Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Copper-transporting ATPase 1

Gene

Atp7a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Active sitei10364-aspartylphosphate intermediateBy similarity1
Metal bindingi1293MagnesiumPROSITE-ProRule annotation1
Metal bindingi1297MagnesiumPROSITE-ProRule annotation1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chaperone binding Source: RGD
  • copper-exporting ATPase activity Source: GO_Central
  • copper ion binding Source: Ensembl
  • copper ion transmembrane transporter activity Source: RGD
  • Rac GTPase binding Source: RGD

GO - Biological processi

  • cellular copper ion homeostasis Source: RGD
  • cellular response to amino acid stimulus Source: RGD
  • cellular response to antibiotic Source: RGD
  • cellular response to cadmium ion Source: RGD
  • cellular response to cobalt ion Source: RGD
  • cellular response to copper ion Source: RGD
  • cellular response to hypoxia Source: RGD
  • cellular response to iron ion Source: RGD
  • cellular response to lead ion Source: RGD
  • cellular response to platelet-derived growth factor stimulus Source: RGD
  • copper ion export Source: RGD
  • in utero embryonic development Source: RGD
  • lactation Source: RGD
  • liver development Source: RGD
  • negative regulation of iron ion transmembrane transport Source: RGD
  • plasma membrane copper ion transport Source: RGD
  • positive regulation of cell size Source: RGD
  • positive regulation of epithelial cell proliferation Source: RGD
  • positive regulation of lamellipodium assembly Source: RGD
  • positive regulation of oxidoreductase activity Source: Ensembl
  • positive regulation of response to wounding Source: RGD
  • positive regulation of vascular associated smooth muscle cell migration Source: RGD
  • regulation of cytochrome-c oxidase activity Source: RGD
  • regulation of gene expression Source: RGD
  • response to copper ion Source: RGD
  • response to iron(III) ion Source: RGD
  • response to lead ion Source: RGD
  • response to manganese ion Source: RGD
  • response to zinc ion Source: RGD
Complete GO annotation...

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. 5301.
ReactomeiR-RNO-6803544. Ion influx/efflux at host-pathogen interface.
R-RNO-936837. Ion transport by P-type ATPases.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi2179. Atp7a.

Subcellular locationi

  • Golgi apparatustrans-Golgi network membrane By similarity; Multi-pass membrane protein Sequence analysis
  • Cell membrane By similarity; Multi-pass membrane protein Sequence analysis

  • 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.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 645CytoplasmicSequence analysisAdd BLAST645
Transmembranei646 – 667HelicalSequence analysisAdd BLAST22
Topological domaini668 – 706ExtracellularSequence analysisAdd BLAST39
Transmembranei707 – 726HelicalSequence analysisAdd BLAST20
Topological domaini727 – 733CytoplasmicSequence analysis7
Transmembranei734 – 754HelicalSequence analysisAdd BLAST21
Topological domaini755 – 773ExtracellularSequence analysisAdd BLAST19
Transmembranei774 – 794HelicalSequence analysisAdd BLAST21
Topological domaini795 – 927CytoplasmicSequence analysisAdd BLAST133
Transmembranei928 – 951HelicalSequence analysisAdd BLAST24
Topological domaini952 – 981ExtracellularSequence analysisAdd BLAST30
Transmembranei982 – 1003HelicalSequence analysisAdd BLAST22
Topological domaini1004 – 1348CytoplasmicSequence analysisAdd BLAST345
Transmembranei1349 – 1366HelicalSequence analysisAdd BLAST18
Topological domaini1367 – 1377ExtracellularSequence analysisAdd BLAST11
Transmembranei1378 – 1397HelicalSequence analysisAdd BLAST20
Topological domaini1398 – 1492CytoplasmicSequence analysisAdd BLAST95

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • basolateral plasma membrane Source: RGD
  • brush border membrane Source: RGD
  • cell leading edge Source: RGD
  • cytosol Source: RGD
  • Golgi apparatus Source: MGI
  • integral component of membrane Source: MGI
  • integral component of plasma membrane Source: GO_Central
  • late endosome Source: RGD
  • membrane raft Source: RGD
  • microvillus Source: RGD
  • nucleus Source: RGD
  • perikaryon Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: RGD
  • secretory granule Source: RGD
  • trans-Golgi network Source: MGI
  • trans-Golgi network transport vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000463131 – 1492Copper-transporting ATPase 1Add BLAST1492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei152PhosphothreonineBy similarity1
Modified residuei270PhosphoserineBy similarity1
Modified residuei327PhosphothreonineBy similarity1
Modified residuei339PhosphoserineBy similarity1
Modified residuei353PhosphoserineCombined sources1
Modified residuei357PhosphoserineBy similarity1
Modified residuei362PhosphoserineBy similarity1
Glycosylationi678N-linked (GlcNAc...)Sequence analysis1
Modified residuei1204PhosphothreonineCombined sources1
Modified residuei1422PhosphoserineBy similarity1
Modified residuei1424PhosphoserineBy similarity1
Modified residuei1452PhosphoserineBy similarity1
Modified residuei1455PhosphoserineBy similarity1
Modified residuei1458PhosphoserineBy similarity1
Modified residuei1461PhosphoserineBy similarity1
Modified residuei1465PhosphoserineCombined sources1
Modified residuei1468PhosphoserineBy similarity1
Modified residuei1478PhosphoserineBy similarity1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP70705.
PRIDEiP70705.

PTM databases

iPTMnetiP70705.
PhosphoSitePlusiP70705.

Expressioni

Gene expression databases

BgeeiENSRNOG00000002515.
ExpressionAtlasiP70705. baseline.
GenevisibleiP70705. RN.

Interactioni

Subunit structurei

Monomer. Interacts with PDZD11 (By similarity). Interacts with ATOX1 and COMMD1 (By similarity).By similarity

GO - Molecular functioni

  • chaperone binding Source: RGD
  • Rac GTPase binding Source: RGD

Protein-protein interaction databases

IntActiP70705. 1 interactor.
STRINGi10116.ENSRNOP00000063702.

Structurei

3D structure databases

ProteinModelPortaliP70705.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 75HMA 1PROSITE-ProRule annotationAdd BLAST67
Domaini172 – 238HMA 2PROSITE-ProRule annotationAdd BLAST67
Domaini278 – 344HMA 3PROSITE-ProRule annotationAdd BLAST67
Domaini378 – 444HMA 4PROSITE-ProRule annotationAdd BLAST67
Domaini481 – 547HMA 5PROSITE-ProRule annotationAdd BLAST67
Domaini557 – 623HMA 6PROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1478 – 1492PDZD11-bindingBy similarityAdd BLAST15

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1479 – 1480Endocytosis signalBy similarity2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi356 – 362Poly-Ser7

Domaini

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).By similarity

Sequence similaritiesi

Contains 6 HMA domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0207. Eukaryota.
COG2217. LUCA.
GeneTreeiENSGT00530000063773.
HOGENOMiHOG000250397.
HOVERGENiHBG050616.
InParanoidiP70705.
KOiK17686.
OMAiININGMT.
OrthoDBiEOG091G022E.
PhylomeDBiP70705.

Family and domain databases

CDDicd00371. HMA. 6 hits.
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.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006122. HMA_Cu_ion-bd.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 6 hits.
[Graphical view]
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.

P70705-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPNMDANSI TITVEGMTCI SCVRTIEQQI GKVNGVHHIK VSLEEKSATV
60 70 80 90 100
IYNPKLQTPK TLQEAIDDMG FDALLHNANP LPVLTNTVFL TVTAPLALPW
110 120 130 140 150
DHIQSTLLKT KGVTGVKISP QQRSAVVTII PSVVSANQIV ELVPDLSLDM
160 170 180 190 200
GTQEKKSGTS EEHSTPQAGE VLLKMRVEGM TCHSCTSTIE GKVGKLQGVQ
210 220 230 240 250
RIKVSLDNQE ATIVYQPHLI TAEEIKKQIE AVGFPAFIKK QPKYLKLGAI
260 270 280 290 300
DVERLKSTPV KSSEGSQQKS PAYPSDSAIT FTIDGMHCKS CVSNIESALS
310 320 330 340 350
TLQYVSSIVV SLENRSAIVK YNASLVTPEI LRKAIEAVSP GQYRVSISSE
360 370 380 390 400
VESPTSSPSS SSLQKMPLNL VSQPLTQEVV ININGMTCNS CVQSIEGVIS
410 420 430 440 450
KKPGVKSIHV SLTNSTGTIE YDPLLTSPEP LREAIEDMGF DAVLPADMKE
460 470 480 490 500
PLVVIAQPSL ETPLLPSTTE PENVMTPVQN KCYIQVSGMT CASCVANIER
510 520 530 540 550
NLRREEGIYS VLVALMAGKA EVRYNPAVIQ PRVIAELIRE LGFGAVVMEN
560 570 580 590 600
AGEGNGILEL VVRGMTCASC VHKIESTLTK HKGIFYCSVA LATNKAHIKY
610 620 630 640 650
DPEIIGPRDI IHTIGNLGFE ASLVKKDRSA NHLDHKREIK QWRGSFLVSL
660 670 680 690 700
FFCIPVMGLM IYMMVMDHHL ATLNHNQNMS NEEMINMHSS MFLERQILPG
710 720 730 740 750
LSIMNLLSLL LCLPVQFCGG WYFYIQAYKA LRHKTANMDV LIVLATTIAF
760 770 780 790 800
AYSLVILLVA MYERAKVNPI TFFDTPPMLF VFIALGRWLE HIAKGKTSEA
810 820 830 840 850
LAKLISLQAT EATIVTLNSE NLLLSEEQVD VELVQRGDII KVVPGGKFPV
860 870 880 890 900
DGRVIEGHSM VDESLITGEA MPVAKKPGST VIAGSINQNG SLLIRATHVG
910 920 930 940 950
ADTTLSQIVK LVEEAQTSKA PIQQFADKLS GYFVPFIVLV SIVTLLVWII
960 970 980 990 1000
IGFQNFEIVE AYFPGYNRSI SRTETIIRFA FQASITVLCI ACPCSLGLAT
1010 1020 1030 1040 1050
PTAVMVGTGV GAQNGILIKG GEPLEMAHKV KVVVFDKTGT ITHGTPVVNQ
1060 1070 1080 1090 1100
VKVLVESNKI SRNKILAIVG TAESNSEHPL GAAVTKYCKQ ELDTETLGTC
1110 1120 1130 1140 1150
TDFQVVPGCG ISCKVTNIEG LLHKSNLKIE ENNIKNASLV QIDAINEQSS
1160 1170 1180 1190 1200
PSSSMIIDAH LSNAVNTQQY KVLIGNREWM IRNGLVISND VDESMIEHER
1210 1220 1230 1240 1250
RGRTAVLVTI DDELCGLIAI ADTVKPEAEL AVHILKSMGL EVVLMTGDNS
1260 1270 1280 1290 1300
KTARSIASQV GITKVFAEVL PSHKVAKVKQ LQEEGKRVAM VGDGINDSPA
1310 1320 1330 1340 1350
LAMASVGIAI GTGTDVAIEA ADVVLIRNDL LDVVASIDLS RKTVKRIRIN
1360 1370 1380 1390 1400
FVFALIYNLI GIPIAAGVFL PIGLVLQPWM GSAAMAASSV SVVLSSLFLK
1410 1420 1430 1440 1450
LYRKPTYDNY ELRPRSHTGQ RSPSEISVHV GIDDTSRNSP RLGLLDRIVN
1460 1470 1480 1490
YSRASINSLL SDKRSLNSVV TSEPDKHSLL VGDFREDDDT TL
Length:1,492
Mass (Da):162,093
Last modified:February 1, 1997 - v1
Checksum:i34F75152B105AE9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59245 mRNA. Translation: AAB06393.1.
PIRiS46483.
RefSeqiNP_434690.1. NM_052803.2.
XP_006257057.1. XM_006256995.3.
XP_008771556.1. XM_008773334.2.
UniGeneiRn.10554.
Rn.3287.

Genome annotation databases

EnsembliENSRNOT00000080141; ENSRNOP00000071625; ENSRNOG00000061367.
ENSRNOT00000091527; ENSRNOP00000073176; ENSRNOG00000061367.
GeneIDi24941.
KEGGirno:24941.
UCSCiRGD:2179. rat.

Cross-referencesi

Web resourcesi

Protein Spotlight

Heavy metal - Issue 79 of February 2007

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59245 mRNA. Translation: AAB06393.1.
PIRiS46483.
RefSeqiNP_434690.1. NM_052803.2.
XP_006257057.1. XM_006256995.3.
XP_008771556.1. XM_008773334.2.
UniGeneiRn.10554.
Rn.3287.

3D structure databases

ProteinModelPortaliP70705.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP70705. 1 interactor.
STRINGi10116.ENSRNOP00000063702.

PTM databases

iPTMnetiP70705.
PhosphoSitePlusiP70705.

Proteomic databases

PaxDbiP70705.
PRIDEiP70705.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000080141; ENSRNOP00000071625; ENSRNOG00000061367.
ENSRNOT00000091527; ENSRNOP00000073176; ENSRNOG00000061367.
GeneIDi24941.
KEGGirno:24941.
UCSCiRGD:2179. rat.

Organism-specific databases

CTDi538.
RGDi2179. Atp7a.

Phylogenomic databases

eggNOGiKOG0207. Eukaryota.
COG2217. LUCA.
GeneTreeiENSGT00530000063773.
HOGENOMiHOG000250397.
HOVERGENiHBG050616.
InParanoidiP70705.
KOiK17686.
OMAiININGMT.
OrthoDBiEOG091G022E.
PhylomeDBiP70705.

Enzyme and pathway databases

BRENDAi3.6.3.4. 5301.
ReactomeiR-RNO-6803544. Ion influx/efflux at host-pathogen interface.
R-RNO-936837. Ion transport by P-type ATPases.

Miscellaneous databases

PROiP70705.

Gene expression databases

BgeeiENSRNOG00000002515.
ExpressionAtlasiP70705. baseline.
GenevisibleiP70705. RN.

Family and domain databases

CDDicd00371. HMA. 6 hits.
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.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006122. HMA_Cu_ion-bd.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 6 hits.
[Graphical view]
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]
ProtoNetiSearch...

Entry informationi

Entry nameiATP7A_RAT
AccessioniPrimary (citable) accession number: P70705
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: February 1, 1997
Last modified: November 30, 2016
This is version 157 of the entry and version 1 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.