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

P-type cation-transporting ATPase (EC 3.6.3.3) (Cadmium resistance protein 2) (Cadmium-translocating P-type ATPase) (Cd(2 )-exporting ATPase)

 ATU1_YEAST              Reviewed;        1216 AA.
P38360; D6VQT9;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 167.
RecName: Full=P-type cation-transporting ATPase;
EC=3.6.3.3;
AltName: Full=Cadmium resistance protein 2;
AltName: Full=Cadmium-translocating P-type ATPase;
AltName: Full=Cd(2+)-exporting ATPase;
Name=PCA1; Synonyms=CAD2, PAY2; OrderedLocusNames=YBR295W;
ORFNames=YBR2112;
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], AND FUNCTION.
STRAIN=ATCC 204508 / S288c;
PubMed=7754711; DOI=10.1002/yea.320100910;
Rad M.R., Kirchrath L., Hollenberg C.;
"A putative P-type Cu(2+)-transporting ATPase gene on chromosome II of
Saccharomyces cerevisiae.";
Yeast 10:1217-1225(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[3]
GENOME REANNOTATION, AND SEQUENCE REVISION TO 382.
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).
[4]
FUNCTION.
PubMed=2249249; DOI=10.1007/BF00318377;
Tohoyama H., Inouhe M., Joho M., Murayama T.;
"Resistance to cadmium is under control of the CAD2 gene in the yeast
Saccharomyces cerevisiae.";
Curr. Genet. 18:181-185(1990).
[5]
FUNCTION, AND MUTAGENESIS OF ARG-970.
PubMed=10743563; DOI=10.1007/s002940050013;
Shiraishi E., Inouhe M., Joho M., Tohoyama H.;
"The cadmium-resistant gene, CAD2, which is a mutated putative copper-
transporter gene (PCA1), controls the intracellular cadmium-level in
the yeast S. cerevisiae.";
Curr. Genet. 37:79-86(2000).
[6]
FUNCTION.
PubMed=14534306; DOI=10.1074/jbc.M212308200;
De Freitas J.M., Kim J.H., Poynton H., Su T., Wintz H., Fox T.,
Holman P., Loguinov A., Keles S., van der Laan M., Vulpe C.;
"Exploratory and confirmatory gene expression profiling of
mac1Delta.";
J. Biol. Chem. 279:4450-4458(2004).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-970.
PubMed=17107946; DOI=10.1074/jbc.M609535200;
Adle D.J., Sinani D., Kim H., Lee J.;
"A cadmium-transporting P1B-type ATPase in yeast Saccharomyces
cerevisiae.";
J. Biol. Chem. 282:947-955(2007).
[8]
FUNCTION, MOTIF, UBIQUITINATION, AND MUTAGENESIS OF CYS-298; CYS-300;
CYS-311 AND CYS-312.
PubMed=18753133; DOI=10.1074/jbc.M806054200;
Adle D.J., Lee J.;
"Expressional control of a cadmium-transporting P1B-type ATPase by a
metal sensing degradation signal.";
J. Biol. Chem. 283:31460-31468(2008).
[9]
FUNCTION.
PubMed=21483812; DOI=10.1371/journal.pgen.1002034;
Chang S.L., Leu J.Y.;
"A tradeoff drives the evolution of reduced metal resistance in
natural populations of yeast.";
PLoS Genet. 7:E1002034-E1002034(2011).
-!- FUNCTION: Cadmium transporting P-type ATPase which plays a
critical role in cadmium resistance by extruding intracellular
cadmium. Capable of high affinity copper ion binding, but not
active copper ion transport. May play a role in copper resistance
by chelating and sequestering copper ions.
{ECO:0000269|PubMed:10743563, ECO:0000269|PubMed:14534306,
ECO:0000269|PubMed:17107946, ECO:0000269|PubMed:18753133,
ECO:0000269|PubMed:21483812, ECO:0000269|PubMed:2249249,
ECO:0000269|PubMed:7754711}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Cd(2+)(In) = ADP + phosphate +
Cd(2+)(Out).
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17107946};
Multi-pass membrane protein {ECO:0000269|PubMed:17107946}.
-!- PTM: In the absence of cadmium, is ubiquitinated and targeted for
degradation before reaching the plasma membrane. This allows a
rapid and specific cellular response to cadmium.
{ECO:0000269|PubMed:18753133}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IB subfamily. {ECO:0000305}.
-!- CAUTION: Although initial characterizations described PCA1 as a
copper-transporting ATPase, subsequent experiments have
demonstrated that PCA1 is capable of high affinity copper ion
binding, but not active copper ion transport.
{ECO:0000305|PubMed:7754711}.
-!- CAUTION: Strain S288C, as well as other laboratory cadmium-
sensitive strains, contain a natural Gly-970-Arg mutation which
eliminates cadmium transport function. Loss of cadmium resistance
provides a fitness advantage under cadmium-free conditions.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z29332; CAA82529.1; -; Genomic_DNA.
EMBL; Z36164; CAA85260.1; -; Genomic_DNA.
EMBL; BK006936; DAA07409.2; -; Genomic_DNA.
PIR; S46177; S46177.
RefSeq; NP_009854.2; NM_001178643.2.
ProteinModelPortal; P38360; -.
SMR; P38360; -.
BioGrid; 32988; 59.
DIP; DIP-6641N; -.
IntAct; P38360; 3.
MINT; MINT-620940; -.
STRING; 4932.YBR295W; -.
TCDB; 3.A.3.5.14; the p-type atpase (p-atpase) superfamily.
PRIDE; P38360; -.
EnsemblFungi; YBR295W; YBR295W; YBR295W.
GeneID; 852598; -.
KEGG; sce:YBR295W; -.
EuPathDB; FungiDB:YBR295W; -.
SGD; S000000499; PCA1.
HOGENOM; HOG000160566; -.
InParanoid; P38360; -.
KO; K01533; -.
OMA; CTGCENK; -.
OrthoDB; EOG092C0DN9; -.
BioCyc; YEAST:G3O-29213-MONOMER; -.
PRO; PR:P38360; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0005839; C:proteasome core complex; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008551; F:cadmium-exporting ATPase activity; IMP:SGD.
GO; GO:0005388; F:calcium-transporting ATPase activity; IBA:GO_Central.
GO; GO:0005507; F:copper ion binding; IMP:SGD.
GO; GO:0070628; F:proteasome binding; IPI:SGD.
GO; GO:0015691; P:cadmium ion transport; IMP:SGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
GO; GO:0006879; P:cellular iron ion homeostasis; IEP:SGD.
GO; GO:0006875; P:cellular metal ion homeostasis; IMP:SGD.
GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
GO; GO:0055085; P:transmembrane transport; IMP:SGD.
CDD; cd00371; HMA; 1.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
InterPro; IPR027256; P-typ_ATPase_IB.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00403; HMA; 1.
SUPFAM; SSF55008; SSF55008; 1.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81665; SSF81665; 2.
TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 1.
PROSITE; PS00154; ATPASE_E1_E2; 1.
PROSITE; PS50846; HMA_2; 1.
1: Evidence at protein level;
ATP-binding; Cadmium; Cadmium resistance; Cell membrane;
Complete proteome; Copper; Hydrolase; Ion transport; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 1216 P-type cation-transporting ATPase.
/FTId=PRO_0000046317.
TOPO_DOM 1 556 Cytoplasmic. {ECO:0000255}.
TRANSMEM 557 578 Helical. {ECO:0000255}.
TOPO_DOM 579 592 Extracellular. {ECO:0000255}.
TRANSMEM 593 612 Helical. {ECO:0000255}.
TOPO_DOM 613 620 Cytoplasmic. {ECO:0000255}.
TRANSMEM 621 641 Helical. {ECO:0000255}.
TOPO_DOM 642 659 Extracellular. {ECO:0000255}.
TRANSMEM 660 680 Helical. {ECO:0000255}.
TOPO_DOM 681 808 Cytoplasmic. {ECO:0000255}.
TRANSMEM 809 831 Helical. {ECO:0000255}.
TOPO_DOM 832 847 Extracellular. {ECO:0000255}.
TRANSMEM 848 865 Helical. {ECO:0000255}.
TOPO_DOM 866 1161 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1162 1181 Helical. {ECO:0000255}.
TOPO_DOM 1182 1190 Extracellular. {ECO:0000255}.
TRANSMEM 1191 1209 Helical. {ECO:0000255}.
TOPO_DOM 1210 1216 Cytoplasmic. {ECO:0000255}.
DOMAIN 411 474 HMA. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
REGION 250 350 Metal-responding degradation signal.
ACT_SITE 903 903 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 421 421 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 424 424 Copper. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 1107 1107 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 1111 1111 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
MUTAGEN 298 298 C->A: Abolishes copper resistance but not
cadmium resistance; when associated with
A-300. {ECO:0000269|PubMed:18753133}.
MUTAGEN 300 300 C->A: Abolishes copper resistance but not
cadmium resistance; when associated with
A-298. {ECO:0000269|PubMed:18753133}.
MUTAGEN 311 311 C->A: Abolishes cadmium resistance yet
retains the ability to confer copper
resistance; when associated with A-312.
{ECO:0000269|PubMed:18753133}.
MUTAGEN 312 312 C->A: Abolishes cadmium resistance yet
retains the ability to confer copper
resistance; when associated with A-311.
{ECO:0000269|PubMed:18753133}.
MUTAGEN 970 970 R->G: Confers localization to the plasma
membrane and cadmium transport function.
{ECO:0000269|PubMed:10743563,
ECO:0000269|PubMed:17107946}.
CONFLICT 382 382 H -> T (in Ref. 1; CAA82529 and 2;
CAA85260). {ECO:0000305}.
SEQUENCE 1216 AA; 131875 MW; E4DCAFB23AA1F138 CRC64;
MKPEKLFSGL GTSDGEYGVV NSENISIDAM QDNRGECHRR SIEMHANDNL GLVSQRDCTN
RPKITPQECL SETEQICHHG ENRTKAGLDV DDAETGGDHT NESRVDECCA EKVNDTETGL
DVDSCCGDAQ TGGDHTNESC VDGCCVRDSS VMVEEVTGSC EAVSSKEQLL TSFEVVPSKS
EGLQSIHDIR ETTRCNTNSN QHTGKGRLCI ESSDSTLKKR SCKVSRQKIE VSSKPECCNI
SCVERIASRS CEKRTFKGST NVGISGSSST DSLSEKFFSE QYSRMYNRYS SILKNLGCIC
NYLRTLGKES CCLPKVRFCS GEGASKKTKY SYRNSSGCLT KKKTHGDKER LSNDNGHADF
VCSKSCCTKM KDCAVTSTIS GHSSSEISRI VSMEPIENHL NLEAGSTGTE HIVLSVSGMS
CTGCESKLKK SFGALKCVHG LKTSLILSQA EFNLDLAQGS VKDVIKHLSK TTEFKYEQIS
NHGSTIDVVV PYAAKDFINE EWPQGVTELK IVERNIIRIY FDPKVIGARD LVNEGWSVPV
SIAPFSCHPT IEVGRKHLVR VGCTTALSII LTIPILVMAW APQLREKIST ISASMVLATI
IQFVIAGPFY LNALKSLIFS RLIEMDLLIV LSTSAAYIFS IVSFGYFVVG RPLSTEQFFE
TSSLLVTLIM VGRFVSELAR HRAVKSISVR SLQASSAILV DKTGKETEIN IRLLQYGDIF
KVLPDSRIPT DGTVISGSSE VDEALITGES MPVPKKCQSI VVAGSVNGTG TLFVKLSKLP
GNNTISTIAT MVDEAKLTKP KIQNIADKIA SYFVPTIIGI TVVTFCVWIA VGIRVEKQSR
SDAVIQAIIY AITVLIVSCP CVIGLAVPIV FVIASGVAAK RGVIFKSAES IEVAHNTSHV
VFDKTGTLTE GKLTVVHETV RGDRHNSQSL LLGLTEGIKH PVSMAIASYL KEKGVSAQNV
SNTKAVTGKR VEGTSYSGLK LQGGNCRWLG HNNDPDVRKA LEQGYSVFCF SVNGSVTAVY
ALEDSLRADA VSTINLLRQR GISLHILSGD DDGAVRSMAA RLGIESSNIR SHATPAEKSE
YIKDIVEGRN CDSSSQSKRP VVVFCGDGTN DAIGLTQATI GVHINEGSEV AKLAADVVML
KPKLNNILTM ITVSQKAMFR VKLNFLWSFT YNLFAILLAA GAFVDFHIPP EYAGLGELVS
ILPVIFVAIL LRYAKI


Related products :

Catalog number Product name Quantity
EIAAB45909 ATP6V0A2,Homo sapiens,Human,Lysosomal H(+)-transporting ATPase V0 subunit a2,TJ6,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2,V-ATPase 116 kDa isoform a2,V-type proton ATPase 116 k
EIAAB45911 ATP6N1B,ATP6V0A2,Bos taurus,Bovine,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2,V-ATPase 116 kDa isoform a2,V-type proton ATPase 116 kDa subunit a isoform 2
EIAAB45910 Atp6n1b,Atp6v0a2,Immune suppressor factor J6B7,ISF,Lysosomal H(+)-transporting ATPase V0 subunit a2,Mouse,Mus musculus,ShIF,Tj6,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2,V-ATPas
EIAAB45577 ATP6V0E2,ATP6V0E2L,C7orf32,Homo sapiens,Human,Lysosomal 9 kDa H(+)-transporting ATPase V0 subunit e2,Vacuolar proton pump subunit e 2,V-ATPase subunit e 2,V-type proton ATPase subunit e 2
EIAAB45573 ATP6H,ATP6V0E,ATP6V0E1,Homo sapiens,Human,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45570 ATP6H,ATP6V0E,ATP6V0E1,Bos taurus,Bovine,Vacuolar proton pump subunit e 1,V-ATPase 9.2 kDa membrane accessory protein,V-ATPase M9.2 subunit,V-ATPase subunit e 1,V-type proton ATPase subunit e 1
EIAAB45629 ATP6AP1,ATP6IP1,ATP6S1,Bos taurus,Bovine,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45562 Atp6d,Atp6v0d1,Mouse,Mus musculus,P39,Physophilin,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,V-type proton ATPase subunit d 1
EIAAB45913 ATP6N1B,ATP6N2,ATP6V0A4,Homo sapiens,Human,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4,Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform,V-ATPase 116 kDa isofo
EIAAB45632 ATP6AP1,ATP6IP1,ATP6S1,Homo sapiens,Human,Protein XAP-3,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,VATPS1,V-type proton ATPase subunit S1,X
EIAAB45631 Atp6ap1,Atp6ip1,Atp6s1,Mouse,Mus musculus,Protein C7-1,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45630 Atp6ap1,Atp6ip1,Atp6s1,C7-1 protein,Rat,Rattus norvegicus,Vacuolar proton pump subunit S1,V-ATPase Ac45 subunit,V-ATPase S1 accessory protein,V-ATPase subunit S1,V-type proton ATPase subunit S1
EIAAB45563 32 kDa accessory protein,ATP6D,ATP6V0D1,Homo sapiens,Human,p39,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,VPATPD,V-type proton ATPase
EIAAB45564 32 kDa accessory protein,ATP6D,ATP6V0D1,Bos taurus,Bovine,P39,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,VPATPD,V-type proton ATPase
EIAAB45905 ATP6V0A1,Chicken,Gallus gallus,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 1,V-ATPase 116 kDa isoform a1,V-type proton ATPase 116 kDa subunit a isoform 1
EIAAB45914 Atp6n1b,Atp6v0a4,Mouse,Mus musculus,Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4,Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform,V-ATPase 116 kDa isoform a4,V
bs-1152P Peptides: ATP1b2_Na+K+ ATPase(ATPase, Na+_K+ transporting, beta 2 polypeptide) Protein Length:12-25 amino acids. 200ug lyophilized
EIAAB34264 ATP6AP2,ATP6IP2,ATP6M8-9,ATPase H(+)-transporting lysosomal accessory protein 2,ATPase H(+)-transporting lysosomal-interacting protein 2,CAPER,ELDF10,Embryonic liver differentiation factor 10,ER-local
EIAAB45649 ATP6A1,ATP6V1A,ATP6V1A1,Homo sapiens,Human,Vacuolar ATPase isoform VA68,Vacuolar proton pump subunit alpha,V-ATPase 69 kDa subunit,V-ATPase subunit A,VPP2,V-type proton ATPase catalytic subunit A
EIAAB45668 ATP6M,ATP6V1D,Homo sapiens,Human,Vacuolar proton pump subunit D,VATD,V-ATPase 28 kDa accessory protein,V-ATPase subunit D,V-type proton ATPase subunit D
EIAAB45669 ATP6M,ATP6V1D,Oryctolagus cuniculus,Rabbit,Vacuolar proton pump subunit D,VATD,V-ATPase 28 kDa accessory protein,V-ATPase subunit D,V-type proton ATPase subunit D
EIAAB45667 Atp6m,Atp6v1d,Mouse,Mus musculus,Vacuolar proton pump subunit D,Vatd,V-ATPase 28 kDa accessory protein,V-ATPase subunit D,V-type proton ATPase subunit D
EIAAB45670 ATP6M,ATP6V1D,Bos taurus,Bovine,Vacuolar proton pump subunit D,VATD,V-ATPase 28 kDa accessory protein,V-ATPase subunit D,V-type proton ATPase subunit D
EIAAB41970 15S Mg(2+)-ATPase p97 subunit,Rat,Rattus norvegicus,TER ATPase,Transitional endoplasmic reticulum ATPase,Valosin-containing protein,VCP,Vcp
EIAAB41971 15S Mg(2+)-ATPase p97 subunit,Bos taurus,Bovine,TER ATPase,Transitional endoplasmic reticulum ATPase,Valosin-containing protein,VCP,VCP


 

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