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Short transient receptor potential channel 3 (TrpC3) (Transient receptor protein 3) (TRP-3) (hTrp-3) (hTrp3)

 TRPC3_HUMAN             Reviewed;         836 AA.
Q13507; A7VJS1; E9PCJ9; O00593; Q15660; Q52M35; Q5G1L5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
03-MAY-2011, sequence version 3.
25-OCT-2017, entry version 168.
RecName: Full=Short transient receptor potential channel 3;
Short=TrpC3;
AltName: Full=Transient receptor protein 3;
Short=TRP-3;
Short=hTrp-3;
Short=hTrp3;
Name=TRPC3; Synonyms=TRP3;
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 3), AND FUNCTION.
TISSUE=Embryonic kidney;
PubMed=8646775; DOI=10.1016/S0092-8674(00)81233-7;
Zhu X., Jiang M., Peyton M., Boulay G., Hurst R., Stefani E.,
Birnbaumer L.;
"trp, a novel mammalian gene family essential for agonist-activated
capacitative Ca2+ entry.";
Cell 85:661-671(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=9215637; DOI=10.1016/S0092-8674(00)80302-5;
Xu X.-Z.S., Li H.-S., Guggino W.B., Montell C.;
"Coassembly of TRP and TRPL produces a distinct store-operated
conductance.";
Cell 89:1155-1164(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=15728370; DOI=10.1073/pnas.0409908102;
Yildirim E., Kawasaki B.T., Birnbaumer L.;
"Molecular cloning of TRPC3a, an N-terminally extended, store-operated
variant of the human C3 transient receptor potential channel.";
Proc. Natl. Acad. Sci. U.S.A. 102:3307-3311(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Brain;
Yamazaki D., Yamamura H., Ohya S., Asai K., Imaizumi Y.;
"Molecular cloning of novel TRPC3 isoform.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
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 [MRNA] OF 620-735 (ISOFORMS 1/2/3).
TISSUE=Fetal brain;
PubMed=7568191; DOI=10.1073/pnas.92.21.9652;
Wes P.D., Chevesich J., Jeromin A., Rosenberg C., Stetten G.,
Montell C.;
"TRPC1, a human homolog of a Drosophila store-operated channel.";
Proc. Natl. Acad. Sci. U.S.A. 92:9652-9656(1995).
[8]
GLYCOSYLATION AT ASN-404, AND MEMBRANE TOPOLOGY.
PubMed=9535843; DOI=10.1074/jbc.273.15.8675;
Vannier B., Zhu X., Brown D., Birnbaumer L.;
"The membrane topology of human transient receptor potential 3 as
inferred from glycosylation-scanning mutagenesis and epitope
immunocytochemistry.";
J. Biol. Chem. 273:8675-8679(1998).
[9]
FUNCTION.
PubMed=9417057; DOI=10.1074/jbc.273.1.133;
Zhu X., Jiang M., Birnbaumer L.;
"Receptor-activated Ca2+ influx via human Trp3 stably expressed in
human embryonic kidney (HEK)293 cells. Evidence for a non-capacitative
Ca2+ entry.";
J. Biol. Chem. 273:133-142(1998).
[10]
INTERACTION WITH ITPR1.
PubMed=9853757; DOI=10.1038/24890;
Kiselyov K., Xu X., Mozhayeva G., Kuo T., Pessah I., Mignery G.,
Zhu X., Birnbaumer L., Muallem S.;
"Functional interaction between InsP3 receptors and store-operated
Htrp3 channels.";
Nature 396:478-482(1998).
[11]
FUNCTION.
PubMed=9930701; DOI=10.1038/16711;
Hofmann T., Obukhov A.G., Schaefer M., Harteneck C., Gudermann T.,
Schultz G.;
"Direct activation of human TRPC6 and TRPC3 channels by
diacylglycerol.";
Nature 397:259-263(1999).
[12]
INTERACTION WITH ITPR3.
PubMed=10611319; DOI=10.1073/pnas.96.26.14955;
Boulay G., Brown D.M., Qin N., Jiang M., Dietrich A., Zhu M.X.,
Chen Z., Birnbaumer M., Mikoshiba K., Birnbaumer L.;
"Modulation of Ca(2+) entry by polypeptides of the inositol 1,4, 5-
trisphosphate receptor (IP3R) that bind transient receptor potential
(TRP): evidence for roles of TRP and IP3R in store depletion-activated
Ca(2+) entry.";
Proc. Natl. Acad. Sci. U.S.A. 96:14955-14960(1999).
[13]
INTERACTION WITH MX1.
PubMed=15757897; DOI=10.1074/jbc.M500391200;
Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N.,
St-Hilaire M., Pinard M., Boulay G.;
"MxA, a member of the dynamin superfamily, interacts with the ankyrin-
like repeat domain of TRPC.";
J. Biol. Chem. 280:19393-19400(2005).
[14]
INTERACTION WITH RNF24.
PubMed=17850865; DOI=10.1016/j.ceca.2007.07.009;
Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.;
"RNF24, a new TRPC interacting protein, causes the intracellular
retention of TRPC.";
Cell Calcium 43:432-443(2008).
[15]
INTERACTION WITH JPH2, AND FUNCTION.
PubMed=20095964; DOI=10.1042/BJ20091225;
Woo J.S., Hwang J.H., Ko J.K., Weisleder N., Kim do H., Ma J.,
Lee E.H.;
"S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletal
muscle.";
Biochem. J. 427:125-134(2010).
[16]
ELECTRON MICROSCOPY (15 ANGSTROMS), AND MEMBRANE TOPOLOGY.
PubMed=17258231; DOI=10.1016/j.jmb.2006.12.043;
Mio K., Ogura T., Kiyonaka S., Hiroaki Y., Tanimura Y., Fujiyoshi Y.,
Mori Y., Sato C.;
"The TRPC3 channel has a large internal chamber surrounded by signal
sensing antennas.";
J. Mol. Biol. 367:373-383(2007).
[17]
INVOLVEMENT IN SCA41, VARIANT SCA41 HIS-762, AND CHARACTERIZATION OF
VARIANT SCA41 HIS-762.
PubMed=25477146; DOI=10.1002/mds.26096;
Fogel B.L., Hanson S.M., Becker E.B.;
"Do mutations in the murine ataxia gene TRPC3 cause cerebellar ataxia
in humans?";
Mov. Disord. 30:284-286(2015).
-!- FUNCTION: Thought to form a receptor-activated non-selective
calcium permeant cation channel. Probably is operated by a
phosphatidylinositol second messenger system activated by receptor
tyrosine kinases or G-protein coupled receptors. Activated by
diacylglycerol (DAG) in a membrane-delimited fashion,
independently of protein kinase C, and by inositol 1,4,5-
triphosphate receptors (ITPR) with bound IP3. May also be
activated by internal calcium store depletion.
{ECO:0000269|PubMed:20095964, ECO:0000269|PubMed:8646775,
ECO:0000269|PubMed:9417057, ECO:0000269|PubMed:9930701}.
-!- SUBUNIT: Interacts with TRPC1, ITPR1, ITPR3, MX1 and RNF24.
Interacts with JPH2; the interaction is involved in maintaining
Ca(2+) homeostasis in skeletal muscle and is mediated by JPH2
'Ser-165' phosphorylation. {ECO:0000269|PubMed:10611319,
ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:17850865,
ECO:0000269|PubMed:20095964, ECO:0000269|PubMed:9853757}.
-!- INTERACTION:
Q14573:ITPR3; NbExp=5; IntAct=EBI-520807, EBI-351055;
P20591:MX1; NbExp=2; IntAct=EBI-520807, EBI-929476;
Q96D31:ORAI1; NbExp=2; IntAct=EBI-520807, EBI-2291476;
P10686:Plcg1 (xeno); NbExp=2; IntAct=EBI-520807, EBI-520788;
P05480:Src (xeno); NbExp=4; IntAct=EBI-15563545, EBI-298680;
Q80UE6:Wnk4 (xeno); NbExp=2; IntAct=EBI-15563545, EBI-295378;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q13507-1; Sequence=Displayed;
Name=2;
IsoId=Q13507-2; Sequence=VSP_042446;
Name=3;
IsoId=Q13507-3; Sequence=VSP_042445;
-!- TISSUE SPECIFICITY: Expressed predominantly in brain and at much
lower levels in ovary, colon, small intestine, lung, prostate,
placenta and testis.
-!- DISEASE: Spinocerebellar ataxia 41 (SCA41) [MIM:616410]: A form of
spinocerebellar ataxia, a clinically and genetically heterogeneous
group of cerebellar disorders. Patients show progressive
incoordination of gait and often poor coordination of hands,
speech and eye movements, due to degeneration of the cerebellum
with variable involvement of the brainstem and spinal cord.
{ECO:0000269|PubMed:25477146}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
STrpC subfamily. TRPC3 sub-subfamily. {ECO:0000305}.
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EMBL; U47050; AAC51653.1; -; mRNA.
EMBL; Y13758; CAA74083.1; -; mRNA.
EMBL; AY865574; AAW62292.1; -; mRNA.
EMBL; AB255424; BAF76424.1; -; mRNA.
EMBL; AC079341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC093682; AAH93682.1; -; mRNA.
EMBL; BC093684; AAH93684.1; -; mRNA.
EMBL; X89068; CAA61448.1; -; mRNA.
CCDS; CCDS3725.1; -. [Q13507-3]
CCDS; CCDS47130.1; -. [Q13507-2]
RefSeq; NP_001124170.1; NM_001130698.1. [Q13507-2]
RefSeq; NP_003296.1; NM_003305.2. [Q13507-3]
UniGene; Hs.150981; -.
ProteinModelPortal; Q13507; -.
BioGrid; 113073; 14.
CORUM; Q13507; -.
DIP; DIP-34311N; -.
IntAct; Q13507; 8.
STRING; 9606.ENSP00000368966; -.
BindingDB; Q13507; -.
ChEMBL; CHEMBL2417348; -.
GuidetoPHARMACOLOGY; 488; -.
TCDB; 1.A.4.1.4; the transient receptor potential ca(2+) channel (trp-cc) family.
iPTMnet; Q13507; -.
PhosphoSitePlus; Q13507; -.
BioMuta; TRPC3; -.
DMDM; 332278239; -.
PaxDb; Q13507; -.
PeptideAtlas; Q13507; -.
PRIDE; Q13507; -.
Ensembl; ENST00000264811; ENSP00000264811; ENSG00000138741. [Q13507-3]
Ensembl; ENST00000379645; ENSP00000368966; ENSG00000138741. [Q13507-2]
GeneID; 7222; -.
KEGG; hsa:7222; -.
UCSC; uc003ief.3; human. [Q13507-1]
CTD; 7222; -.
DisGeNET; 7222; -.
EuPathDB; HostDB:ENSG00000138741.10; -.
GeneCards; TRPC3; -.
HGNC; HGNC:12335; TRPC3.
HPA; HPA037969; -.
MalaCards; TRPC3; -.
MIM; 602345; gene.
MIM; 616410; phenotype.
neXtProt; NX_Q13507; -.
OpenTargets; ENSG00000138741; -.
PharmGKB; PA37008; -.
eggNOG; KOG3609; Eukaryota.
eggNOG; ENOG410XQ0Y; LUCA.
GeneTree; ENSGT00760000119180; -.
HOGENOM; HOG000020590; -.
HOVERGEN; HBG068337; -.
InParanoid; Q13507; -.
KO; K04966; -.
OMA; CMEKQRH; -.
OrthoDB; EOG091G01FB; -.
TreeFam; TF313147; -.
Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
Reactome; R-HSA-3295583; TRP channels.
Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
SIGNOR; Q13507; -.
ChiTaRS; TRPC3; human.
GeneWiki; TRPC3; -.
GenomeRNAi; 7222; -.
PRO; PR:Q13507; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138741; -.
CleanEx; HS_TRPC3; -.
ExpressionAtlas; Q13507; baseline and differential.
Genevisible; Q13507; HS.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:BHF-UCL.
GO; GO:0015279; F:store-operated calcium channel activity; TAS:ProtInc.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; TAS:ProtInc.
GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
GO; GO:0007602; P:phototransduction; TAS:ProtInc.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:UniProtKB.
GO; GO:1903244; P:positive regulation of cardiac muscle hypertrophy in response to stress; IDA:BHF-UCL.
GO; GO:0033198; P:response to ATP; IDA:UniProtKB.
GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
GO; GO:0007338; P:single fertilization; IBA:GO_Central.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR004729; TRP_channel.
InterPro; IPR013555; TRP_dom.
InterPro; IPR005459; TRPC3_channel.
InterPro; IPR002153; TRPC_channel.
PANTHER; PTHR10117; PTHR10117; 1.
PANTHER; PTHR10117:SF8; PTHR10117:SF8; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF08344; TRP_2; 1.
PRINTS; PR01097; TRNSRECEPTRP.
PRINTS; PR01644; TRPCHANNEL3.
SMART; SM00248; ANK; 3.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Calcium; Calcium channel;
Calcium transport; Complete proteome; Disease mutation; Glycoprotein;
Ion channel; Ion transport; Membrane; Neurodegeneration;
Reference proteome; Repeat; Spinocerebellar ataxia; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 836 Short transient receptor potential
channel 3.
/FTId=PRO_0000215310.
TOPO_DOM 1 369 Cytoplasmic. {ECO:0000255}.
TRANSMEM 370 390 Helical. {ECO:0000255}.
TOPO_DOM 391 418 Extracellular. {ECO:0000255}.
TRANSMEM 419 439 Helical. {ECO:0000255}.
TOPO_DOM 440 451 Cytoplasmic. {ECO:0000255}.
TRANSMEM 452 472 Helical. {ECO:0000255}.
TOPO_DOM 473 523 Extracellular. {ECO:0000255}.
TRANSMEM 524 544 Helical. {ECO:0000255}.
TOPO_DOM 545 567 Cytoplasmic. {ECO:0000255}.
TRANSMEM 568 588 Helical. {ECO:0000255}.
TOPO_DOM 589 637 Extracellular. {ECO:0000255}.
TRANSMEM 638 658 Helical. {ECO:0000255}.
TOPO_DOM 659 836 Cytoplasmic. {ECO:0000255}.
REPEAT 26 55 ANK 1.
REPEAT 61 90 ANK 2.
REPEAT 92 118 ANK 3.
REPEAT 147 176 ANK 4.
REGION 765 785 Binds to IP3R3.
CARBOHYD 404 404 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9535843}.
VAR_SEQ 1 1 M -> MSTKVRKCKEQARVTFPAPEEEEDEGEDEGAEPQRR
RRGWRGVNGGLEPRSAPSQREPHGYCPPPFSHGPDLSMEGS
PSLRRMTVM (in isoform 2).
{ECO:0000303|PubMed:15728370}.
/FTId=VSP_042446.
VAR_SEQ 1 1 M -> MEGSPSLRRMTVM (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8646775,
ECO:0000303|PubMed:9215637,
ECO:0000303|Ref.4}.
/FTId=VSP_042445.
VARIANT 762 762 R -> H (in SCA41; toxic gain of function
effect). {ECO:0000269|PubMed:25477146}.
/FTId=VAR_073835.
CONFLICT 525 525 I -> L (in Ref. 4; BAF76424).
{ECO:0000305}.
CONFLICT 662 662 Y -> C (in Ref. 4; BAF76424).
{ECO:0000305}.
SEQUENCE 836 AA; 96009 MW; 4179CB3DA8B3F508 CRC64;
MREKGRRQAV RGPAFMFNDR GTSLTAEEER FLDAAEYGNI PVVRKMLEES KTLNVNCVDY
MGQNALQLAV GNEHLEVTEL LLKKENLARI GDALLLAISK GYVRIVEAIL NHPGFAASKR
LTLSPCEQEL QDDDFYAYDE DGTRFSPDIT PIILAAHCQK YEVVHMLLMK GARIERPHDY
FCKCGDCMEK QRHDSFSHSR SRINAYKGLA SPAYLSLSSE DPVLTALELS NELAKLANIE
KEFKNDYRKL SMQCKDFVVG VLDLCRDSEE VEAILNGDLE SAEPLEVHRH KASLSRVKLA
IKYEVKKFVA HPNCQQQLLT IWYENLSGLR EQTIAIKCLV VLVVALGLPF LAIGYWIAPC
SRLGKILRSP FMKFVAHAAS FIIFLGLLVF NASDRFEGIT TLPNITVTDY PKQIFRVKTT
QFTWTEMLIM VWVLGMMWSE CKELWLEGPR EYILQLWNVL DFGMLSIFIA AFTARFLAFL
QATKAQQYVD SYVQESDLSE VTLPPEIQYF TYARDKWLPS DPQIISEGLY AIAVVLSFSR
IAYILPANES FGPLQISLGR TVKDIFKFMV LFIMVFFAFM IGMFILYSYY LGAKVNAAFT
TVEESFKTLF WSIFGLSEVT SVVLKYDHKF IENIGYVLYG IYNVTMVVVL LNMLIAMINS
SYQEIEDDSD VEWKFARSKL WLSYFDDGKT LPPPFSLVPS PKSFVYFIMR IVNFPKCRRR
RLQKDIEMGM GNSKSRLNLF TQSNSRVFES HSFNSILNQP TRYQQIMKRL IKRYVLKAQV
DKENDEVNEG ELKEIKQDIS SLRYELLEDK SQATEELAIL IHKLSEKLNP SMLRCE


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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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