NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Astrocyte;
DOI=10.1023/A:1006896612272; PubMed=9562241 [NCBI, ExPASy, EBI, Israel, Japan]
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 SER-353; SER-356 AND SER-357, AND MASS SPECTROMETRY.
TISSUE=Kidney;
DOI=10.1073/pnas.0600895103; PubMed=16641100 [NCBI, ExPASy, EBI, Israel, Japan]
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).

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 + Cu²⁺(In) = ADP + phosphate + Cu²⁺(Out).
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Golgi apparatus, trans-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).
SIMILARITY: Belongs to the cation transport ATPase (P-type) family. Type IB subfamily.
SIMILARITY: Contains 6 HMA domains.
WEB RESOURCE: Name=Protein Spotlight; Note=Heavy metal - Issue 79 of February 2007; URL="http://www.expasy.org/spotlight/back_issues/sptlt079.shtml";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U59245; AAB06393.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S46483; S46483.

NP_434690.1; -.

3D structure databases

HSSP

Q04656; 1AW0. [HSSP ENTRY / PDB]

SMR

P70705; 1-79, 164-246, 275-351, 375-444.

ModBase

P70705.

PTM databases

PhosphoSite

P70705; -.

Organism-specific databases

RGD

2179; Atp7a.

Gene expression databases

ArrayExpress

P70705; -.

Family and domain databases

InterPro

IPR006416; ATPase-IB_hvy.
IPR001757; ATPase_P.
IPR006403; ATPase_P_cat/Cu.
IPR001877; Cu_ATPase1.
IPR006122; Cu_ion_bd.
IPR005834; Dehalogen-like_hydro.
IPR008250; E1-E2_ATPase_reg.
IPR006121; HeavyMe_transpt.
Graphical view of domain structure.

PANTHER

PTHR11939; ATPase_P; 1.

Pfam

PF00122; E1-E2_ATPase; 1.
PF00403; HMA; 6.
PF00702; Hydrolase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00119; CATATPASE.
PR00942; CUATPASEI.

TIGRFAMs

TIGR01511; ATPase-IB1_Cu; 1.
TIGR01525; ATPase-IB_hvy; 1.
TIGR01494; ATPase_P-type; 2.
TIGR00003; Cu_ion_bd; 4.

PROSITE

PS00154; ATPASE_E1_E2; 1.
PS01047; HMA_1; 6.
PS50846; HMA_2; 6.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P70705.

Genome annotation databases

Ensembl

ENSRNOG00000002515; Rattus norvegicus. [Contig view]

GeneID

24941; -.

KEGG

rno:24941; -.

Phylogenomic databases

HOVERGEN

P70705; -.

Other

ProtoNet

P70705.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell membrane; Copper; Copper transport; Glycoprotein; Golgi apparatus; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1492`	`1492`	`Copper-transporting ATPase 1.`	`PRO_0000046313`
`TOPO_DOM`	`1 645`	`645`	`Cytoplasmic (Potential).`
`TRANSMEM`	`646 667`	`22`	`Potential.`
`TOPO_DOM`	`668 706`	`39`	`Extracellular (Potential).`
`TRANSMEM`	`707 726`	`20`	`Potential.`
`TOPO_DOM`	`727 733`	`7`	`Cytoplasmic (Potential).`
`TRANSMEM`	`734 754`	`21`	`Potential.`
`TOPO_DOM`	`755 773`	`19`	`Extracellular (Potential).`
`TRANSMEM`	`774 794`	`21`	`Potential.`
`TOPO_DOM`	`795 927`	`133`	`Cytoplasmic (Potential).`
`TRANSMEM`	`928 951`	`24`	`Potential.`
`TOPO_DOM`	`952 981`	`30`	`Extracellular (Potential).`
`TRANSMEM`	`982 1003`	`22`	`Potential.`
`TOPO_DOM`	`1004 1348`	`345`	`Cytoplasmic (Potential).`
`TRANSMEM`	`1349 1366`	`18`	`Potential.`
`TOPO_DOM`	`1367 1377`	`11`	`Extracellular (Potential).`
`TRANSMEM`	`1378 1397`	`20`	`Potential.`
`TOPO_DOM`	`1398 1492`	`95`	`Cytoplasmic (Potential).`
`DOMAIN`	`9 75`	`67`	`HMA 1.`
`DOMAIN`	`172 238`	`67`	`HMA 2.`
`DOMAIN`	`278 344`	`67`	`HMA 3.`
`DOMAIN`	`378 444`	`67`	`HMA 4.`
`DOMAIN`	`481 547`	`67`	`HMA 5.`
`DOMAIN`	`557 623`	`67`	`HMA 6.`
`MOTIF`	`1479 1480`	`2`	`Endocytosis signal (By similarity).`
`COMPBIAS`	`356 362`	`7`	`Poly-Ser.`
`ACT_SITE`	`1036 1036`		`4-aspartylphosphate intermediate (By similarity).`
`METAL`	`1293 1293`		`Magnesium (By similarity).`
`METAL`	`1297 1297`		`Magnesium (By similarity).`
`MOD_RES`	`353 353`		`Phosphoserine.`
`MOD_RES`	`356 356`		`Phosphoserine.`
`MOD_RES`	`357 357`		`Phosphoserine.`
`CARBOHYD`	`678 678`		`N-linked (GlcNAc...) (Potential).`

Sequence information

Length: 1492 AA [This is the length of the unprocessed precursor]

Molecular weight: 162093 Da [This is the MW of the unprocessed precursor]

CRC64: 34F75152B105AE9F [This is a checksum on the sequence]

        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

P70705 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools