METAL 619 619 Divalent metal cation 1; via tele
nitrogen. {ECO:0000250|UniProtKB:O60658}.
METAL 655 655 Divalent metal cation 1; via tele
nitrogen. {ECO:0000250|UniProtKB:O60658}.
METAL 656 656 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O60658}.
METAL 656 656 Divalent metal cation 2.
{ECO:0000250|UniProtKB:O60658}.
METAL 781 781 Divalent metal cation 1.
{ECO:0000250|UniProtKB:O60658}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q4S1}.
VAR_SEQ 1 535 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3}.
/FTId=VSP_008081.
VAR_SEQ 114 133 Missing (in isoform 4).
{ECO:0000303|PubMed:12681444}.
/FTId=VSP_008082.
VAR_SEQ 293 389 Missing (in isoform 2).
{ECO:0000303|PubMed:12372422,
ECO:0000303|PubMed:12681444}.
/FTId=VSP_008084.
VAR_SEQ 293 339 Missing (in isoform 6).
{ECO:0000303|PubMed:12372422}.
/FTId=VSP_008083.
VAR_SEQ 456 510 Missing (in isoform 3).
{ECO:0000303|PubMed:12681444}.
/FTId=VSP_008085.
VARIANT 305 305 H -> P (in PPNAD3; shows significantly
higher cyclic AMP levels after
transfection with the mutant protein than
after transfection with the wild-type,
indicating an impaired ability of the
mutant protein to degrade cAMP;
dbSNP:rs121918360).
{ECO:0000269|PubMed:18431404}.
/FTId=VAR_066503.
CONFLICT 147 147 G -> R (in Ref. 7; CAD38584).
{ECO:0000305}.
SEQUENCE 885 AA; 98979 MW; DB4F763E51F745A3 CRC64;
MGCAPSIHVS QSGVIYCRDS DESSSPRQTT SVSQGPAAPL PGLFVQTDAA DAIPPSRASG
PPSVARVRRA RTELGSGSSA GSAAPAATTS RGRRRHCCSS AEAETQTCYT SVKQVSSAEV
RIGPMRLTQD PIQVLLIFAK EDSQSDGFWW ACDRAGYRCN IARTPESALE CFLDKHHEII
VIDHRQTQNF DAEAVCRSIR ATNPSEHTVI LAVVSRVSDD HEEASVLPLL HAGFNRRFME
NSSIIACYNE LIQIEHGEVR SQFKLRACNS VFTALDHCHE AIEITSDDHV IQYVNPAFER
MMGYHKGELL GKELADLPKS DKNRADLLDT INTCIKKGKE WQGVYYARRK SGDSIQQHVK
ITPVIGQGGK IRHFVSLKKL CCTTDNNKQI HKIHRDSGDN SQTEPHSFRY KNRRKESIDV
KSISSRGSDA PSLQNRRYPS MARIHSMTIE APITKVINII NAAQENSPVT VAEALDRVLE
ILRTTELYSP QLGTKDEDPH TSDLVGGLMT DGLRRLSGNE YVFTKNVHQS HSHLAMPITI
NDVPPCISQL LDNEESWDFN IFELEAITHK RPLVYLGLKV FSRFGVCEFL NCSETTLRAW
FQVIEANYHS SNAYHNSTHA ADVLHATAFF LGKERVKGSL DQLDEVAALI AATVHDVDHP
GRTNSFLCNA GSELAVLYND TAVLESHHTA LAFQLTVKDT KCNIFKNIDR NHYRTLRQAI
IDMVLATEMT KHFEHVNKFV NSINKPMAAE IEGSDCECNP AGKNFPENQI LIKRMMIKCA
DVANPCRPLD LCIEWAGRIS EEYFAQTDEE KRQGLPVVMP VFDRNTCSIP KSQISFIDYF
ITDMFDAWDA FAHLPALMQH LADNYKHWKT LDDLKCKSLR LPSDS


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Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
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IBAN lautet DE8839050000107569353
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Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
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San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
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GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
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София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
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GENTAUR Poland Sp. z o.o.


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TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

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GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
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Fax 02 36 00 65 94
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