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Copper-transporting ATPase 1 (EC 3.6.3.54) (Copper pump 1) (Menkes disease-associated protein homolog)

 ATP7A_MOUSE             Reviewed;        1491 AA.
Q64430; A2AG69; O35101; P97422; Q64431;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
22-NOV-2017, entry version 177.
RecName: Full=Copper-transporting ATPase 1;
EC=3.6.3.54;
AltName: Full=Copper pump 1;
AltName: Full=Menkes disease-associated protein homolog;
Name=Atp7a; Synonyms=Mnk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN MOTTLED PHENOTYPES.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=8054976; DOI=10.1038/ng0494-369;
Levinson B., Vulpe C., Elder B., Martin C., Verley F., Packman S.,
Gitschier J.;
"The mottled gene is the mouse homologue of the Menkes disease gene.";
Nat. Genet. 6:369-373(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN MOTTLED PHENOTYPES.
STRAIN=BALB/cJ, DL, and ICR X Swiss Webster;
TISSUE=Embryo, and Kidney;
PubMed=8054977; DOI=10.1038/ng0494-374;
Mercer J.F.B., Grimes A., Ambrosini L., Lockhart P., Paynter J.A.,
Dierick H., Glover T.W.;
"Mutations in the murine homologue of the Menkes gene in dappled and
blotchy mice.";
Nat. Genet. 6:374-378(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN MOTTLED PHENOTYPES, AND
VARIANTS ARG-674 AND PRO-1381.
STRAIN=C3H/HeJ; TISSUE=Placenta;
PubMed=9385451;
Ohta Y., Shiraishi N., Nishikimi M.;
"Occurrence of two missense mutations in Cu-ATPase of the macular
mouse, a Menkes disease model.";
Biochem. Mol. Biol. Int. 43:913-918(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN MOTTLED PHENOTYPES.
STRAIN=CBA X C3H;
PubMed=9215672; DOI=10.1093/hmg/6.7.1037;
Grimes A., Hearn C.J., Lockhart P., Newgreen D.F., Mercer J.F.B.;
"Molecular basis of the brindled mouse mutant (Mo(br)): a murine model
of Menkes disease.";
Hum. Mol. Genet. 6:1037-1042(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND SER-1457, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; SER-362; SER-1464;
SER-1467 AND SER-1477, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, Pancreas, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May supply copper to copper-requiring proteins within
the secretory pathway, when localized in the trans-Golgi network.
Under conditions of elevated extracellular copper, it relocalized
to the plasma membrane where it functions in the efflux of copper
from cells (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate
+ Cu(+)(Side 2).
-!- SUBUNIT: Monomer. Interacts with PDZD11 (By similarity). Interacts
with ATOX1 and COMMD1 (By similarity).
{ECO:0000250|UniProtKB:Q04656}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000250|UniProtKB:Q04656}; Multi-pass membrane
protein {ECO:0000255}. Cell membrane
{ECO:0000250|UniProtKB:Q04656}; Multi-pass membrane protein
{ECO:0000255}. Note=Cycles constitutively between the trans-Golgi
network (TGN) and the plasma membrane. Predominantly found in the
TGN and relocalized to the plasma membrane in response to elevated
copper levels. {ECO:0000250|UniProtKB:Q04656}.
-!- TISSUE SPECIFICITY: Found in most tissues except liver. In the
kidney, it is detected in the proximal and distal tubules.
-!- DEVELOPMENTAL STAGE: Widespread expressed throughout development.
-!- DOMAIN: The C-terminal di-leucine, 1478-Leu-Leu-1479, is an
endocytic targeting signal which functions in retrieving recycling
from the plasma membrane to the TGN. Mutation of the di-leucine
signal results in the accumulation of the protein in the plasma
membrane (By similarity). {ECO:0000250}.
-!- DISEASE: Note=Defects in Atp7a are associated with mottled, an X-
linked recessive condition characterized by mottled pigmentation
of the coat, defects in connective tissue and neonatal or fetal
death. It is due to a defect in absorption and transport of
copper. The mottled mutants exhibit a diversity of phenotypes. Two
of these mutants are called brindled and blotchy and their
phenotypes resemble classical Menkes disease (MD) and occipital
horn syndrome (OHS) in humans, respectively. Other mutants are
called dappled, mosaic, tortoiseshell, pewter, etc.
{ECO:0000269|PubMed:8054976, ECO:0000269|PubMed:8054977,
ECO:0000269|PubMed:9215672, ECO:0000269|PubMed:9385451}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IB subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Heavy metal - Issue 79
of February 2007;
URL="https://web.expasy.org/spotlight/back_issues/079";
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EMBL; U03434; AAA57445.1; -; mRNA.
EMBL; U03736; AAB08487.1; -; mRNA.
EMBL; AB007134; BAA22369.1; -; mRNA.
EMBL; U71091; AAB37301.1; -; mRNA.
EMBL; AL672288; CAM16891.1; -; Genomic_DNA.
CCDS; CCDS41097.1; -.
PIR; S43793; S43793.
RefSeq; NP_033856.3; NM_009726.5.
UniGene; Mm.254297; -.
ProteinModelPortal; Q64430; -.
SMR; Q64430; -.
BioGrid; 198268; 28.
CORUM; Q64430; -.
IntAct; Q64430; 27.
STRING; 10090.ENSMUSP00000058840; -.
iPTMnet; Q64430; -.
PhosphoSitePlus; Q64430; -.
MaxQB; Q64430; -.
PaxDb; Q64430; -.
PRIDE; Q64430; -.
Ensembl; ENSMUST00000113557; ENSMUSP00000109186; ENSMUSG00000033792.
GeneID; 11977; -.
KEGG; mmu:11977; -.
UCSC; uc012hnn.2; mouse.
CTD; 538; -.
MGI; MGI:99400; Atp7a.
eggNOG; KOG0207; Eukaryota.
eggNOG; COG2217; LUCA.
GeneTree; ENSGT00530000063773; -.
HOGENOM; HOG000250397; -.
HOVERGEN; HBG050616; -.
InParanoid; Q64430; -.
KO; K17686; -.
BRENDA; 3.6.3.4; 3474.
Reactome; R-MMU-6803544; Ion influx/efflux at host-pathogen interface.
Reactome; R-MMU-936837; Ion transport by P-type ATPases.
ChiTaRS; Atp7a; mouse.
PRO; PR:Q64430; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000033792; -.
CleanEx; MM_ATP7A; -.
ExpressionAtlas; Q64430; baseline and differential.
Genevisible; Q64430; MM.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0005770; C:late endosome; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:HGNC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0005375; F:copper ion transmembrane transporter activity; IMP:MGI.
GO; GO:0032767; F:copper-dependent protein binding; ISO:MGI.
GO; GO:0004008; F:copper-exporting ATPase activity; IDA:MGI.
GO; GO:1903136; F:cuprous ion binding; ISO:MGI.
GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IDA:MGI.
GO; GO:0046034; P:ATP metabolic process; IMP:MGI.
GO; GO:0001568; P:blood vessel development; IMP:MGI.
GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
GO; GO:0051216; P:cartilage development; IMP:MGI.
GO; GO:0006584; P:catecholamine metabolic process; IMP:MGI.
GO; GO:0006878; P:cellular copper ion homeostasis; IMP:MGI.
GO; GO:0021954; P:central nervous system neuron development; IMP:MGI.
GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
GO; GO:0060003; P:copper ion export; IMP:MGI.
GO; GO:0015677; P:copper ion import; IMP:MGI.
GO; GO:0006825; P:copper ion transport; IDA:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0010273; P:detoxification of copper ion; IMP:MGI.
GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
GO; GO:0048251; P:elastic fiber assembly; IMP:MGI.
GO; GO:0051542; P:elastin biosynthetic process; IMP:MGI.
GO; GO:0042414; P:epinephrine metabolic process; IMP:MGI.
GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0048286; P:lung alveolus development; IMP:MGI.
GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
GO; GO:0043086; P:negative regulation of catalytic activity; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
GO; GO:0042421; P:norepinephrine biosynthetic process; IMP:MGI.
GO; GO:0042415; P:norepinephrine metabolic process; IMP:MGI.
GO; GO:0018205; P:peptidyl-lysine modification; IMP:MGI.
GO; GO:0043473; P:pigmentation; IMP:MGI.
GO; GO:0043085; P:positive regulation of catalytic activity; IMP:MGI.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISO:MGI.
GO; GO:0021860; P:pyramidal neuron development; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0002082; P:regulation of oxidative phosphorylation; IMP:MGI.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:MGI.
GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI.
GO; GO:0042428; P:serotonin metabolic process; IMP:MGI.
GO; GO:0043588; P:skin development; IMP:MGI.
GO; GO:0042093; P:T-helper cell differentiation; IMP:MGI.
GO; GO:0006568; P:tryptophan metabolic process; IMP:MGI.
GO; GO:0006570; P:tyrosine metabolic process; IMP:MGI.
CDD; cd00371; HMA; 6.
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; IPR017969; Heavy-metal-associated_CS.
InterPro; IPR006122; HMA_Cu_ion-bd.
InterPro; IPR006121; HMA_dom.
InterPro; IPR036163; HMA_dom_sf.
InterPro; IPR027256; P-typ_ATPase_IB.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00403; HMA; 6.
SUPFAM; SSF55008; SSF55008; 6.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
TIGRFAMs; TIGR00003; TIGR00003; 6.
PROSITE; PS00154; ATPASE_E1_E2; 1.
PROSITE; PS01047; HMA_1; 6.
PROSITE; PS50846; HMA_2; 6.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Copper;
Copper transport; Disease mutation; Glycoprotein; Golgi apparatus;
Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1491 Copper-transporting ATPase 1.
/FTId=PRO_0000046312.
TOPO_DOM 1 644 Cytoplasmic. {ECO:0000255}.
TRANSMEM 645 666 Helical. {ECO:0000255}.
TOPO_DOM 667 705 Extracellular. {ECO:0000255}.
TRANSMEM 706 725 Helical. {ECO:0000255}.
TOPO_DOM 726 732 Cytoplasmic. {ECO:0000255}.
TRANSMEM 733 753 Helical. {ECO:0000255}.
TOPO_DOM 754 772 Extracellular. {ECO:0000255}.
TRANSMEM 773 793 Helical. {ECO:0000255}.
TOPO_DOM 794 926 Cytoplasmic. {ECO:0000255}.
TRANSMEM 927 950 Helical. {ECO:0000255}.
TOPO_DOM 951 980 Extracellular. {ECO:0000255}.
TRANSMEM 981 1002 Helical. {ECO:0000255}.
TOPO_DOM 1003 1347 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1348 1365 Helical. {ECO:0000255}.
TOPO_DOM 1366 1376 Extracellular. {ECO:0000255}.
TRANSMEM 1377 1396 Helical. {ECO:0000255}.
TOPO_DOM 1397 1491 Cytoplasmic. {ECO:0000255}.
DOMAIN 9 75 HMA 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 172 238 HMA 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 278 344 HMA 3. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 378 444 HMA 4. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 480 546 HMA 5. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 556 622 HMA 6. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
REGION 1477 1491 PDZD11-binding. {ECO:0000250}.
MOTIF 1478 1479 Endocytosis signal. {ECO:0000250}.
COMPBIAS 356 362 Poly-Ser.
ACT_SITE 1035 1035 4-aspartylphosphate intermediate.
{ECO:0000305}.
METAL 1292 1292 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 1296 1296 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
MOD_RES 152 152 Phosphothreonine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 327 327 Phosphothreonine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 339 339 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 353 353 Phosphoserine.
{ECO:0000250|UniProtKB:P70705}.
MOD_RES 357 357 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1203 1203 Phosphothreonine.
{ECO:0000250|UniProtKB:P70705}.
MOD_RES 1421 1421 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1423 1423 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1451 1451 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1454 1454 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1457 1457 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 1460 1460 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1464 1464 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1467 1467 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1477 1477 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 677 677 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 966 966 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 674 674 H -> R (in MD).
{ECO:0000269|PubMed:9385451}.
VARIANT 1381 1381 S -> P (in MD).
{ECO:0000269|PubMed:9385451}.
CONFLICT 44 44 E -> D (in Ref. 1; AAA57445 and 4;
AAB37301). {ECO:0000305}.
CONFLICT 103 103 I -> V (in Ref. 1; AAA57445 and 4;
AAB37301). {ECO:0000305}.
CONFLICT 172 172 M -> R (in Ref. 1; AAA57445 and 4;
AAB37301). {ECO:0000305}.
CONFLICT 245 246 LK -> PI (in Ref. 2; AAB08487).
{ECO:0000305}.
CONFLICT 445 445 P -> PA (in Ref. 2; AAB08487 and 4;
AAB37301). {ECO:0000305}.
CONFLICT 470 470 L -> P (in Ref. 2; AAB08487, 3; BAA22369
and 4; AAB37301). {ECO:0000305}.
CONFLICT 515 515 M -> T (in Ref. 1; AAA57445 and 4;
AAB37301). {ECO:0000305}.
CONFLICT 717 717 C -> F (in Ref. 2; AAB08487).
{ECO:0000305}.
CONFLICT 770 770 T -> A (in Ref. 2; AAB08487).
{ECO:0000305}.
CONFLICT 775 775 P -> S (in Ref. 2; AAB08487).
{ECO:0000305}.
CONFLICT 885 885 I -> T (in Ref. 2; AAB08487).
{ECO:0000305}.
CONFLICT 1169 1169 Y -> H (in Ref. 2; AAB08487).
{ECO:0000305}.
CONFLICT 1204 1204 A -> P (in Ref. 2; AAB08487 and 4;
AAB37301). {ECO:0000305}.
CONFLICT 1217 1217 I -> M (in Ref. 1; AAA57445).
{ECO:0000305}.
CONFLICT 1253 1253 R -> Q (in Ref. 1; AAA57445).
{ECO:0000305}.
SEQUENCE 1491 AA; 161959 MW; 2FADCC6806994CA5 CRC64;
MEPSVDANSI TITVEGMTCI SCVRTIEQQI GKVNGVHHIK VSLEEKSATI IYDPKLQTPK
TLQEAIDDMG FDALLHNANP LPVLTNTVFL TVTAPLTLPW DHIQSTLLKT KGVTGVKISP
QQRSAVVTII PSVVSASQIV ELVPDLSLDM GTQEKKSGAC EEHSTPQAGE VMLKMKVEGM
TCHSCTSTIE GKVGKLQGVQ RIKVSLDNQE ATIVFQPHLI TAEEIKKQIE AVGFPAFIKK
QPKYLKLGAI DVERLKNTPV KSSEGSQQKS PSYPSDSTTM FTIEGMHCKS CVSNIESALS
TLQYVSSIVV SLENRSAIVK YNASLVTPEM LRKAIEAISP GQYRVSIASE VESTASSPSS
SSLQKMPLNI VSQPLTQEAV ININGMTCNS CVQSIEGVIS KKPGVKSIHV SLANSTGTIE
FDPLLTSPET LREAIEDMGF DAALPDMKEP LVVIAQPSLE TPLLPSSNEL ENVMTSVQNK
CYIQVSGMTC ASCVANIERN LRREEGIYSV LVALMAGKAE VRYNPAVIQP RVIAEFIREL
GFGAMVMENA GEGNGILELV VRGMTCASCV HKIESTLTKH KGIFYCSVAL ATNKAHIKYD
PEIIGPRDII HTIGSLGFEA SLVKKDRSAN HLDHKREIKQ WRGSFLVSLF FCIPVMGLMV
YMMVMDHHLA TLHHNQNMSN EEMINMHSAM FLERQILPGL SIMNLLSLLL CLPVQFCGGW
YFYIQAYKAL KHKTANMDVL IVLATTIAFA YSLVILLVAM FERAKVNPIT FFDTPPMLFV
FIALGRWLEH IAKGKTSEAL AKLISLQATE ATIVTLNSEN LLLSEEQVDV ELVQRGDIIK
VVPGGKFPVD GRVIEGHSMV DESLITGEAM PVAKKPGSTV IAGSINQNGS LLIRATHVGA
DTTLSQIVKL VEEAQTSKAP IQQFADKLSG YFVPFIVLVS IVTLLVWIII GFQNFEIVET
YFPGYNRSIS RTETIIRFAF QASITVLCIA CPCSLGLATP TAVMVGTGVG AQNGILIKGG
EPLEMAHKVK VVVFDKTGTI THGTPVVNQV KVLVESNKIS RNKILAIVGT AESNSEHPLG
AAVTKYCKKE LDTETLGTCT DFQVVPGCGI SCKVTNIEGL LHKSNLKIEE NNIKNASLVQ
IDAINEQSST SSSMIIDAHL SNAVNTQQYK VLIGNREWMI RNGLVISNDV DESMIEHERR
GRTAVLVTID DELCGLIAIA DTVKPEAELA VHILKSMGLE VVLMTGDNSK TARSIASQVG
ITKVFAEVLP SHKVAKVKQL QEEGKRVAMV GDGINDSPAL AMANVGIAIG TGTDVAIEAA
DVVLIRNDLL DVVASIDLSR KTVKRIRINF VFALIYNLVG IPIAAGVFLP IGLVLQPWMG
SAAMAASSVS VVLSSLFLKL YRKPTYDNYE LHPRSHTGQR SPSEISVHVG IDDTSRNSPR
LGLLDRIVNY SRASINSLLS DKRSLNSVVT SEPDKHSLLV GDFREDDDTT L


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27-945 The ATP7A gene encodes the Menkes copper-translocating P-type ATPase, a ubiquitous protein that regulates the absorption of copper in the gastrointestinal tract. Inside cells, this protein has a dual 0.05 mg
SMC-398D Menke's Disease Protein_Cu2+ Transporting Atpase Protein, S60-4 Monoclonals AntibodiesS60_4 Synthetic peptide amino acids 42-61 (cytoplasmic C-terminus) of human Copper- transporting ATPase1 100ug
SMC-399D Copper Transporting ATPase2 Antibody Monoclonal, Clone number: S62-29 Host: Mouse, Isotype: IgG1 Immunogen: Synthetic peptide amino acids 3-21 (cytoplasmic N-terminus) of human Copper-transporting ATP 100ug
SMC-398D Copper Transporting ATPase1 Antibody Monoclonal, Clone number: S60-4 Host: Mouse, Isotype: IgG2b Immunogen: Synthetic peptide amino acids 42-61 (cytoplasmic C-terminus) of human Copper- transporting A 100ug
EH1732 Copper-transporting ATPase 1 Elisa Kit 96T
CSB-EL002415RA Rat Copper-transporting ATPase 2(ATP7B) ELISA kit 96T
E1425h Human ELISA Kit FOR Copper-transporting ATPase 2 96T
CSB-EL002414RA Rat Copper-transporting ATPase 1(ATP7A) ELISA kit 96T
CSB-EL002414MO Mouse Copper-transporting ATPase 1(ATP7A) ELISA kit 96T
CSB-EL002415MO Mouse Copper-transporting ATPase 2(ATP7B) ELISA kit 96T
CSB-EL002415HU Human Copper-transporting ATPase 2(ATP7B) ELISA kit 96T
CSB-EL002414HU Human Copper-transporting ATPase 1(ATP7A) ELISA kit 96T
AE54895SH Sheep Copper-transporting ATPase 2 (ATP7B) ELISA Kit 48T
CSB-EL002415RA Rat Copper-transporting ATPase 2(ATP7B) ELISA kit SpeciesRat 96T
CSB-EL002414RA Rat Copper-transporting ATPase 1(ATP7A) ELISA kit SpeciesRat 96T
CSB-EL002414MO Mouse Copper-transporting ATPase 1(ATP7A) ELISA kit SpeciesMouse 96T
CSB-EL002415SH Sheep Copper-transporting ATPase 2(ATP7B) ELISA kit SpeciesSheep 96T
CSB-EL002415HU Human Copper-transporting ATPase 2(ATP7B) ELISA kit SpeciesHuman 96T
CSB-EL002414HU Human Copper-transporting ATPase 1(ATP7A) ELISA kit SpeciesHuman 96T
CSB-EL002415MO Mouse Copper-transporting ATPase 2(ATP7B) ELISA kit SpeciesMouse 96T


 

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