Protein: ATP7A_MOUSE
Sequence: MEPSVDANSITITVEGMTCISCVRTIEQQIGKVNGVHHIKVSLEEKSATIIYDPKLQTPKTLQEAIDDMGFDALLHNANPLPVLTNTVFLTVTAPLTLPWDHIQSTLLKTKGVTGVKISPQQRSAVVTIIPSVVSASQIVELVPDLSLDMGTQEKKSGACEEHSTPQAGEVMLKMKVEGMTCHSCTSTIEGKVGKLQGVQRIKVSLDNQEATIVFQPHLITAEEIKKQIEAVGFPAFIKKQPKYLKLGAIDVERLKNTPVKSSEGSQQKSPSYPSDSTTMFTIEGMHCKSCVSNIESALSTLQYVSSIVVSLENRSAIVKYNASLVTPEMLRKAIEAISPGQYRVSIASEVESTASSPSSSSLQKMPLNIVSQPLTQEAVININGMTCNSCVQSIEGVISKKPGVKSIHVSLANSTGTIEFDPLLTSPETLREAIEDMGFDAALPDMKEPLVVIAQPSLETPLLPSSNELENVMTSVQNKCYIQVSGMTCASCVANIERNLRREEGIYSVLVALMAGKAEVRYNPAVIQPRVIAEFIRELGFGAMVMENAGEGNGILELVVRGMTCASCVHKIESTLTKHKGIFYCSVALATNKAHIKYDPEIIGPRDIIHTIGSLGFEASLVKKDRSANHLDHKREIKQWRGSFLVSLFFCIPVMGLMVYMMVMDHHLATLHHNQNMSNEEMINMHSAMFLERQILPGLSIMNLLSLLLCLPVQFCGGWYFYIQAYKALKHKTANMDVLIVLATTIAFAYSLVILLVAMFERAKVNPITFFDTPPMLFVFIALGRWLEHIAKGKTSEALAKLISLQATEATIVTLNSENLLLSEEQVDVELVQRGDIIKVVPGGKFPVDGRVIEGHSMVDESLITGEAMPVAKKPGSTVIAGSINQNGSLLIRATHVGADTTLSQIVKLVEEAQTSKAPIQQFADKLSGYFVPFIVLVSIVTLLVWIIIGFQNFEIVETYFPGYNRSISRTETIIRFAFQASITVLCIACPCSLGLATPTAVMVGTGVGAQNGILIKGGEPLEMAHKVKVVVFDKTGTITHGTPVVNQVKVLVESNKISRNKILAIVGTAESNSEHPLGAAVTKYCKKELDTETLGTCTDFQVVPGCGISCKVTNIEGLLHKSNLKIEENNIKNASLVQIDAINEQSSTSSSMIIDAHLSNAVNTQQYKVLIGNREWMIRNGLVISNDVDESMIEHERRGRTAVLVTIDDELCGLIAIADTVKPEAELAVHILKSMGLEVVLMTGDNSKTARSIASQVGITKVFAEVLPSHKVAKVKQLQEEGKRVAMVGDGINDSPALAMANVGIAIGTGTDVAIEAADVVLIRNDLLDVVASIDLSRKTVKRIRINFVFALIYNLVGIPIAAGVFLPIGLVLQPWMGSAAMAASSVSVVLSSLFLKLYRKPTYDNYELHPRSHTGQRSPSEISVHVGIDDTSRNSPRLGLLDRIVNYSRASINSLLSDKRSLNSVVTSEPDKHSLLVGDFREDDDTTL
What is the function of this protein?
ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:25639447, PubMed:27337370, PubMed:18650808).  Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side.  The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (By similarity).  Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:27337370, PubMed:18650808, PubMed:16371425, PubMed:12488345).  Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (By similarity).  May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (PubMed:25639447, PubMed:15634787, PubMed:16371425, PubMed:12488345).  In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (PubMed:18650808).
What are the official names of this protein?
Copper-transporting ATPase 1, Copper pump 1, Menkes disease-associated protein homolog.
What is the protein family that this protein belongs to?
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.
What are the subcellular locations of this protein?
Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Melanosome membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Cell projection, axon. Cell projection, dendrite. Postsynaptic density. Note=Cycles constitutively between the TGN and the plasma membrane. Predominantly found in the TGN and relocalized to the plasma membrane in response to elevated copper levels (PubMed:27337370). Targeting into melanosomes is regulated by BLOC-1 complex (PubMed:18650808). In response to glutamate translocates to neuron processes with a minor fraction at extrasynaptic sites (By similarity).