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P70705 (ATP7A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-transporting ATPase 1

EC=3.6.3.54
Alternative name(s):
Copper pump 1
Menkes disease-associated protein homolog
Gene names
Name:Atp7a
Synonyms:Mnk
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1492 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Catalytic activity

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

Subunit structure

Monomer By similarity. Interacts with PDZD11 By similarity.

Subcellular location

Golgi apparatustrans-Golgi network membrane; Multi-pass membrane protein By similarity. Cell membrane; 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.

Domain

The C-terminal di-leucine, 1479-Leu-Leu-1480, 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.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 6 HMA domains.

Ontologies

Keywords
   Biological processCopper transport
Ion transport
Transport
   Cellular componentCell membrane
Golgi apparatus
Membrane
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Copper
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT-helper cell differentiation

Inferred from electronic annotation. Source: Ensembl

blood vessel development

Inferred from electronic annotation. Source: Ensembl

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

cartilage development

Inferred from electronic annotation. Source: Ensembl

cellular copper ion homeostasis

Inferred from mutant phenotype PubMed 22442359. Source: RGD

cerebellar Purkinje cell differentiation

Inferred from electronic annotation. Source: Ensembl

collagen fibril organization

Inferred from electronic annotation. Source: Ensembl

copper ion import

Inferred from electronic annotation. Source: Ensembl

dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

detoxification of copper ion

Inferred from electronic annotation. Source: Ensembl

dopamine metabolic process

Inferred from electronic annotation. Source: Ensembl

elastic fiber assembly

Inferred from electronic annotation. Source: Ensembl

elastin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

epinephrine metabolic process

Inferred from electronic annotation. Source: Ensembl

hair follicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from expression pattern PubMed 10864443. Source: RGD

lactation

Inferred from expression pattern PubMed 16741141. Source: RGD

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

lung alveolus development

Inferred from electronic annotation. Source: Ensembl

negative regulation of metalloenzyme activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

norepinephrine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

peptidyl-lysine modification

Inferred from electronic annotation. Source: Ensembl

pigmentation

Inferred from electronic annotation. Source: Ensembl

plasma membrane copper ion transport

Inferred from mutant phenotype PubMed 22442359. Source: RGD

positive regulation of metalloenzyme activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of oxidoreductase activity

Inferred from electronic annotation. Source: Ensembl

pyramidal neuron development

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

regulation of oxidative phosphorylation

Inferred from electronic annotation. Source: Ensembl

release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

removal of superoxide radicals

Inferred from electronic annotation. Source: Ensembl

response to copper ion

Inferred from direct assay PubMed 17158254. Source: RGD

response to iron(III) ion

Inferred from expression pattern PubMed 16629162. Source: RGD

response to zinc ion

Inferred from expression pattern PubMed 12840169. Source: RGD

serotonin metabolic process

Inferred from electronic annotation. Source: Ensembl

tryptophan metabolic process

Inferred from electronic annotation. Source: Ensembl

tyrosine metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 15634787. Source: MGI

basolateral plasma membrane

Inferred from direct assay PubMed 16081413. Source: RGD

brush border membrane

Inferred from direct assay PubMed 16081413. Source: RGD

integral component of membrane

Inferred from direct assay PubMed 12488345. Source: MGI

late endosome

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17158254. Source: RGD

secretory granule

Inferred from direct assay PubMed 16185750. Source: RGD

trans-Golgi network

Inferred from direct assay PubMed 12488345. Source: MGI

trans-Golgi network transport vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

copper ion transmembrane transporter activity

Inferred from mutant phenotype PubMed 22442359. Source: RGD

copper-exporting ATPase activity

Inferred from electronic annotation. Source: Ensembl

superoxide dismutase copper chaperone activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14921492Copper-transporting ATPase 1
PRO_0000046313

Regions

Topological domain1 – 645645Cytoplasmic Potential
Transmembrane646 – 66722Helical; Potential
Topological domain668 – 70639Extracellular Potential
Transmembrane707 – 72620Helical; Potential
Topological domain727 – 7337Cytoplasmic Potential
Transmembrane734 – 75421Helical; Potential
Topological domain755 – 77319Extracellular Potential
Transmembrane774 – 79421Helical; Potential
Topological domain795 – 927133Cytoplasmic Potential
Transmembrane928 – 95124Helical; Potential
Topological domain952 – 98130Extracellular Potential
Transmembrane982 – 100322Helical; Potential
Topological domain1004 – 1348345Cytoplasmic Potential
Transmembrane1349 – 136618Helical; Potential
Topological domain1367 – 137711Extracellular Potential
Transmembrane1378 – 139720Helical; Potential
Topological domain1398 – 149295Cytoplasmic Potential
Domain9 – 7567HMA 1
Domain172 – 23867HMA 2
Domain278 – 34467HMA 3
Domain378 – 44467HMA 4
Domain481 – 54767HMA 5
Domain557 – 62367HMA 6
Region1478 – 149215PDZD11-binding By similarity
Motif1479 – 14802Endocytosis signal By similarity
Compositional bias356 – 3627Poly-Ser

Sites

Active site103614-aspartylphosphate intermediate By similarity
Metal binding12931Magnesium By similarity
Metal binding12971Magnesium By similarity

Amino acid modifications

Modified residue3391Phosphoserine By similarity
Modified residue3571Phosphoserine By similarity
Modified residue12041Phosphothreonine Ref.2
Modified residue14581Phosphoserine By similarity
Glycosylation6781N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P70705 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 34F75152B105AE9F

FASTA1,492162,093
        10         20         30         40         50         60 
MEPNMDANSI TITVEGMTCI SCVRTIEQQI GKVNGVHHIK VSLEEKSATV IYNPKLQTPK 

        70         80         90        100        110        120 
TLQEAIDDMG FDALLHNANP LPVLTNTVFL TVTAPLALPW DHIQSTLLKT KGVTGVKISP 

       130        140        150        160        170        180 
QQRSAVVTII PSVVSANQIV ELVPDLSLDM GTQEKKSGTS EEHSTPQAGE VLLKMRVEGM 

       190        200        210        220        230        240 
TCHSCTSTIE GKVGKLQGVQ RIKVSLDNQE ATIVYQPHLI TAEEIKKQIE AVGFPAFIKK 

       250        260        270        280        290        300 
QPKYLKLGAI DVERLKSTPV KSSEGSQQKS PAYPSDSAIT FTIDGMHCKS CVSNIESALS 

       310        320        330        340        350        360 
TLQYVSSIVV SLENRSAIVK YNASLVTPEI LRKAIEAVSP GQYRVSISSE VESPTSSPSS 

       370        380        390        400        410        420 
SSLQKMPLNL VSQPLTQEVV ININGMTCNS CVQSIEGVIS KKPGVKSIHV SLTNSTGTIE 

       430        440        450        460        470        480 
YDPLLTSPEP LREAIEDMGF DAVLPADMKE PLVVIAQPSL ETPLLPSTTE PENVMTPVQN 

       490        500        510        520        530        540 
KCYIQVSGMT CASCVANIER NLRREEGIYS VLVALMAGKA EVRYNPAVIQ PRVIAELIRE 

       550        560        570        580        590        600 
LGFGAVVMEN AGEGNGILEL VVRGMTCASC VHKIESTLTK HKGIFYCSVA LATNKAHIKY 

       610        620        630        640        650        660 
DPEIIGPRDI IHTIGNLGFE ASLVKKDRSA NHLDHKREIK QWRGSFLVSL FFCIPVMGLM 

       670        680        690        700        710        720 
IYMMVMDHHL ATLNHNQNMS NEEMINMHSS MFLERQILPG LSIMNLLSLL LCLPVQFCGG 

       730        740        750        760        770        780 
WYFYIQAYKA LRHKTANMDV LIVLATTIAF AYSLVILLVA MYERAKVNPI TFFDTPPMLF 

       790        800        810        820        830        840 
VFIALGRWLE HIAKGKTSEA LAKLISLQAT EATIVTLNSE NLLLSEEQVD VELVQRGDII 

       850        860        870        880        890        900 
KVVPGGKFPV DGRVIEGHSM VDESLITGEA MPVAKKPGST VIAGSINQNG SLLIRATHVG 

       910        920        930        940        950        960 
ADTTLSQIVK LVEEAQTSKA PIQQFADKLS GYFVPFIVLV SIVTLLVWII IGFQNFEIVE 

       970        980        990       1000       1010       1020 
AYFPGYNRSI SRTETIIRFA FQASITVLCI ACPCSLGLAT PTAVMVGTGV GAQNGILIKG 

      1030       1040       1050       1060       1070       1080 
GEPLEMAHKV KVVVFDKTGT ITHGTPVVNQ VKVLVESNKI SRNKILAIVG TAESNSEHPL 

      1090       1100       1110       1120       1130       1140 
GAAVTKYCKQ ELDTETLGTC TDFQVVPGCG ISCKVTNIEG LLHKSNLKIE ENNIKNASLV 

      1150       1160       1170       1180       1190       1200 
QIDAINEQSS PSSSMIIDAH LSNAVNTQQY KVLIGNREWM IRNGLVISND VDESMIEHER 

      1210       1220       1230       1240       1250       1260 
RGRTAVLVTI DDELCGLIAI ADTVKPEAEL AVHILKSMGL EVVLMTGDNS KTARSIASQV 

      1270       1280       1290       1300       1310       1320 
GITKVFAEVL PSHKVAKVKQ LQEEGKRVAM VGDGINDSPA LAMASVGIAI GTGTDVAIEA 

      1330       1340       1350       1360       1370       1380 
ADVVLIRNDL LDVVASIDLS RKTVKRIRIN FVFALIYNLI GIPIAAGVFL PIGLVLQPWM 

      1390       1400       1410       1420       1430       1440 
GSAAMAASSV SVVLSSLFLK LYRKPTYDNY ELRPRSHTGQ RSPSEISVHV GIDDTSRNSP 

      1450       1460       1470       1480       1490 
RLGLLDRIVN YSRASINSLL SDKRSLNSVV TSEPDKHSLL VGDFREDDDT TL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of a Menkes-type Cu-transporting ATPase from rat C6 glioma cells: comparison of the rat protein with other mammalian Cu-transporting ATPases."
Qian Y., Tiffany-Castiglioni E., Harris E.D.
Mol. Cell. Biochem. 181:49-61(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Astrocyte.
[2]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Protein Spotlight

Heavy metal - Issue 79 of February 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59245 mRNA. Translation: AAB06393.1.
PIRS46483.
RefSeqNP_434690.1. NM_052803.2.
XP_006257057.1. XM_006256995.1.
XP_006257058.1. XM_006256996.1.
UniGeneRn.10554.

3D structure databases

ProteinModelPortalP70705.
SMRP70705. Positions 1-79, 164-246, 275-351, 375-444, 475-625.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP70705.

Proteomic databases

PaxDbP70705.
PRIDEP70705.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000065388; ENSRNOP00000063702; ENSRNOG00000002515.
GeneID24941.
KEGGrno:24941.
UCSCRGD:2179. rat.

Organism-specific databases

CTD538.
RGD2179. Atp7a.

Phylogenomic databases

eggNOGCOG2217.
GeneTreeENSGT00530000063773.
HOGENOMHOG000250397.
HOVERGENHBG050616.
KOK17686.
OMAEYEDREQ.
OrthoDBEOG7C2R0G.
PhylomeDBP70705.

Enzyme and pathway databases

BRENDA3.6.3.4. 5301.

Gene expression databases

GenevestigatorP70705.

Family and domain databases

Gene3D2.70.150.10. 1 hit.
3.40.1110.10. 2 hits.
3.40.50.1000. 2 hits.
InterProIPR023299. 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]
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 6 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SUPFAMSSF55008. SSF55008. 6 hits.
SSF56784. SSF56784. 2 hits.
TIGRFAMsTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
TIGR00003. TIGR00003. 6 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 6 hits.
PS50846. HMA_2. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio604931.
PROP70705.

Entry information

Entry nameATP7A_RAT
AccessionPrimary (citable) accession number: P70705
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries