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Oxysterol-binding protein-related protein 1 (ORP-1) (OSBP-related protein 1)

 OSBL1_HUMAN             Reviewed;         950 AA.
Q9BXW6; B7Z7D3; Q9BZF5; Q9NW87;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
27-MAR-2002, sequence version 2.
05-DEC-2018, entry version 168.
RecName: Full=Oxysterol-binding protein-related protein 1;
Short=ORP-1;
Short=OSBP-related protein 1;
Name=OSBPL1A; Synonyms=ORP1, OSBP8, OSBPL1, OSBPL1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND VARIANT PRO-810.
PubMed=11735225; DOI=10.1006/geno.2001.6663;
Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.;
"A family of 12 human genes containing oxysterol-binding domains.";
Genomics 78:185-196(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=11279184; DOI=10.1074/jbc.M101204200;
Xu Y., Liu Y., Ridgway N.D., McMaster C.R.;
"Novel members of the human oxysterol-binding protein family bind
phospholipids and regulate vesicle transport.";
J. Biol. Chem. 276:18407-18414(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND GENE FAMILY.
PubMed=11483621;
Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C.,
Staels B., Ikonen E., Olkkonen V.M.;
"The OSBP-related protein family in humans.";
J. Lipid Res. 42:1203-1213(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 514-790 (ISOFORM A).
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB7A.
PubMed=16176980; DOI=10.1091/mbc.E05-03-0189;
Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.;
"The oxysterol-binding protein homologue ORP1L interacts with Rab7 and
alters functional properties of late endocytic compartments.";
Mol. Biol. Cell 16:5480-5492(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
FUNCTION.
PubMed=17428193; DOI=10.1042/BJ20070176;
Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M.,
Saarinen H., Radzikowska A., Thiele C., Olkkonen V.M.;
"The mammalian oxysterol-binding protein-related proteins (ORPs) bind
25-hydroxycholesterol in an evolutionarily conserved pocket.";
Biochem. J. 405:473-480(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, 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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, 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).
-!- FUNCTION: Binds phospholipids; exhibits strong binding to
phosphatidic acid and weak binding to phosphatidylinositol 3-
phosphate (By similarity). Stabilizes GTP-bound RAB7A on late
endosomes/lysosomes and alters functional properties of late
endocytic compartments via its interaction with RAB7A
(PubMed:16176980). Binds 25-hydroxycholesterol and cholesterol
(PubMed:17428193). {ECO:0000250, ECO:0000269|PubMed:16176980,
ECO:0000269|PubMed:17428193}.
-!- SUBUNIT: Interacts with VAPA (By similarity). Interacts with the
GTP-bound form of RAB7A. Interacts with OAS1B (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:16176980}.
Note=Colocalizes with RAB7A, RAB9A and LAMP1 in late endosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=B; Synonyms=OSBPL1B, OSBP8L, ORP1L;
IsoId=Q9BXW6-1; Sequence=Displayed;
Name=A; Synonyms=OSBPL1A, OSBP8S;
IsoId=Q9BXW6-2; Sequence=VSP_003779;
Name=4;
IsoId=Q9BXW6-4; Sequence=VSP_045443;
-!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG53407.2; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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EMBL; AF392449; AAL40662.1; -; mRNA.
EMBL; AF392450; AAL40663.1; -; mRNA.
EMBL; AF274714; AAK15154.1; -; mRNA.
EMBL; AF323726; AAG53407.2; ALT_SEQ; mRNA.
EMBL; AK001079; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK301862; BAH13569.1; -; mRNA.
EMBL; AC023983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS11884.1; -. [Q9BXW6-1]
CCDS; CCDS11885.1; -. [Q9BXW6-2]
CCDS; CCDS56056.1; -. [Q9BXW6-4]
RefSeq; NP_001229437.1; NM_001242508.1. [Q9BXW6-4]
RefSeq; NP_060500.3; NM_018030.4. [Q9BXW6-2]
RefSeq; NP_542164.2; NM_080597.3. [Q9BXW6-1]
RefSeq; XP_016881022.1; XM_017025533.1. [Q9BXW6-2]
RefSeq; XP_016881023.1; XM_017025534.1.
UniGene; Hs.370725; -.
ProteinModelPortal; Q9BXW6; -.
SMR; Q9BXW6; -.
BioGrid; 125379; 24.
IntAct; Q9BXW6; 13.
STRING; 9606.ENSP00000320291; -.
SwissLipids; SLP:000001534; -.
iPTMnet; Q9BXW6; -.
PhosphoSitePlus; Q9BXW6; -.
BioMuta; OSBPL1A; -.
DMDM; 20143880; -.
EPD; Q9BXW6; -.
MaxQB; Q9BXW6; -.
PaxDb; Q9BXW6; -.
PeptideAtlas; Q9BXW6; -.
PRIDE; Q9BXW6; -.
ProteomicsDB; 79527; -.
ProteomicsDB; 79528; -. [Q9BXW6-2]
Ensembl; ENST00000319481; ENSP00000320291; ENSG00000141447. [Q9BXW6-1]
Ensembl; ENST00000357041; ENSP00000349545; ENSG00000141447. [Q9BXW6-4]
Ensembl; ENST00000399443; ENSP00000382372; ENSG00000141447. [Q9BXW6-2]
GeneID; 114876; -.
KEGG; hsa:114876; -.
UCSC; uc002kvd.5; human. [Q9BXW6-1]
CTD; 114876; -.
DisGeNET; 114876; -.
EuPathDB; HostDB:ENSG00000141447.16; -.
GeneCards; OSBPL1A; -.
H-InvDB; HIX0014371; -.
HGNC; HGNC:16398; OSBPL1A.
HPA; HPA040959; -.
HPA; HPA043401; -.
MIM; 606730; gene.
neXtProt; NX_Q9BXW6; -.
OpenTargets; ENSG00000141447; -.
PharmGKB; PA32826; -.
eggNOG; KOG1737; Eukaryota.
eggNOG; ENOG410XP9E; LUCA.
GeneTree; ENSGT00940000155295; -.
HOGENOM; HOG000048711; -.
HOVERGEN; HBG082087; -.
InParanoid; Q9BXW6; -.
KO; K20174; -.
OMA; IEDHSAY; -.
OrthoDB; EOG091G07RK; -.
PhylomeDB; Q9BXW6; -.
TreeFam; TF320922; -.
Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
ChiTaRS; OSBPL1A; human.
GeneWiki; OSBPL1A; -.
GenomeRNAi; 114876; -.
PRO; PR:Q9BXW6; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000141447; Expressed in 230 organ(s), highest expression level in corpus callosum.
CleanEx; HS_OSBPL1A; -.
ExpressionAtlas; Q9BXW6; baseline and differential.
Genevisible; Q9BXW6; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO; GO:0008289; F:lipid binding; IBA:GO_Central.
GO; GO:0005543; F:phospholipid binding; NAS:UniProtKB.
GO; GO:0032934; F:sterol binding; IBA:GO_Central.
GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
GO; GO:0008203; P:cholesterol metabolic process; NAS:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 2.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR037239; OSBP_sf.
InterPro; IPR000648; Oxysterol-bd.
InterPro; IPR018494; Oxysterol-bd_CS.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR10972; PTHR10972; 3.
Pfam; PF12796; Ank_2; 1.
Pfam; PF01237; Oxysterol_BP; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 3.
SMART; SM00233; PH; 1.
SUPFAM; SSF144000; SSF144000; 1.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
PROSITE; PS01013; OSBP; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Coiled coil; Complete proteome;
Endosome; Lipid transport; Lipid-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transport.
CHAIN 1 950 Oxysterol-binding protein-related protein
1.
/FTId=PRO_0000100367.
REPEAT 47 76 ANK 1.
REPEAT 80 109 ANK 2.
REPEAT 175 204 ANK 3.
DOMAIN 235 334 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
REGION 1 237 Interaction with RAB7A.
{ECO:0000269|PubMed:16176980}.
COILED 430 463 {ECO:0000255}.
COILED 877 913 {ECO:0000255}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 513 Missing (in isoform A).
{ECO:0000303|PubMed:11279184,
ECO:0000303|PubMed:11735225,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_003779.
VAR_SEQ 1 382 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045443.
VARIANT 810 810 S -> P (in dbSNP:rs35693789).
{ECO:0000269|PubMed:11735225}.
/FTId=VAR_053547.
CONFLICT 735 735 T -> A (in Ref. 4; AK001079).
{ECO:0000305}.
CONFLICT 841 841 P -> S (in Ref. 1; AAL40662).
{ECO:0000305}.
CONFLICT 844 844 A -> G (in Ref. 1; AAL40662).
{ECO:0000305}.
SEQUENCE 950 AA; 108470 MW; CDDA26CA27B65F63 CRC64;
MNTEAEQQLL HHARNGNAEE VRQLLETMAR NEVIADINCK GRSKSNLGWT PLHLACYFGH
RQVVQDLLKA GAEVNVLNDM GDTPLHRAAF TGRKELVMLL LEYNADTTIV NGSGQTAKEV
THAEEIRSML EAVERTQQRK LEELLLAAAR EGKTTELTAL LNRPNPPDVN CSDQLGNTPL
HCAAYRAHKQ CALKLLRSGA DPNLKNKNDQ KPLDLAQGAE MKHILVGNKV IYKALKRYEG
PLWKSSRFFG WRLFWVVLEH GVLSWYRKQP DAVHNIYRQG CKHLTQAVCT VKSTDSCLFF
IKCFDDTIHG FRVPKNSLQQ SREDWLEAIE EHSAYSTHYC SQDQLTDEEE EDTVSAADLK
KSLEKAQSCQ QRLDREISNF LKMIKECDMA KEMLPSFLQK VEVVSEASRE TCVALTDCLN
LFTKQEGVRN FKLEQEQEKN KILSEALETL ATEHHELEQS LVKGSPPASI LSEDEFYDAL
SDSESERSLS RLEAVTARSF EEEGEHLGSR KHRMSEEKDC GGGDALSNGI KKHRTSLPSP
MFSRNDFSIW SILRKCIGME LSKITMPVIF NEPLSFLQRL TEYMEHTYLI HKASSLSDPV
ERMQCVAAFA VSAVASQWER TGKPFNPLLG ETYELVRDDL GFRLISEQVS HHPPISAFHA
EGLNNDFIFH GSIYPKLKFW GKSVEAEPKG TITLELLEHN EAYTWTNPTC CVHNIIVGKL
WIEQYGNVEI INHKTGDKCV LNFKPCGLFG KELHKVEGYI QDKSKKKLCA LYGKWTECLY
SVDPATFDAY KKNDKKNTEE KKNSKQMSTS EELDEMPVPD SESVFIIPGS VLLWRIAPRP
PNSAQMYNFT SFAMVLNEVD KDMESVIPKT DCRLRPDIRA MENGEIDQAS EEKKRLEEKQ
RAARKNRSKS EEDWKTRWFH QGPNPYNGAQ DWIYSGSYWD RNYFNLPDIY


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GENTAUR Ltd.
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Hertfordshire, Potters Bar EN6 1TL
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
RIB 30004 00187 00010092253 10
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
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
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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
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
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BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

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GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
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