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Copper-transporting ATPase 2 (EC 3.6.3.54) (Copper pump 2) (Pineal night-specific ATPase) (Wilson disease-associated protein homolog)

 ATP7B_RAT               Reviewed;        1451 AA.
Q64535; Q63676; Q9JLY3;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 153.
RecName: Full=Copper-transporting ATPase 2;
EC=3.6.3.54 {ECO:0000250|UniProtKB:P35670};
AltName: Full=Copper pump 2;
AltName: Full=Pineal night-specific ATPase;
AltName: Full=Wilson disease-associated protein homolog;
Name=Atp7b; Synonyms=Pina, Wnd;
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], AND INVOLVEMENT IN LEC.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=7951327; DOI=10.1038/ng0894-541;
Wu J., Forbes J.R., Chen H.S., Cox D.W.;
"The LEC rat has a deletion in the copper transporting ATPase gene
homologous to the Wilson disease gene.";
Nat. Genet. 7:541-545(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
STRAIN=Sprague-Dawley; TISSUE=Pineal gland;
PubMed=9920665;
Borjigin J., Payne A.S., Deng J., Li X., Wang M.M., Ovodenko B.,
Gitlin J.D., Snyder S.H.;
"A novel pineal night-specific ATPase encoded by the Wilson disease
gene.";
J. Neurosci. 19:1018-1026(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 530-616, AND INVOLVEMENT IN LEC.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=8037655; DOI=10.1042/bj3010001;
Yamaguchi Y., Heiny M.E., Shimizu N., Aoki T., Gitlin J.D.;
"Expression of the Wilson disease gene is deficient in the Long-Evans
Cinnamon rat.";
Biochem. J. 301:1-4(1994).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469; SER-471; SER-474;
SER-1384 AND SER-1443, 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: Copper ion transmembrane transporter involved in the
export of copper out of the cells, such as the efflux of hepatic
copper into the bile. {ECO:0000250|UniProtKB:P35670}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate
+ Cu(+)(Side 2). {ECO:0000250|UniProtKB:P35670}.
-!- SUBUNIT: Monomer. Interacts with COMMD1/MURR1 (By similarity).
Interacts with DCTN4, in a copper-dependent manner (By
similarity). Interacts with ATOX1 (By similarity). Interacts (via
C-terminus) with ZBTB16/PLZF (By similarity).
{ECO:0000250|UniProtKB:P35670}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000250|UniProtKB:P35670}; Multi-pass membrane
protein {ECO:0000255}. Late endosome
{ECO:0000250|UniProtKB:P35670}. Note=Predominantly found in the
trans-Golgi network (TGN). Not redistributed to the plasma
membrane in response to elevated copper levels.
{ECO:0000250|UniProtKB:P35670}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Name=Long;
IsoId=Q64535-1; Sequence=Displayed;
Name=Short;
IsoId=Q64535-2; Sequence=VSP_000428;
Note=Produced by alternative splicing. Does not show copper
transport activity.;
Name=PINAM2;
IsoId=Q64535-3; Sequence=VSP_018666;
Note=Produced by alternative initiation at Met-815 of isoform
Long. Shows copper transport activity.;
-!- TISSUE SPECIFICITY: Expressed in brain, liver, kidney, spleen and
stomach. In brain, detected in neuronal cells of the hippocampal
formation, olfactory bulbs, cerebellum, cerebral cortex and nuclei
in the brainstem. Isoform PINA is expressed during night in adult
pineal gland (pinealocytes) and retina. Isoform PINA is not
detected in other tissue.
-!- DEVELOPMENTAL STAGE: Isoform PINA is expressed during daytime in
embryonic pineal (postnatal day 2 and 7) and embryonic retinal
pigment epithelium (embryonic day 14.5 and postnatal day 16).
Daytime expression disappears in pineal at postnatal day 16 and in
adult retina.
-!- DOMAIN: Each HMA domain can bind a copper ion, they are tightly
packed and closely interact with each other. Wild-type ATP7B can
usually be loaded with an average 5.5 copper atoms per molecule
(By similarity). {ECO:0000250}.
-!- DISEASE: Note=Deficiency of Atp7b expression is the cause of the
Long-Evans Cinnamon (LEC) phenotype, inherited in an autosomal
recessive manner, characterized by excessive hepatic copper
accumulation, defective holoceruloplasmin biosynthesis, impaired
biliary copper excretion and the development of necrotizing
hepatitis by 4 months of age. {ECO:0000269|PubMed:7951327,
ECO:0000269|PubMed:8037655}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IB subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U08344; AAA62157.1; -; mRNA.
EMBL; AF120492; AAD16009.1; -; mRNA.
EMBL; L28173; AAA21810.1; -; mRNA.
PIR; I58124; I58124.
UniGene; Rn.10025; -.
ProteinModelPortal; Q64535; -.
SMR; Q64535; -.
STRING; 10116.ENSRNOP00000054880; -.
iPTMnet; Q64535; -.
PhosphoSitePlus; Q64535; -.
PaxDb; Q64535; -.
PRIDE; Q64535; -.
UCSC; RGD:2180; rat. [Q64535-1]
RGD; 2180; Atp7b.
eggNOG; KOG0207; Eukaryota.
eggNOG; COG2217; LUCA.
HOVERGEN; HBG050616; -.
InParanoid; Q64535; -.
PhylomeDB; Q64535; -.
BRENDA; 3.6.3.4; 5301.
PRO; PR:Q64535; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0045177; C:apical part of cell; IDA:RGD.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0005923; C:bicellular tight junction; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; IDA:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0070160; C:occluding junction; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISO:RGD.
GO; GO:0005507; F:copper ion binding; IDA:RGD.
GO; GO:0005375; F:copper ion transmembrane transporter activity; IDA:RGD.
GO; GO:0004008; F:copper-exporting ATPase activity; ISO:RGD.
GO; GO:0043682; F:copper-transporting ATPase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:RGD.
GO; GO:0006878; P:cellular copper ion homeostasis; ISO:RGD.
GO; GO:0071280; P:cellular response to copper ion; IDA:RGD.
GO; GO:0071287; P:cellular response to manganese ion; IDA:RGD.
GO; GO:0006882; P:cellular zinc ion homeostasis; ISO:RGD.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:0060003; P:copper ion export; IMP:RGD.
GO; GO:0015677; P:copper ion import; ISO:RGD.
GO; GO:0006825; P:copper ion transport; ISO:RGD.
GO; GO:0015680; P:intracellular copper ion transport; ISO:RGD.
GO; GO:0007595; P:lactation; IEP:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0046688; P:response to copper ion; IEP:RGD.
GO; GO:0010042; P:response to manganese ion; IEP:RGD.
GO; GO:1990637; P:response to prolactin; IEP:RGD.
GO; GO:0010043; P:response to zinc ion; IEP:RGD.
GO; GO:0051208; P:sequestering of calcium ion; ISO:RGD.
CDD; cd00371; HMA; 6.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 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; IPR023214; HAD_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; 5.
SUPFAM; SSF55008; SSF55008; 6.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81665; SSF81665; 2.
TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
TIGRFAMs; TIGR00003; TIGR00003; 5.
PROSITE; PS00154; ATPASE_E1_E2; 1.
PROSITE; PS01047; HMA_1; 5.
PROSITE; PS50846; HMA_2; 6.
1: Evidence at protein level;
Alternative initiation; Alternative splicing; ATP-binding;
Biological rhythms; Complete proteome; Copper; Copper transport;
Endosome; Golgi apparatus; Hydrolase; Ion transport; Magnesium;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 1451 Copper-transporting ATPase 2.
/FTId=PRO_0000002511.
TOPO_DOM 1 646 Cytoplasmic. {ECO:0000255}.
TRANSMEM 647 668 Helical. {ECO:0000255}.
TOPO_DOM 669 690 Extracellular. {ECO:0000255}.
TRANSMEM 691 710 Helical. {ECO:0000255}.
TOPO_DOM 711 717 Cytoplasmic. {ECO:0000255}.
TRANSMEM 718 738 Helical. {ECO:0000255}.
TOPO_DOM 739 757 Extracellular. {ECO:0000255}.
TRANSMEM 758 778 Helical. {ECO:0000255}.
TOPO_DOM 779 912 Cytoplasmic. {ECO:0000255}.
TRANSMEM 913 935 Helical. {ECO:0000255}.
TOPO_DOM 936 965 Extracellular. {ECO:0000255}.
TRANSMEM 966 987 Helical. {ECO:0000255}.
TOPO_DOM 988 1310 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1311 1328 Helical. {ECO:0000255}.
TOPO_DOM 1329 1339 Extracellular. {ECO:0000255}.
TRANSMEM 1340 1357 Helical. {ECO:0000255}.
TOPO_DOM 1358 1451 Cytoplasmic. {ECO:0000255}.
DOMAIN 58 124 HMA 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 143 209 HMA 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 257 323 HMA 3. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 356 422 HMA 4. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 482 548 HMA 5. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 558 624 HMA 6. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
COMPBIAS 921 924 Poly-Ile.
ACT_SITE 1020 1020 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 68 68 Copper 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 71 71 Copper 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 153 153 Copper 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 156 156 Copper 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 267 267 Copper 3. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 270 270 Copper 3. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 492 492 Copper 5. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 495 495 Copper 5. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 568 568 Copper 6. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 571 571 Copper 6. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 1255 1255 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 1259 1259 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 471 471 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 474 474 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1384 1384 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1443 1443 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 1 814 Missing (in isoform PINAM2).
{ECO:0000305}.
/FTId=VSP_018666.
VAR_SEQ 1 788 Missing (in isoform Short).
{ECO:0000303|PubMed:9920665}.
/FTId=VSP_000428.
CONFLICT 1194 1195 SI -> IY (in Ref. 2; AAD16009).
{ECO:0000305}.
CONFLICT 1281 1281 D -> E (in Ref. 2; AAD16009).
{ECO:0000305}.
CONFLICT 1346 1346 A -> AMA (in Ref. 2; AAD16009).
{ECO:0000305}.
SEQUENCE 1451 AA; 155990 MW; 2029940643318401 CRC64;
MPEQERKVTA KEASRKILSK LALPTRPWGQ SMKQSFAFDN VGYEGGLDST CFILQLTTGV
VSILGMTCHS CVKSIEDRIS SLKGIVSIKV SLEQGSATVK YVPSVLNLQQ ICLQIEDMGF
EASAAEGKAA SWPSRSSPAQ EAVVKLRVEG MTCQSCVSSI EGKIRKLQGV VRVKVSLSNQ
EAVITYQPYL IQPEDLRDHI CDMGFEAAIK NRTAPLRLGP IDINKLESTN LKRAAVPPIQ
NSNHLETPGH QQNHLATLPL RIDGMHCKSC VLNIEGNIGQ LPGVQNIHVS LENKTAQVQY
DSSCITPLFL QTAIEALPPG YFKVSLPDGL EKESGSSSVP SLGSSQRQQE PGPCRTAVLT
ITGIPRDSSV QPMEDMLSQM KGVQQIDISL AEGTGAVLYD PSVVSSDELR TAVEDMGFEV
SVNPENITTN RVSSGNSVPQ AVGDSPGSVQ NMASDTRGLL THQGPGYLSD SPPSPGGTAS
QKCFVQIKGM TCASCVSNIE RSLQRHAGIL SVLVALMSGK AEVKYDPEVI QSPRIAQLIE
DLGFEAAIME DNTVSEGDIE LIITGMTCAS CVHNIESKLT RTNGITYASV ALATSKAHVK
FDPEIIGPRD IIKVIEEIGF HASLAHRNPN AHHLDHKTEI KQWKKSFLCS LVFGIPVMGL
MIYMLIPSSK PHETMVLDHN IIPGLSVLNL IFFILCTFVQ FLGGWYFYVQ AYKSLRHKSA
NMDVLIVLAT TIAYAYSLVI LVVAIAEKAE KSPVTFFDTP PMLFVFIALG RWLEHVAKSK
TSEALAKLMS LQATEATVVT LGEDNLILRE EQVPMELVQR GDIIKVVPGG KFPVDGKVLE
GNTMADESLI TGEAMPVTKK PGSIVIAGSI NAHGSVLIKA THVGNDTTLA QIVKLVEEAQ
MSKAPIQQLA DRFSGYFVPF IIIISTLTLV VWIIIGFVDF GIVQKYFPSP SKHISQTEVI
IRFAFQTSIT VLCIACPCSL GLATPTAVMV GTGVAAQNGV LIKGGKPLEM AHKIKTVMFD
KTGTITHGVP RVMRFLLLVD VATLSLRKVL AVVGTAEASS EHPLGVAVTK YCKEELGTET
LGYSTDFQAV PGCGISCKVS NVESILAHRG PTAHPIGVGN PPIGEGTGPQ TFSVLIGNRE
WMRRNGLTIS SDISDAMTDH EMKGQTAILV AIDGVLCGMI AIADAVKPEA ALASITLKSM
GVDVALITGD NRKTARAIAT QVGINKVFAE VLPSHKVAKV QELQNKGKKV AMVGDGVNDS
PALAQADVGI AIGTGTDVAI DAADVVLIRN DLLDVVASIH LSKRTVRRIR VNLVLALIYN
MVGIPIAAGV FMPIGIVLQP WMGSAAASSV SVVLSSLQLK CYRKPDLERY EAQAHGRMKP
LSASQVSVHV GMDDRRRDSP RATPWDQVSY VSQVSLSSLT SDRLSRHGGM AEDGGDKWSL
LLSDRDEEQC I


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