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Q64430

- ATP7A_MOUSE

UniProt

Q64430 - ATP7A_MOUSE

Protein

Copper-transporting ATPase 1

Gene

Atp7a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    ATP + H2O + Cu+(Side 1) = ADP + phosphate + Cu+(Side 2).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei1035 – 103514-aspartylphosphate intermediateCurated
    Metal bindingi1292 – 12921MagnesiumPROSITE-ProRule annotation
    Metal bindingi1296 – 12961MagnesiumPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. copper-exporting ATPase activity Source: MGI
    3. copper ion binding Source: UniProtKB
    4. copper ion transmembrane transporter activity Source: MGI
    5. protein binding Source: MGI
    6. superoxide dismutase copper chaperone activity Source: MGI

    GO - Biological processi

    1. ATP metabolic process Source: MGI
    2. blood vessel development Source: MGI
    3. blood vessel remodeling Source: MGI
    4. cartilage development Source: MGI
    5. catecholamine metabolic process Source: MGI
    6. cellular copper ion homeostasis Source: MGI
    7. central nervous system neuron development Source: MGI
    8. cerebellar Purkinje cell differentiation Source: MGI
    9. collagen fibril organization Source: MGI
    10. copper ion export Source: MGI
    11. copper ion import Source: MGI
    12. copper ion transport Source: UniProtKB
    13. dendrite morphogenesis Source: MGI
    14. detoxification of copper ion Source: MGI
    15. dopamine metabolic process Source: MGI
    16. elastic fiber assembly Source: MGI
    17. elastin biosynthetic process Source: MGI
    18. epinephrine metabolic process Source: MGI
    19. extracellular matrix organization Source: MGI
    20. hair follicle morphogenesis Source: MGI
    21. locomotory behavior Source: MGI
    22. lung alveolus development Source: MGI
    23. mitochondrion organization Source: MGI
    24. negative regulation of metalloenzyme activity Source: MGI
    25. negative regulation of neuron apoptotic process Source: MGI
    26. neuron projection morphogenesis Source: MGI
    27. norepinephrine biosynthetic process Source: MGI
    28. norepinephrine metabolic process Source: MGI
    29. peptidyl-lysine modification Source: MGI
    30. pigmentation Source: MGI
    31. positive regulation of catalytic activity Source: MGI
    32. positive regulation of metalloenzyme activity Source: MGI
    33. pyramidal neuron development Source: MGI
    34. regulation of gene expression Source: MGI
    35. regulation of oxidative phosphorylation Source: MGI
    36. release of cytochrome c from mitochondria Source: MGI
    37. removal of superoxide radicals Source: MGI
    38. serotonin metabolic process Source: MGI
    39. skin development Source: MGI
    40. T-helper cell differentiation Source: MGI
    41. tryptophan metabolic process Source: MGI
    42. tyrosine metabolic process Source: MGI

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Copper transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Copper, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.6.3.4. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Copper-transporting ATPase 1 (EC:3.6.3.54)
    Alternative name(s):
    Copper pump 1
    Menkes disease-associated protein homolog
    Gene namesi
    Name:Atp7a
    Synonyms:Mnk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:99400. Atp7a.

    Subcellular locationi

    Golgi apparatustrans-Golgi network membrane By similarity; Multi-pass membrane protein By similarity. Cell membrane By similarity; Multi-pass membrane protein By similarity
    Note: Constitutively cycles 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 By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasmic vesicle Source: MGI
    2. Golgi apparatus Source: MGI
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: MGI
    5. neuronal cell body Source: MGI
    6. neuron projection Source: MGI
    7. plasma membrane Source: MGI
    8. trans-Golgi network Source: MGI
    9. trans-Golgi network transport vesicle Source: HGNC

    Keywords - Cellular componenti

    Cell membrane, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Keywords - Diseasei

    Disease mutation

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14911491Copper-transporting ATPase 1PRO_0000046312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei339 – 3391PhosphoserineBy similarity
    Modified residuei357 – 3571Phosphoserine1 Publication
    Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi966 – 9661N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1203 – 12031PhosphothreonineBy similarity
    Modified residuei1457 – 14571Phosphoserine1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ64430.
    PaxDbiQ64430.
    PRIDEiQ64430.

    PTM databases

    PhosphoSiteiQ64430.

    Expressioni

    Tissue specificityi

    Found in most tissues except liver. In the kidney, it is detected in the proximal and distal tubules.

    Developmental stagei

    Widespread expressed throughout development.

    Gene expression databases

    ArrayExpressiQ64430.
    BgeeiQ64430.
    CleanExiMM_ATP7A.
    GenevestigatoriQ64430.

    Interactioni

    Subunit structurei

    Monomer. Interacts with PDZD11 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi198268. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64430.
    SMRiQ64430. Positions 8-624, 636-1404.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 644644CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini667 – 70539ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini726 – 7327CytoplasmicSequence Analysis
    Topological domaini754 – 77219ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini794 – 926133CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini951 – 98030ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1003 – 1347345CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1366 – 137611ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1397 – 149195CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei645 – 66622HelicalSequence AnalysisAdd
    BLAST
    Transmembranei706 – 72520HelicalSequence AnalysisAdd
    BLAST
    Transmembranei733 – 75321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei773 – 79321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei927 – 95024HelicalSequence AnalysisAdd
    BLAST
    Transmembranei981 – 100222HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1348 – 136518HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1377 – 139620HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 7567HMA 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini172 – 23867HMA 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini278 – 34467HMA 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini378 – 44467HMA 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini480 – 54667HMA 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini556 – 62267HMA 6PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1477 – 149115PDZD11-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1478 – 14792Endocytosis signalBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi356 – 3627Poly-Ser

    Domaini

    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.By similarity

    Sequence similaritiesi

    Contains 6 HMA domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2217.
    GeneTreeiENSGT00530000063773.
    HOGENOMiHOG000250397.
    HOVERGENiHBG050616.
    KOiK17686.
    OrthoDBiEOG7C2R0G.

    Family and domain databases

    Gene3Di2.70.150.10. 1 hit.
    3.40.1110.10. 2 hits.
    3.40.50.1000. 2 hits.
    InterProiIPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR027256. Cation_transp_P-typ_ATPase_IB.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    IPR006122. HMA_Cu_ion-bd.
    [Graphical view]
    PfamiPF00122. E1-E2_ATPase. 1 hit.
    PF00403. HMA. 6 hits.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SUPFAMiSSF55008. SSF55008. 6 hits.
    SSF56784. SSF56784. 2 hits.
    TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    TIGR00003. TIGR00003. 6 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    PS01047. HMA_1. 6 hits.
    PS50846. HMA_2. 6 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q64430-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPSVDANSI TITVEGMTCI SCVRTIEQQI GKVNGVHHIK VSLEEKSATI     50
    IYDPKLQTPK TLQEAIDDMG FDALLHNANP LPVLTNTVFL TVTAPLTLPW 100
    DHIQSTLLKT KGVTGVKISP QQRSAVVTII PSVVSASQIV ELVPDLSLDM 150
    GTQEKKSGAC EEHSTPQAGE VMLKMKVEGM TCHSCTSTIE GKVGKLQGVQ 200
    RIKVSLDNQE ATIVFQPHLI TAEEIKKQIE AVGFPAFIKK QPKYLKLGAI 250
    DVERLKNTPV KSSEGSQQKS PSYPSDSTTM FTIEGMHCKS CVSNIESALS 300
    TLQYVSSIVV SLENRSAIVK YNASLVTPEM LRKAIEAISP GQYRVSIASE 350
    VESTASSPSS SSLQKMPLNI VSQPLTQEAV ININGMTCNS CVQSIEGVIS 400
    KKPGVKSIHV SLANSTGTIE FDPLLTSPET LREAIEDMGF DAALPDMKEP 450
    LVVIAQPSLE TPLLPSSNEL ENVMTSVQNK CYIQVSGMTC ASCVANIERN 500
    LRREEGIYSV LVALMAGKAE VRYNPAVIQP RVIAEFIREL GFGAMVMENA 550
    GEGNGILELV VRGMTCASCV HKIESTLTKH KGIFYCSVAL ATNKAHIKYD 600
    PEIIGPRDII HTIGSLGFEA SLVKKDRSAN HLDHKREIKQ WRGSFLVSLF 650
    FCIPVMGLMV YMMVMDHHLA TLHHNQNMSN EEMINMHSAM FLERQILPGL 700
    SIMNLLSLLL CLPVQFCGGW YFYIQAYKAL KHKTANMDVL IVLATTIAFA 750
    YSLVILLVAM FERAKVNPIT FFDTPPMLFV FIALGRWLEH IAKGKTSEAL 800
    AKLISLQATE ATIVTLNSEN LLLSEEQVDV ELVQRGDIIK VVPGGKFPVD 850
    GRVIEGHSMV DESLITGEAM PVAKKPGSTV IAGSINQNGS LLIRATHVGA 900
    DTTLSQIVKL VEEAQTSKAP IQQFADKLSG YFVPFIVLVS IVTLLVWIII 950
    GFQNFEIVET YFPGYNRSIS RTETIIRFAF QASITVLCIA CPCSLGLATP 1000
    TAVMVGTGVG AQNGILIKGG EPLEMAHKVK VVVFDKTGTI THGTPVVNQV 1050
    KVLVESNKIS RNKILAIVGT AESNSEHPLG AAVTKYCKKE LDTETLGTCT 1100
    DFQVVPGCGI SCKVTNIEGL LHKSNLKIEE NNIKNASLVQ IDAINEQSST 1150
    SSSMIIDAHL SNAVNTQQYK VLIGNREWMI RNGLVISNDV DESMIEHERR 1200
    GRTAVLVTID DELCGLIAIA DTVKPEAELA VHILKSMGLE VVLMTGDNSK 1250
    TARSIASQVG ITKVFAEVLP SHKVAKVKQL QEEGKRVAMV GDGINDSPAL 1300
    AMANVGIAIG TGTDVAIEAA DVVLIRNDLL DVVASIDLSR KTVKRIRINF 1350
    VFALIYNLVG IPIAAGVFLP IGLVLQPWMG SAAMAASSVS VVLSSLFLKL 1400
    YRKPTYDNYE LHPRSHTGQR SPSEISVHVG IDDTSRNSPR LGLLDRIVNY 1450
    SRASINSLLS DKRSLNSVVT SEPDKHSLLV GDFREDDDTT L 1491
    Length:1,491
    Mass (Da):161,959
    Last modified:July 27, 2011 - v3
    Checksum:i2FADCC6806994CA5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441E → D in AAA57445. (PubMed:8054976)Curated
    Sequence conflicti44 – 441E → D in AAB37301. (PubMed:9215672)Curated
    Sequence conflicti103 – 1031I → V in AAA57445. (PubMed:8054976)Curated
    Sequence conflicti103 – 1031I → V in AAB37301. (PubMed:9215672)Curated
    Sequence conflicti172 – 1721M → R in AAA57445. (PubMed:8054976)Curated
    Sequence conflicti172 – 1721M → R in AAB37301. (PubMed:9215672)Curated
    Sequence conflicti245 – 2462LK → PI in AAB08487. (PubMed:8054977)Curated
    Sequence conflicti445 – 4451P → PA in AAB08487. (PubMed:8054977)Curated
    Sequence conflicti445 – 4451P → PA in AAB37301. (PubMed:9215672)Curated
    Sequence conflicti470 – 4701L → P in AAB08487. (PubMed:8054977)Curated
    Sequence conflicti470 – 4701L → P in BAA22369. (PubMed:9385451)Curated
    Sequence conflicti470 – 4701L → P in AAB37301. (PubMed:9215672)Curated
    Sequence conflicti515 – 5151M → T in AAA57445. (PubMed:8054976)Curated
    Sequence conflicti515 – 5151M → T in AAB37301. (PubMed:9215672)Curated
    Sequence conflicti717 – 7171C → F in AAB08487. (PubMed:8054977)Curated
    Sequence conflicti770 – 7701T → A in AAB08487. (PubMed:8054977)Curated
    Sequence conflicti775 – 7751P → S in AAB08487. (PubMed:8054977)Curated
    Sequence conflicti885 – 8851I → T in AAB08487. (PubMed:8054977)Curated
    Sequence conflicti1169 – 11691Y → H in AAB08487. (PubMed:8054977)Curated
    Sequence conflicti1204 – 12041A → P in AAB08487. (PubMed:8054977)Curated
    Sequence conflicti1204 – 12041A → P in AAB37301. (PubMed:9215672)Curated
    Sequence conflicti1217 – 12171I → M in AAA57445. (PubMed:8054976)Curated
    Sequence conflicti1253 – 12531R → Q in AAA57445. (PubMed:8054976)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti674 – 6741H → R in MD. 1 Publication
    Natural varianti1381 – 13811S → P in MD. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03434 mRNA. Translation: AAA57445.1.
    U03736 mRNA. Translation: AAB08487.1.
    AB007134 mRNA. Translation: BAA22369.1.
    U71091 mRNA. Translation: AAB37301.1.
    AL672288 Genomic DNA. Translation: CAM16891.1.
    CCDSiCCDS41097.1.
    PIRiS43793.
    RefSeqiNP_033856.3. NM_009726.5.
    UniGeneiMm.254297.

    Genome annotation databases

    EnsembliENSMUST00000113557; ENSMUSP00000109186; ENSMUSG00000033792.
    GeneIDi11977.
    KEGGimmu:11977.
    UCSCiuc012hnn.1. mouse.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Heavy metal - Issue 79 of February 2007

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03434 mRNA. Translation: AAA57445.1 .
    U03736 mRNA. Translation: AAB08487.1 .
    AB007134 mRNA. Translation: BAA22369.1 .
    U71091 mRNA. Translation: AAB37301.1 .
    AL672288 Genomic DNA. Translation: CAM16891.1 .
    CCDSi CCDS41097.1.
    PIRi S43793.
    RefSeqi NP_033856.3. NM_009726.5.
    UniGenei Mm.254297.

    3D structure databases

    ProteinModelPortali Q64430.
    SMRi Q64430. Positions 8-624, 636-1404.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198268. 1 interaction.

    PTM databases

    PhosphoSitei Q64430.

    Proteomic databases

    MaxQBi Q64430.
    PaxDbi Q64430.
    PRIDEi Q64430.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000113557 ; ENSMUSP00000109186 ; ENSMUSG00000033792 .
    GeneIDi 11977.
    KEGGi mmu:11977.
    UCSCi uc012hnn.1. mouse.

    Organism-specific databases

    CTDi 538.
    MGIi MGI:99400. Atp7a.

    Phylogenomic databases

    eggNOGi COG2217.
    GeneTreei ENSGT00530000063773.
    HOGENOMi HOG000250397.
    HOVERGENi HBG050616.
    KOi K17686.
    OrthoDBi EOG7C2R0G.

    Enzyme and pathway databases

    BRENDAi 3.6.3.4. 3474.

    Miscellaneous databases

    ChiTaRSi ATP7A. mouse.
    NextBioi 280111.
    PROi Q64430.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64430.
    Bgeei Q64430.
    CleanExi MM_ATP7A.
    Genevestigatori Q64430.

    Family and domain databases

    Gene3Di 2.70.150.10. 1 hit.
    3.40.1110.10. 2 hits.
    3.40.50.1000. 2 hits.
    InterProi IPR023299. ATPase_P-typ_cyto_domN.
    IPR018303. ATPase_P-typ_P_site.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR027256. Cation_transp_P-typ_ATPase_IB.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    IPR017969. Heavy-metal-associated_CS.
    IPR006121. HeavyMe-assoc_HMA.
    IPR006122. HMA_Cu_ion-bd.
    [Graphical view ]
    Pfami PF00122. E1-E2_ATPase. 1 hit.
    PF00403. HMA. 6 hits.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SUPFAMi SSF55008. SSF55008. 6 hits.
    SSF56784. SSF56784. 2 hits.
    TIGRFAMsi TIGR01525. ATPase-IB_hvy. 1 hit.
    TIGR01494. ATPase_P-type. 2 hits.
    TIGR00003. TIGR00003. 6 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    PS01047. HMA_1. 6 hits.
    PS50846. HMA_2. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The mottled gene is the mouse homologue of the Menkes disease gene."
      Levinson B., Vulpe C., Elder B., Martin C., Verley F., Packman S., Gitschier J.
      Nat. Genet. 6:369-373(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    2. "Mutations in the murine homologue of the Menkes gene in dappled and blotchy mice."
      Mercer J.F.B., Grimes A., Ambrosini L., Lockhart P., Paynter J.A., Dierick H., Glover T.W.
      Nat. Genet. 6:374-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c, DL and ICR X Swiss Webster.
      Tissue: Embryo and Kidney.
    3. "Occurrence of two missense mutations in Cu-ATPase of the macular mouse, a Menkes disease model."
      Ohta Y., Shiraishi N., Nishikimi M.
      Biochem. Mol. Biol. Int. 43:913-918(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-674 AND PRO-1381.
      Strain: C3H.
      Tissue: Placenta.
    4. "Molecular basis of the brindled mouse mutant (Mo(br)): a murine model of Menkes disease."
      Grimes A., Hearn C.J., Lockhart P., Newgreen D.F., Mercer J.F.B.
      Hum. Mol. Genet. 6:1037-1042(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: CBA X C3H.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND SER-1457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiATP7A_MOUSE
    AccessioniPrimary (citable) accession number: Q64430
    Secondary accession number(s): A2AG69
    , O35101, P97422, Q64431
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3