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

 ATP7B_SHEEP             Reviewed;        1505 AA.
Q9XT50; O46518;
08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
07-NOV-2018, entry version 129.
RecName: Full=Copper-transporting ATPase 2;
EC=3.6.3.54 {ECO:0000250|UniProtKB:P35670};
AltName: Full=Copper pump 2;
AltName: Full=Wilson disease-associated protein homolog;
Name=ATP7B; Synonyms=WND;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
PubMed=10760584; DOI=10.1016/S0167-4781(00)00054-3;
Lockhart P.J., Wilcox S.A., Dahl H.-H.M., Mercer J.F.B.;
"Cloning, mapping and expression analysis of the sheep wilson disease
gene homologue.";
Biochim. Biophys. Acta 1491:229-239(2000).
-!- 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; Named isoforms=2;
Name=Long;
IsoId=Q9XT50-1; Sequence=Displayed;
Name=Short;
IsoId=Q9XT50-2; Sequence=VSP_000429, VSP_000430;
-!- TISSUE SPECIFICITY: The short isoform is expressed primarily in
the liver with lower levels present in the intestine, hypothalamus
and ovary. The long isoform is expressed in the liver.
-!- 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}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IB subfamily. {ECO:0000305}.
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EMBL; AF118225; AAD39371.1; -; mRNA.
EMBL; AF032881; AAB94620.1; -; mRNA.
RefSeq; NP_001009732.1; NM_001009732.1. [Q9XT50-1]
UniGene; Oar.747; -.
ProteinModelPortal; Q9XT50; -.
SMR; Q9XT50; -.
PRIDE; Q9XT50; -.
GeneID; 443046; -.
KEGG; oas:443046; -.
CTD; 540; -.
HOVERGEN; HBG050616; -.
KO; K17686; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005507; F:copper ion binding; IEA:InterPro.
GO; GO:0043682; F:copper-transporting ATPase activity; ISS:UniProtKB.
GO; GO:0006825; P:copper ion transport; ISS:UniProtKB.
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; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81665; SSF81665; 1.
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.
2: Evidence at transcript level;
Alternative splicing; ATP-binding; 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 1505 Copper-transporting ATPase 2.
/FTId=PRO_0000046316.
TOPO_DOM 1 694 Cytoplasmic. {ECO:0000255}.
TRANSMEM 695 716 Helical. {ECO:0000255}.
TOPO_DOM 717 737 Extracellular. {ECO:0000255}.
TRANSMEM 738 757 Helical. {ECO:0000255}.
TOPO_DOM 758 764 Cytoplasmic. {ECO:0000255}.
TRANSMEM 765 785 Helical. {ECO:0000255}.
TOPO_DOM 786 804 Extracellular. {ECO:0000255}.
TRANSMEM 805 825 Helical. {ECO:0000255}.
TOPO_DOM 826 959 Cytoplasmic. {ECO:0000255}.
TRANSMEM 960 982 Helical. {ECO:0000255}.
TOPO_DOM 983 1012 Extracellular. {ECO:0000255}.
TRANSMEM 1013 1034 Helical. {ECO:0000255}.
TOPO_DOM 1035 1362 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1363 1380 Helical. {ECO:0000255}.
TOPO_DOM 1381 1391 Extracellular. {ECO:0000255}.
TRANSMEM 1392 1411 Helical. {ECO:0000255}.
TOPO_DOM 1412 1505 Cytoplasmic. {ECO:0000255}.
DOMAIN 114 180 HMA 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 199 265 HMA 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 310 376 HMA 3. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 401 467 HMA 4. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 530 596 HMA 5. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
DOMAIN 606 672 HMA 6. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
COMPBIAS 968 971 Poly-Ile.
ACT_SITE 1067 1067 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 124 124 Copper 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 127 127 Copper 1. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 209 209 Copper 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 212 212 Copper 2. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 320 320 Copper 3. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 323 323 Copper 3. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 411 411 Copper 4. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 414 414 Copper 4. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 540 540 Copper 5. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 543 543 Copper 5. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 616 616 Copper 6. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 619 619 Copper 6. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 1307 1307 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
METAL 1311 1311 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00280}.
MOD_RES 519 519 Phosphoserine.
{ECO:0000250|UniProtKB:P35670}.
MOD_RES 1438 1438 Phosphoserine.
{ECO:0000250|UniProtKB:Q64535}.
VAR_SEQ 1 61 Missing (in isoform Short).
{ECO:0000303|PubMed:10760584}.
/FTId=VSP_000429.
VAR_SEQ 62 79 GEFSQKVLNGSEEISSKQ -> MKPEEERPIIDREKASRR
(in isoform Short).
{ECO:0000303|PubMed:10760584}.
/FTId=VSP_000430.
SEQUENCE 1505 AA; 161019 MW; 63202B55EB2CA8B5 CRC64;
MERAGDQAPG NPEPSSLATL GDPQVTLLTV HKRWSFKRSP GTGGSSRPVI SEEECPPPSE
EGEFSQKVLN GSEEISSKQI LSKLFQPAMK QSFAFDNNGY EDDLDGVCPS QTAAGTISIV
GMTCQSCVKS IEGRVSSLKG IVSIKVSLEQ SSAEVRYVPS VVSLMQICHQ IEDMGFQASV
AEGKATSWAS RVSPTSEAVV KLRVEGMTCQ SCVSSIEGKI GKLQGVMRVR VSLSNQEAVI
TYQPYLIQPQ DLRDHITDMG FEAVIKNKVA PVSLGPIDVR RLQSTLSVAP PAPVNQNDNN
SETPGGQGVP LHLRVDGMHC KSCVLNIEDN IGQLPGVQSI HVSLESRTAR VQYNPSLVSP
GALRRAIEAL PPGNFKVSFP NGAEGSGPDS RTPPAPSAPC TMMLAIAGMT CKSCVQSIEG
LISQRVGVHQ ISVFLAEGTA VVLYDPSRTH PEELRAAVED MGFEASILAE NCSSNQVGNH
SAGSAVGPEA AGAPVPMQGE APQPGGLHTN HIPHQSPKSL LASTTVAPKK CFLQISGMTC
ASCVSNIERN LQKEPGILSV LVALMAGKAE VKYNPEAIQP LEIAKLVQDL GFEAAVMEDY
TGSDGDLELM ITGMTCASCV HNIESKLRRT EGITYASVAL ATSKAHVKFD PEIIGPRDIV
KLIEEIGFRA SLAQRIPNAH HLDHKVEIKQ WKNSFLCSLV FGIPVMGLMI YMLIPSHEPQ
SSVLDHNVIP GLSILNLIFF ILCTFVQFLG GWYFYVQAYK SLRHGMANMD VLIVLATSIA
YVYSLVILVV AVAEKAERSP VTFFDTPPML FVFIALGRWL EHVVKSKTSE ALARLMSLQA
TEATVVTLGE DNVIIREEQV PMELVQRGDI IKVVPGGKFP VDGKVLEGNT MADESLITGE
AMPVTKKPGS MVIAGSMNAH GSVLITATHV GNDTTLAQIV KLVEEAQMSK APIQQLADRF
SGYFVPFIII ISTVTLVVWI VIGFIDFGVV QKYFPAPSKG ISQAEVVLRF AFQTSITVLC
IACPCSLGLA TPTAVMVGTG VAAQNGILIK GGKPLEMAHK IKTVMFDKTG TITHGVPKVS
RVLLLVDLAT LPLRKVLAVV GTAEASSEHP LGVAVTRYCK EELGTETLGC CMDFQAVPGC
GISCKVSSVE SILAQGERLQ GPPTAHQNRV GSEPSETDAA TQTFSVLIGN REWMRRNGLT
VTSDVRDAMT DHETKGQTAI LVAIDGVLCG MIAVADSVKQ EAALAVHTLK SMGVDVVLIT
GDNRKTARAI ATQVGINKVF AEVLPSHKVA KVQELQNQGK RVAMVGDGVN DSPALAQADV
GIAIGTGTDV AIEAADVVLI RNDLLDVVAS IHLSRRTVWR IRLNLVLALI YNLIGIPVAA
GVFIPIGVVL QPWMGSAAMA ASSVSVVLSS LQLKCYRKPD LARYEAQAHG HMKPLSASQV
SVRVGMDDRR RDSPRASAWD QVSYVSQVSL SPLKSDKLSR HSGAADDRGD KWSLLLNDRD
EEQGI


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