Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Maintenance of mitochondrial morphology protein 1 (Mitochondrial outer membrane protein MMM1) (Yeast mitochondrial escape protein 6)

 MMM1_YEAST              Reviewed;         426 AA.
P41800; D6VXZ7;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
25-OCT-2017, entry version 128.
RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000255|HAMAP-Rule:MF_03103};
AltName: Full=Mitochondrial outer membrane protein MMM1 {ECO:0000255|HAMAP-Rule:MF_03103};
AltName: Full=Yeast mitochondrial escape protein 6 {ECO:0000255|HAMAP-Rule:MF_03103};
Name=MMM1 {ECO:0000255|HAMAP-Rule:MF_03103}; Synonyms=YME6;
OrderedLocusNames=YLL006W; ORFNames=L1357;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 90850 / YH8;
PubMed=8089172; DOI=10.1083/jcb.126.6.1375;
Burgess S.M., Delannoy M., Jensen R.E.;
"MMM1 encodes a mitochondrial outer membrane protein essential for
establishing and maintaining the structure of yeast mitochondria.";
J. Cell Biol. 126:1375-1391(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 90840 / EAY235 / FY23;
PubMed=8810043;
DOI=10.1002/(SICI)1097-0061(19960615)12:7<693::AID-YEA956>3.0.CO;2-G;
Miosga T., Zimmermann F.K.;
"Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on
a 43.7 kb fragment of chromosome XII including an open reading frame
homologous to the human cystic fibrosis transmembrane conductance
regulator protein CFTR.";
Yeast 12:693-708(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION.
PubMed=9628893; DOI=10.1083/jcb.141.6.1371;
Boldogh I.R., Vojtov N., Karmon S., Pon L.A.;
"Interaction between mitochondria and the actin cytoskeleton in
budding yeast requires two integral mitochondrial outer membrane
proteins, Mmm1p and Mdm10p.";
J. Cell Biol. 141:1371-1381(1998).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11266455; DOI=10.1083/jcb.152.2.401;
Hobbs A.E.A., Srinivasan M., McCaffery J.M., Jensen R.E.;
"Mmm1p, a mitochondrial outer membrane protein, is connected to
mitochondrial DNA (mtDNA) nucleoids and required for mtDNA
stability.";
J. Cell Biol. 152:401-410(2001).
[7]
FUNCTION, AND MUTAGENESIS OF GLU-215.
PubMed=12454062;
Hanekamp T., Thorsness M.K., Rebbapragada I., Fisher E.M., Seebart C.,
Darland M.R., Coxbill J.A., Updike D.L., Thorsness P.E.;
"Maintenance of mitochondrial morphology is linked to maintenance of
the mitochondrial genome in Saccharomyces cerevisiae.";
Genetics 162:1147-1156(2002).
[8]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=12972421; DOI=10.1074/jbc.M308436200;
Kondo-Okamoto N., Shaw J.M., Okamoto K.;
"Mmm1p spans both the outer and inner mitochondrial membranes and
contains distinct domains for targeting and foci formation.";
J. Biol. Chem. 278:48997-49005(2003).
[9]
IDENTIFICATION IN THE MDM10/MDM12/MMM1 COMPLEX.
PubMed=13679517; DOI=10.1091/mbc.E03-04-0225;
Boldogh I.R., Nowakowski D.W., Yang H.-C., Chung H., Karmon S.,
Royes P., Pon L.A.;
"A protein complex containing Mdm10p, Mdm12p, and Mmm1p links
mitochondrial membranes and DNA to the cytoskeleton-based segregation
machinery.";
Mol. Biol. Cell 14:4618-4627(2003).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14981098; DOI=10.1083/jcb.200308012;
Youngman M.J., Hobbs A.E.A., Burgess S.M., Srinivasan M., Jensen R.E.;
"Mmm2p, a mitochondrial outer membrane protein required for yeast
mitochondrial shape and maintenance of mtDNA nucleoids.";
J. Cell Biol. 164:677-688(2004).
[14]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16407407; DOI=10.1091/mbc.E05-08-0740;
Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
"Proteomic analysis of the yeast mitochondrial outer membrane reveals
accumulation of a subclass of preproteins.";
Mol. Biol. Cell 17:1436-1450(2006).
[15]
FUNCTION, AND IDENTIFICATION IN MDM12/MMM1 AND MDM10/MDM12/MMM1
COMPLEXES.
PubMed=17410204; DOI=10.1038/sj.emboj.7601673;
Meisinger C., Pfannschmidt S., Rissler M., Milenkovic D., Becker T.,
Stojanovski D., Youngman M.J., Jensen R.E., Chacinska A., Guiard B.,
Pfanner N., Wiedemann N.;
"The morphology proteins Mdm12/Mmm1 function in the major beta-barrel
assembly pathway of mitochondria.";
EMBO J. 26:2229-2239(2007).
[16]
FUNCTION, IDENTIFICATION IN ERMES/MDM COMPLEX, SUBCELLULAR LOCATION,
TOPOLOGY, AND GLYCOSYLATION.
PubMed=19556461; DOI=10.1126/science.1175088;
Kornmann B., Currie E., Collins S.R., Schuldiner M., Nunnari J.,
Weissman J.S., Walter P.;
"An ER-mitochondria tethering complex revealed by a synthetic biology
screen.";
Science 325:477-481(2009).
-!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
molecular tether to connect the endoplasmic reticulum and
mitochondria. Components of this complex are involved in the
control of mitochondrial shape and protein biogenesis and may
function in phospholipid exchange. The MDM12-MMM1 subcomplex
functions in the major beta-barrel assembly pathway that is
responsible for biogenesis of all outer membrane beta-barrel
proteins, and acts in a late step after the SAM complex. The
MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific
pathway after the action of the MDM12-MMM1 complex. Essential for
establishing and maintaining the structure of mitochondria and
maintenance of mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03103,
ECO:0000269|PubMed:11266455, ECO:0000269|PubMed:12454062,
ECO:0000269|PubMed:14981098, ECO:0000269|PubMed:17410204,
ECO:0000269|PubMed:19556461, ECO:0000269|PubMed:8089172,
ECO:0000269|PubMed:9628893}.
-!- SUBUNIT: Component of the ER-mitochondria encounter structure
(ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34.
{ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:13679517,
ECO:0000269|PubMed:17410204, ECO:0000269|PubMed:19556461}.
-!- INTERACTION:
Q92328:MDM12; NbExp=5; IntAct=EBI-11029, EBI-10584;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:11266455,
ECO:0000269|PubMed:12972421, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:14981098,
ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:19556461,
ECO:0000269|PubMed:8089172}; Single-pass type I membrane protein
{ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:11266455,
ECO:0000269|PubMed:12972421, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:14981098,
ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:19556461,
ECO:0000269|PubMed:8089172}. Note=The ERMES/MDM complex localizes
to a few discrete foci (around 10 per single cell), that represent
mitochondria-endoplasmic reticulum junctions. These foci are often
found next to mtDNA nucleoids.
-!- PTM: Glycosylated. {ECO:0000255|HAMAP-Rule:MF_03103,
ECO:0000269|PubMed:19556461}.
-!- MISCELLANEOUS: Normal levels of MMM1 require MDM34.
-!- MISCELLANEOUS: Present with 2490 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the MMM1 family. {ECO:0000255|HAMAP-
Rule:MF_03103}.
-!- CAUTION: Was originally (PubMed:12972421 and PubMed:8089172)
proposed to be inserted into either the outer or inner
mitochondrial membrane, yet more recent data indicates that it is
instead inserted into the ER. {ECO:0000305|PubMed:19556461}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L32793; AAA53581.1; -; Genomic_DNA.
EMBL; X91488; CAA62763.1; -; Genomic_DNA.
EMBL; Z73111; CAA97449.1; -; Genomic_DNA.
EMBL; BK006945; DAA09313.1; -; Genomic_DNA.
PIR; S64748; S64748.
RefSeq; NP_013095.1; NM_001181826.1.
ProteinModelPortal; P41800; -.
SMR; P41800; -.
BioGrid; 31245; 633.
DIP; DIP-4150N; -.
IntAct; P41800; 24.
MINT; MINT-495281; -.
STRING; 4932.YLL006W; -.
TCDB; 9.A.58.1.1; the maintenance of mitochondrial morphology (mmm) family.
MaxQB; P41800; -.
PRIDE; P41800; -.
EnsemblFungi; YLL006W; YLL006W; YLL006W.
GeneID; 850654; -.
KEGG; sce:YLL006W; -.
EuPathDB; FungiDB:YLL006W; -.
SGD; S000003929; MMM1.
HOGENOM; HOG000201075; -.
InParanoid; P41800; -.
KO; K17764; -.
OMA; ERCVEPR; -.
OrthoDB; EOG092C2Z53; -.
BioCyc; YEAST:G3O-32111-MONOMER; -.
PRO; PR:P41800; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0032865; C:ERMES complex; IDA:SGD.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
GO; GO:0008289; F:lipid binding; IBA:GO_Central.
GO; GO:0015917; P:aminophospholipid transport; IMP:SGD.
GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IMP:SGD.
GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IMP:SGD.
GO; GO:0015914; P:phospholipid transport; IMP:SGD.
GO; GO:0045040; P:protein import into mitochondrial outer membrane; IMP:SGD.
HAMAP; MF_03103; Mmm1; 1.
InterPro; IPR027537; Mmm1.
InterPro; IPR019411; MMM1_dom.
Pfam; PF10296; MMM1; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Glycoprotein; Membrane;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 426 Maintenance of mitochondrial morphology
protein 1.
/FTId=PRO_0000096506.
TOPO_DOM 1 100 Lumenal.
TRANSMEM 101 121 Helical. {ECO:0000255|HAMAP-
Rule:MF_03103}.
TOPO_DOM 122 426 Cytoplasmic.
CARBOHYD 6 6 N-linked (GlcNAc...) asparagine.
{ECO:0000255|HAMAP-Rule:MF_03103}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255|HAMAP-Rule:MF_03103}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255|HAMAP-Rule:MF_03103}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255|HAMAP-Rule:MF_03103}.
MUTAGEN 215 215 E->K: In MMM1-6; impairs both mtDNA
maintenance and mitochondrial morpholgy.
{ECO:0000269|PubMed:12454062}.
CONFLICT 200 200 W -> S (in Ref. 1; AAA53581).
{ECO:0000305}.
CONFLICT 225 225 S -> W (in Ref. 1; AAA53581).
{ECO:0000305}.
CONFLICT 357 357 S -> A (in Ref. 1; AAA53581).
{ECO:0000305}.
CONFLICT 365 365 E -> Q (in Ref. 1; AAA53581).
{ECO:0000305}.
CONFLICT 368 368 S -> P (in Ref. 1; AAA53581).
{ECO:0000305}.
SEQUENCE 426 AA; 48660 MW; 3610AEC2109355AF CRC64;
MTDSENESTE TDSLMTFDDY ISKELPEHLQ RLIMENLKGS TTNDLKQTSN NSEFNVSKNG
SFKGLDDAIQ ALQMQSVLHP SSLGSLATSS KFSGWSFAQG FFVGQLSIVL LFIFFLKFFI
FSDEPSKSKN PKPAASRHRS KFKEYPFISR EFLTSLVRKG AKQHYELNEE AENEHLQELA
LILEKTYYNV DVHPAESLDW FNVLVAQIIQ QFRSEAWHRD NILHSLNDFI GRKSPDLPEY
LDTIKITELD TGDDFPIFSN CRIQYSPNSG NKKLEAKIDI DLNDHLTLGV ETKLLLNYPK
PGIAALPINL VVSIVRFQAC LTVSLTNAEE FASTSNGSSS ENGMEGNSGY FLMFSFSPEY
RMEFEIKSLI GSRSKLENIP KIGSVIEYQI KKWFVERCVE PRFQFVRLPS MWPRSKNTRE
EKPTEL


Related products :

Catalog number Product name Quantity
EIAAB43394 Homo sapiens,Human,KIAA0016,Mitochondrial 20 kDa outer membrane protein,Mitochondrial import receptor subunit TOM20 homolog,Outer mitochondrial membrane receptor Tom20,TOMM20
EIAAB43391 Mitochondrial 20 kDa outer membrane protein,Mitochondrial import receptor subunit TOM20 homolog,Mouse,Mus musculus,Outer mitochondrial membrane receptor Tom20,Tomm20
EIAAB43393 Mitochondrial 20 kDa outer membrane protein,Mitochondrial import receptor subunit TOM20 homolog,Outer mitochondrial membrane receptor Tom20,Rat,Rattus norvegicus,Tomm20
EIAAB43392 Bos taurus,Bovine,Mitochondrial 20 kDa outer membrane protein,Mitochondrial import receptor subunit TOM20 homolog,Outer mitochondrial membrane receptor Tom20,TOMM20
27-309 BCL2L1 encodes a protein which belongs to the BCL-2 protein family. The proteins encoded by BCL2L1 are located at the outer mitochondrial membrane, and have been shown to regulate outer mitochondrial 0.1 mg
31-011 BCL2L1 encodes a protein which belongs to the BCL-2 protein family. The proteins encoded by BCL2L1 are located at the outer mitochondrial membrane, and have been shown to regulate outer mitochondrial 0.05 mg
EIAAB43405 Mitochondrial import receptor subunit TOM40 homolog,Mitochondrial outer membrane protein of 35 kDa,MOM35,Mom35,Mouse,Mus musculus,Protein Haymaker,Tom40,Tomm40,Translocase of outer membrane 40 kDa sub
25-835 MARCH5 is an ubiquitin ligase of the mitochondrial outer membrane that plays a role in the control of mitochondrial morphology by regulating mitofusin-2 (MFN2) and DRP1 (DNM1L).MARCH5 is a ubiquitin l 0.05 mg
EIAAB43402 Mitochondrial import receptor subunit TOM40 homolog,Mitochondrial outer membrane protein of 38 kDa,OM38,Rat,Rattus norvegicus,Tom40,Tom40a,Tomm40,Translocase of outer membrane 40 kDa subunit homolog
EIAAB41354 Bos taurus,Bovine,Mitochondrial translocator assembly and maintenance protein 41 homolog,MMP37-like protein, mitochondrial,TAM41,TAMM41
EIAAB41355 Mitochondrial translocator assembly and maintenance protein 41 homolog,MMP37-like protein, mitochondrial,Mouse,Mus musculus,TAM41,Tamm41
EIAAB41356 C3orf31,Homo sapiens,Human,Mitochondrial translocator assembly and maintenance protein 41 homolog,MMP37-like protein, mitochondrial,TAM41,TAMM41
30-357 HADHB is the beta subunit of the mitochondrial trifunctional protein, which catalyzes the last three steps of mitochondrial beta-oxidation of long chain fatty acids. The mitochondrial membrane-bound h 0.05 mg
EIAAB40760 Activin receptor-interacting protein 2,ARIP2,Bos taurus,Bovine,Mitochondrial outer membrane protein 25,OMP25,Synaptojanin-2-binding protein,SYNJ2BP
EIAAB40758 Homo sapiens,Human,Mitochondrial outer membrane protein 25,OMP25,Synaptojanin-2-binding protein,SYNJ2BP
EIAAB40759 Mitochondrial outer membrane protein 25,NPW16,Omp25,Rat,Rattus norvegicus,Synaptojanin-2-binding protein,Synj2bp
EIAAB37561 APC1,Calcium-binding mitochondrial carrier protein SCaMC-1,Homo sapiens,Human,MCSC1,Mitochondrial ATP-Mg_Pi carrier protein 1,Mitochondrial Ca(2+)-dependent solute carrier protein 1,SCAMC1,SLC25A24,Sm
EIAAB37568 APC2,Calcium-binding mitochondrial carrier protein SCaMC-3,Homo sapiens,Human,MCSC2,Mitochondrial ATP-Mg_Pi carrier protein 2,Mitochondrial Ca(2+)-dependent solute carrier protein 2,SCAMC3,SLC25A23,Sm
EIAAB37565 APC3,Calcium-binding mitochondrial carrier protein SCaMC-2,Homo sapiens,Human,KIAA1896,MCSC3,Mitochondrial ATP-Mg_Pi carrier protein 3,Mitochondrial Ca(2+)-dependent solute carrier protein 3,SCAMC2,SL
EIAAB45744 Outer mitochondrial membrane protein porin 3,Pig,Sus scrofa,VDAC3,VDAC-3,Voltage-dependent anion-selective channel protein 3
25-246 VDAC3 belongs to a group of mitochondrial membrane channels involved in translocation of adenine nucleotides through the outer membrane. These channels may also function as a mitochondrial binding sit 0.05 mg
EIAAB35298 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,Homo sapiens,HSPC204,Human,L31mt,L42mt,MRPL31,MRP-L31,MRPL42,MRP-L42,MRPS32,M
EIAAB45740 Bos taurus,Bovine,Outer mitochondrial membrane protein porin 2,VDAC2,VDAC-2,Voltage-dependent anion-selective channel protein 2
EIAAB45742 Bos taurus,Bovine,Outer mitochondrial membrane protein porin 3,VDAC3,VDAC-3,Voltage-dependent anion-selective channel protein 3
EIAAB45741 Mouse,Mus musculus,mVDAC3,Outer mitochondrial membrane protein porin 3,Vdac3,VDAC-3,Voltage-dependent anion-selective channel protein 3


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




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

france@gentaur.com | Gentaur

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
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
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
6017 Snell Ave, Ste 357
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
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






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
IBAN: BG11FINV91501014771636
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              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur