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Short transient receptor potential channel 5 (TrpC5) (Transient receptor protein 5) (TRP-5) (hTRP-5) (hTRP5)

 TRPC5_HUMAN             Reviewed;         973 AA.
Q9UL62; B2RP53; O75233; Q5JXY8; Q9Y514;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 155.
RecName: Full=Short transient receptor potential channel 5;
Short=TrpC5;
AltName: Full=Transient receptor protein 5;
Short=TRP-5;
Short=hTRP-5;
Short=hTRP5;
Name=TRPC5; Synonyms=TRP5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal brain;
PubMed=10493832; DOI=10.1006/geno.1999.5924;
Sossey-Alaoui K., Lyon J.A., Jones L., Abidi F.E., Hartung A.J.,
Hane B., Schwartz C.E., Stevenson R.E., Srivastava A.K.;
"Molecular cloning and characterization of TRPC5 (HTRP5), the human
homologue of a mouse brain receptor-activated capacitative Ca(2+)
entry channel.";
Genomics 60:330-340(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
TISSUE SPECIFICITY.
PubMed=9687496; DOI=10.1093/emboj/17.15.4274;
Philipp S., Hambrecht J., Braslavski L., Schroth G., Freichel M.,
Murakami M., Cavalie A., Flockerzi V.;
"A novel capacitative calcium entry channel expressed in excitable
cells.";
EMBO J. 17:4274-4282(1998).
[6]
SUBUNIT.
PubMed=12032305; DOI=10.1073/pnas.102596199;
Hofmann T., Schaefer M., Schultz G., Gudermann T.;
"Subunit composition of mammalian transient receptor potential
channels in living cells.";
Proc. Natl. Acad. Sci. U.S.A. 99:7461-7466(2002).
[7]
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).
[8]
INTERACTION WITH CABP1.
PubMed=15895247; DOI=10.1007/s00424-005-1419-1;
Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K.,
Zhu M.X.;
"Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus
oocytes.";
Pflugers Arch. 450:345-354(2005).
[9]
FUNCTION AS CALCIUM CHANNEL, ENZYME REGULATION, AND SUBCELLULAR
LOCATION.
PubMed=16284075; DOI=10.1113/jphysiol.2005.097998;
Shimizu S., Yoshida T., Wakamori M., Ishii M., Okada T., Takahashi M.,
Seto M., Sakurada K., Kiuchi Y., Mori Y.;
"Ca2+-calmodulin-dependent myosin light chain kinase is essential for
activation of TRPC5 channels expressed in HEK293 cells.";
J. Physiol. (Lond.) 570:219-235(2006).
[10]
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).
[11]
INTERACTION WITH SESTD1.
PubMed=20164195; DOI=10.1074/jbc.M109.068304;
Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H.,
Strubing C.;
"The phospholipid-binding protein SESTD1 is a novel regulator of the
transient receptor potential channels TRPC4 and TRPC5.";
J. Biol. Chem. 285:12426-12434(2010).
[12]
VARIANT THR-667.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
-!- 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. Has also been
shown to be calcium-selective (By similarity). May also be
activated by intracellular calcium store depletion. {ECO:0000250,
ECO:0000269|PubMed:16284075}.
-!- ENZYME REGULATION: Calcium channel activity is enhanced by MYLK,
that promotes its subcellular localization at the plasma membrane.
{ECO:0000269|PubMed:16284075}.
-!- SUBUNIT: Interacts with TRPC4AP (By similarity). Homotetramer and
heterotetramer with TRPC1 and/or TRPC4. Interacts with NHERF (By
similarity). Interacts with MX1 and RNF24. Interacts (via C-
terminus) with CABP1. Interacts with SESTD1 (via the spectrin 1
repeat). {ECO:0000250, ECO:0000269|PubMed:12032305,
ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:15895247,
ECO:0000269|PubMed:17850865, ECO:0000269|PubMed:20164195}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16284075};
Multi-pass membrane protein {ECO:0000269|PubMed:16284075}.
-!- TISSUE SPECIFICITY: Expressed in brain with higher levels in fetal
brain. Found in cerebellum and occipital pole.
{ECO:0000269|PubMed:9687496}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
STrpC subfamily. TRPC5 sub-subfamily. {ECO:0000305}.
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EMBL; AF054568; AAF00002.1; -; mRNA.
EMBL; AC005191; AAC24563.1; -; Genomic_DNA.
EMBL; AL049563; CAI43017.1; -; Genomic_DNA.
EMBL; AC005191; CAI43017.1; JOINED; Genomic_DNA.
EMBL; CH471120; EAX02630.1; -; Genomic_DNA.
EMBL; BC137271; AAI37272.1; -; mRNA.
EMBL; BC137274; AAI37275.1; -; mRNA.
CCDS; CCDS14561.1; -.
RefSeq; NP_036603.1; NM_012471.2.
RefSeq; XP_016885263.1; XM_017029774.1.
UniGene; Hs.657709; -.
ProteinModelPortal; Q9UL62; -.
BioGrid; 113075; 18.
IntAct; Q9UL62; 1.
STRING; 9606.ENSP00000262839; -.
ChEMBL; CHEMBL1250411; -.
GuidetoPHARMACOLOGY; 490; -.
TCDB; 1.A.4.1.7; the transient receptor potential ca(2+) channel (trp-cc) family.
iPTMnet; Q9UL62; -.
PhosphoSitePlus; Q9UL62; -.
BioMuta; TRPC5; -.
DMDM; 10720321; -.
EPD; Q9UL62; -.
MaxQB; Q9UL62; -.
PaxDb; Q9UL62; -.
PeptideAtlas; Q9UL62; -.
PRIDE; Q9UL62; -.
Ensembl; ENST00000262839; ENSP00000262839; ENSG00000072315.
GeneID; 7224; -.
KEGG; hsa:7224; -.
UCSC; uc004epl.2; human.
CTD; 7224; -.
DisGeNET; 7224; -.
EuPathDB; HostDB:ENSG00000072315.3; -.
GeneCards; TRPC5; -.
HGNC; HGNC:12337; TRPC5.
MIM; 300334; gene.
neXtProt; NX_Q9UL62; -.
OpenTargets; ENSG00000072315; -.
PharmGKB; PA37010; -.
eggNOG; KOG3609; Eukaryota.
eggNOG; ENOG410XQ0Y; LUCA.
GeneTree; ENSGT00760000119180; -.
HOGENOM; HOG000020589; -.
HOVERGEN; HBG068337; -.
InParanoid; Q9UL62; -.
KO; K04968; -.
OMA; GFNEYVH; -.
OrthoDB; EOG091G029I; -.
PhylomeDB; Q9UL62; -.
TreeFam; TF313147; -.
Reactome; R-HSA-3295583; TRP channels.
Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
ChiTaRS; TRPC5; human.
GeneWiki; TRPC5; -.
GenomeRNAi; 7224; -.
PRO; PR:Q9UL62; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000072315; -.
CleanEx; HS_TRPC5; -.
Genevisible; Q9UL62; HS.
GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0030426; C:growth cone; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003779; F:actin binding; IEA:Ensembl.
GO; GO:0042805; F:actinin binding; IEA:Ensembl.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:Ensembl.
GO; GO:0015279; F:store-operated calcium channel activity; TAS:ProtInc.
GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome.
GO; GO:0006816; P:calcium ion transport; TAS:ProtInc.
GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
GO; GO:1902630; P:regulation of membrane hyperpolarization; IEA:Ensembl.
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; IPR005461; TRPC5_channel.
InterPro; IPR002153; TRPC_channel.
PANTHER; PTHR10117; PTHR10117; 1.
PANTHER; PTHR10117:SF24; PTHR10117:SF24; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF08344; TRP_2; 1.
PRINTS; PR01097; TRNSRECEPTRP.
PRINTS; PR01646; TRPCHANNEL5.
SMART; SM00248; ANK; 2.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
1: Evidence at protein level;
ANK repeat; Calcium; Calcium channel; Calcium transport;
Cell membrane; Complete proteome; Glycoprotein; Ion channel;
Ion transport; Membrane; Polymorphism; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 973 Short transient receptor potential
channel 5.
/FTId=PRO_0000215318.
TOPO_DOM 1 330 Cytoplasmic. {ECO:0000255}.
TRANSMEM 331 351 Helical. {ECO:0000255}.
TOPO_DOM 352 398 Extracellular. {ECO:0000255}.
TRANSMEM 399 419 Helical. {ECO:0000255}.
TOPO_DOM 420 437 Cytoplasmic. {ECO:0000255}.
TRANSMEM 438 458 Helical. {ECO:0000255}.
TOPO_DOM 459 470 Extracellular. {ECO:0000255}.
TRANSMEM 471 491 Helical. {ECO:0000255}.
TOPO_DOM 492 512 Cytoplasmic. {ECO:0000255}.
TRANSMEM 513 533 Helical. {ECO:0000255}.
TOPO_DOM 534 603 Extracellular. {ECO:0000255}.
TRANSMEM 604 624 Helical. {ECO:0000255}.
TOPO_DOM 625 973 Cytoplasmic. {ECO:0000255}.
REPEAT 31 60 ANK 1.
REPEAT 69 97 ANK 2.
REPEAT 98 124 ANK 3.
REPEAT 141 170 ANK 4.
REGION 971 973 Essential for binding to NHERF PDZ
domain. {ECO:0000250}.
CARBOHYD 461 461 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 667 667 P -> T (found in a patient with severe
delayed speech, autism spectrum and
Gilles de la Tourette disorders).
{ECO:0000269|PubMed:23033978}.
/FTId=VAR_069415.
VARIANT 702 702 R -> H (in dbSNP:rs36047478).
/FTId=VAR_052369.
SEQUENCE 973 AA; 111412 MW; FBC8CBF17BE42166 CRC64;
MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLNAV EKGDYATVKQ ALQEAEIYYN
VNINCMDPLG RSALLIAIEN ENLEIMELLL NHSVYVGDAL LYAIRKEVVG AVELLLSYRR
PSGEKQVPTL MMDTQFSEFT PDITPIMLAA HTNNYEIIKL LVQKRVTIPR PHQIRCNCVE
CVSSSEVDSL RHSRSRLNIY KALASPSLIA LSSEDPILTA FRLGWELKEL SKVENEFKAE
YEELSQQCKL FAKDLLDQAR SSRELEIILN HRDDHSEELD PQKYHDLAKL KVAIKYHQKE
FVAQPNCQQL LATLWYDGFP GWRRKHWVVK LLTCMTIGFL FPMLSIAYLI SPRSNLGLFI
KKPFIKFICH TASYLTFLFM LLLASQHIVR TDLHVQGPPP TVVEWMILPW VLGFIWGEIK
EMWDGGFTEY IHDWWNLMDF AMNSLYLATI SLKIVAYVKY NGSRPREEWE MWHPTLIAEA
LFAISNILSS LRLISLFTAN SHLGPLQISL GRMLLDILKF LFIYCLVLLA FANGLNQLYF
YYETRAIDEP NNCKGIRCEK QNNAFSTLFE TLQSLFWSVF GLLNLYVTNV KARHEFTEFV
GATMFGTYNV ISLVVLLNML IAMMNNSYQL IADHADIEWK FARTKLWMSY FDEGGTLPPP
FNIIPSPKSF LYLGNWFNNT FCPKRDPDGR RRRRNLRSFT ERNADSLIQN QHYQEVIRNL
VKRYVAAMIR NSKTHEGLTE ENFKELKQDI SSFRYEVLDL LGNRKHPRSF STSSTELSQR
DDNNDGSGGA RAKSKSVSFN LGCKKKTCHG PPLIRTMPRS SGAQGKSKAE SSSKRSFMGP
SLKKLGLLFS KFNGHMSEPS SEPMYTISDG IVQQHCMWQD IRYSQMEKGK AEACSQSEIN
LSEVELGEVQ GAAQSSECPL ACSSSLHCAS SICSSNSKLL DSSEDVFETW GEACDLLMHK
WGDGQEEQVT TRL


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GENTAUR France SARL
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Tel 01 43 25 01 50

Fax 01 43 25 01 60
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BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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Support Karolina Elandt
Tel: 0035929830070
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San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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