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

 ATP7A_RAT               Reviewed;        1492 AA.
P70705;
08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
20-JUN-2018, entry version 170.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Astrocyte;
PubMed=9562241; DOI=10.1023/A:1006896612272;
Qian Y., Tiffany-Castiglioni E., Harris E.D.;
"Sequence of a Menkes-type Cu-transporting ATPase from rat C6 glioma
cells: comparison of the rat protein with other mammalian Cu-
transporting ATPases.";
Mol. Cell. Biochem. 181:49-61(1998).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1204, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-1465, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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}.
-!- 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). {ECO:0000250}.
-!- 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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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; U59245; AAB06393.1; -; mRNA.
PIR; S46483; S46483.
RefSeq; NP_434690.1; NM_052803.2.
RefSeq; XP_006257057.1; XM_006256995.3.
RefSeq; XP_008771556.1; XM_008773334.2.
UniGene; Rn.10554; -.
UniGene; Rn.3287; -.
ProteinModelPortal; P70705; -.
SMR; P70705; -.
IntAct; P70705; 1.
STRING; 10116.ENSRNOP00000063702; -.
iPTMnet; P70705; -.
PhosphoSitePlus; P70705; -.
PaxDb; P70705; -.
PRIDE; P70705; -.
Ensembl; ENSRNOT00000080141; ENSRNOP00000071625; ENSRNOG00000061367.
Ensembl; ENSRNOT00000091527; ENSRNOP00000073176; ENSRNOG00000061367.
GeneID; 24941; -.
KEGG; rno:24941; -.
UCSC; RGD:2179; rat.
CTD; 538; -.
RGD; 2179; Atp7a.
eggNOG; KOG0207; Eukaryota.
eggNOG; COG2217; LUCA.
GeneTree; ENSGT00530000063773; -.
HOGENOM; HOG000250397; -.
HOVERGEN; HBG050616; -.
InParanoid; P70705; -.
KO; K17686; -.
OMA; PHLITAE; -.
OrthoDB; EOG091G022E; -.
PhylomeDB; P70705; -.
BRENDA; 3.6.3.4; 5301.
Reactome; R-RNO-6803544; Ion influx/efflux at host-pathogen interface.
Reactome; R-RNO-936837; Ion transport by P-type ATPases.
PRO; PR:P70705; -.
Proteomes; UP000002494; Chromosome X.
Bgee; ENSRNOG00000061367; -.
ExpressionAtlas; P70705; baseline and differential.
Genevisible; P70705; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0031526; C:brush border membrane; IDA:RGD.
GO; GO:0031252; C:cell leading edge; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IDA:MGI.
GO; GO:0005770; C:late endosome; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005902; C:microvillus; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0030141; C:secretory granule; IDA:RGD.
GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
GO; GO:0030140; C:trans-Golgi network transport vesicle; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
GO; GO:0051087; F:chaperone binding; IPI:RGD.
GO; GO:0005375; F:copper ion transmembrane transporter activity; IMP:RGD.
GO; GO:0032767; F:copper-dependent protein binding; IEA:Ensembl.
GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl.
GO; GO:0048365; F:Rac GTPase binding; IPI:RGD.
GO; GO:0006878; P:cellular copper ion homeostasis; IMP:RGD.
GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:RGD.
GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
GO; GO:0071279; P:cellular response to cobalt ion; IEP:RGD.
GO; GO:0071280; P:cellular response to copper ion; IDA:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0071281; P:cellular response to iron ion; IEP:RGD.
GO; GO:0071284; P:cellular response to lead ion; IEP:RGD.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IMP:RGD.
GO; GO:0060003; P:copper ion export; IMP:RGD.
GO; GO:0001701; P:in utero embryonic development; IEP:RGD.
GO; GO:0007595; P:lactation; IEP:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0034760; P:negative regulation of iron ion transmembrane transport; IMP:RGD.
GO; GO:0015679; P:plasma membrane copper ion transport; IMP:RGD.
GO; GO:0045793; P:positive regulation of cell size; IMP:RGD.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:RGD.
GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:RGD.
GO; GO:0051353; P:positive regulation of oxidoreductase activity; IEA:Ensembl.
GO; GO:1903036; P:positive regulation of response to wounding; IMP:RGD.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IMP:RGD.
GO; GO:1904959; P:regulation of cytochrome-c oxidase activity; IMP:RGD.
GO; GO:0010468; P:regulation of gene expression; IMP:RGD.
GO; GO:0046688; P:response to copper ion; IDA:RGD.
GO; GO:0010041; P:response to iron(III) ion; IEP:RGD.
GO; GO:0010288; P:response to lead ion; IEP:RGD.
GO; GO:0010042; P:response to manganese ion; IDA:RGD.
GO; GO:0010043; P:response to zinc ion; IEP:RGD.
CDD; cd00371; HMA; 6.
Gene3D; 3.40.1110.10; -; 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; 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; Glycoprotein; Golgi apparatus; Hydrolase;
Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1492 Copper-transporting ATPase 1.
/FTId=PRO_0000046313.
TOPO_DOM 1 645 Cytoplasmic. {ECO:0000255}.
TRANSMEM 646 667 Helical. {ECO:0000255}.
TOPO_DOM 668 706 Extracellular. {ECO:0000255}.
TRANSMEM 707 726 Helical. {ECO:0000255}.
TOPO_DOM 727 733 Cytoplasmic. {ECO:0000255}.
TRANSMEM 734 754 Helical. {ECO:0000255}.
TOPO_DOM 755 773 Extracellular. {ECO:0000255}.
TRANSMEM 774 794 Helical. {ECO:0000255}.
TOPO_DOM 795 927 Cytoplasmic. {ECO:0000255}.
TRANSMEM 928 951 Helical. {ECO:0000255}.
TOPO_DOM 952 981 Extracellular. {ECO:0000255}.
TRANSMEM 982 1003 Helical. {ECO:0000255}.
TOPO_DOM 1004 1348 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1349 1366 Helical. {ECO:0000255}.
TOPO_DOM 1367 1377 Extracellular. {ECO:0000255}.
TRANSMEM 1378 1397 Helical. {ECO:0000255}.
TOPO_DOM 1398 1492 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 481 547 HMA 5. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 557 623 HMA 6. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
REGION 1478 1492 PDZD11-binding. {ECO:0000250}.
MOTIF 1479 1480 Endocytosis signal. {ECO:0000250}.
COMPBIAS 356 362 Poly-Ser.
ACT_SITE 1036 1036 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 1293 1293 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 1297 1297 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:0000244|PubMed:22673903}.
MOD_RES 357 357 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000250|UniProtKB:Q64430}.
MOD_RES 1204 1204 Phosphothreonine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 1422 1422 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1424 1424 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1452 1452 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1455 1455 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1458 1458 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1461 1461 Phosphoserine.
{ECO:0000250|UniProtKB:Q04656}.
MOD_RES 1465 1465 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1468 1468 Phosphoserine.
{ECO:0000250|UniProtKB:Q64430}.
MOD_RES 1478 1478 Phosphoserine.
{ECO:0000250|UniProtKB:Q64430}.
CARBOHYD 678 678 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 1492 AA; 162093 MW; 34F75152B105AE9F CRC64;
MEPNMDANSI TITVEGMTCI SCVRTIEQQI GKVNGVHHIK VSLEEKSATV IYNPKLQTPK
TLQEAIDDMG FDALLHNANP LPVLTNTVFL TVTAPLALPW DHIQSTLLKT KGVTGVKISP
QQRSAVVTII PSVVSANQIV ELVPDLSLDM GTQEKKSGTS EEHSTPQAGE VLLKMRVEGM
TCHSCTSTIE GKVGKLQGVQ RIKVSLDNQE ATIVYQPHLI TAEEIKKQIE AVGFPAFIKK
QPKYLKLGAI DVERLKSTPV KSSEGSQQKS PAYPSDSAIT FTIDGMHCKS CVSNIESALS
TLQYVSSIVV SLENRSAIVK YNASLVTPEI LRKAIEAVSP GQYRVSISSE VESPTSSPSS
SSLQKMPLNL VSQPLTQEVV ININGMTCNS CVQSIEGVIS KKPGVKSIHV SLTNSTGTIE
YDPLLTSPEP LREAIEDMGF DAVLPADMKE PLVVIAQPSL ETPLLPSTTE PENVMTPVQN
KCYIQVSGMT CASCVANIER NLRREEGIYS VLVALMAGKA EVRYNPAVIQ PRVIAELIRE
LGFGAVVMEN AGEGNGILEL VVRGMTCASC VHKIESTLTK HKGIFYCSVA LATNKAHIKY
DPEIIGPRDI IHTIGNLGFE ASLVKKDRSA NHLDHKREIK QWRGSFLVSL FFCIPVMGLM
IYMMVMDHHL ATLNHNQNMS NEEMINMHSS MFLERQILPG LSIMNLLSLL LCLPVQFCGG
WYFYIQAYKA LRHKTANMDV LIVLATTIAF AYSLVILLVA MYERAKVNPI TFFDTPPMLF
VFIALGRWLE HIAKGKTSEA LAKLISLQAT EATIVTLNSE NLLLSEEQVD VELVQRGDII
KVVPGGKFPV DGRVIEGHSM VDESLITGEA MPVAKKPGST VIAGSINQNG SLLIRATHVG
ADTTLSQIVK LVEEAQTSKA PIQQFADKLS GYFVPFIVLV SIVTLLVWII IGFQNFEIVE
AYFPGYNRSI SRTETIIRFA FQASITVLCI ACPCSLGLAT PTAVMVGTGV GAQNGILIKG
GEPLEMAHKV KVVVFDKTGT ITHGTPVVNQ VKVLVESNKI SRNKILAIVG TAESNSEHPL
GAAVTKYCKQ ELDTETLGTC TDFQVVPGCG ISCKVTNIEG LLHKSNLKIE ENNIKNASLV
QIDAINEQSS PSSSMIIDAH LSNAVNTQQY KVLIGNREWM IRNGLVISND VDESMIEHER
RGRTAVLVTI DDELCGLIAI ADTVKPEAEL AVHILKSMGL EVVLMTGDNS KTARSIASQV
GITKVFAEVL PSHKVAKVKQ LQEEGKRVAM VGDGINDSPA LAMASVGIAI GTGTDVAIEA
ADVVLIRNDL LDVVASIDLS RKTVKRIRIN FVFALIYNLI GIPIAAGVFL PIGLVLQPWM
GSAAMAASSV SVVLSSLFLK LYRKPTYDNY ELRPRSHTGQ RSPSEISVHV GIDDTSRNSP
RLGLLDRIVN YSRASINSLL SDKRSLNSVV TSEPDKHSLL VGDFREDDDT TL


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