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0ATP7B_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameATP7B
DescriptionCopper-transporting atpase 2 (ec 3.6.3.4) (copper pump 2) (wilson disease-associated protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0005770 late endosome (IDA)
0005524 ATP binding (IDA)
0005507 copper ion binding (IDA)
0004008 copper-exporting ATPase activity (TAS)
0006825 copper ion transport (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
P-type (or E1-E2-type) ATPases constitute a superfamily of cation transport enzymes.resent both in prokaryota and eukaryota.hose members mediate membrane flux of all common biologically relevant cations . The enzymes.hat form an aspartyl phosphate intermediate in the course of ATP hydrolysis.an be divided into 4 major groups : (1) Ca2+-transporting ATPases; (2) Na+/K+- and gastric H+/K+-transporting ATPases; (3) plasma membrane H+-transporting ATPases (proton pumps) of plants.ungi and lower eukaryotes; and (4) all bacterial P-type ATPases.xcept the Mg2+-ATPase of Salmonella typhimurium.hich is more similar to the eukaryotic sequences. However.reat variety of sequence analysis methods results in diversity of classification.
  IPR008250:E1-E2 ATPase-associated region
This group of hydrolase enzymes is structurally different from the alpha/beta hydrolase family (abhydrolase). This group includes L-2-haloacid dehalogenase.poxide hydrolases and phosphatases. The structure consists of two domains. One is an inserted four helix bundle.hich is the least well conserved region of the alignment.etween residues 16 and 96 of HAD1_PSESP. The rest of the fold is composed of the core alpha/beta domain.
  IPR005834:Haloacid dehalogenase-like hydrolase
Proteins that transport heavy metals in micro-organisms and mammals share similarities in their sequences and structures. These proteins provide an important focus for research.ome being involved in bacterial resistance to toxic metals.uch as lead and cadmium.hile others are involved in inherited human syndromes.uch as Wilsons and Menkes diseases . A conserved domain has been found in a number of these heavy metal transport or detoxification proteins . The domain.hich has been termed Heavy-Metal-Associated (HMA).ontains two conserved cysteines that are probably involved in metal binding. Structure solution of the fourth HMA domain of the Menkes copper transporting ATPase shows a well-defined structure comprising a four-stranded antiparallel beta-sheet and two alpha helices packed in an alpha-beta sandwich fold . This fold is common to other domains and is classified as "ferredoxin-like".
  IPR006121:Heavy metal transport/detoxification protein
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient.sing the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse.sing the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases.hich can differ in function (ATP synthesis and/or hydrolysis).tructure (F-.- and A-ATPases contain rotary motors) and in the type of ions they transport . F-ATPases (F1F0-ATPases) in mitochondria.hloroplasts and bacterial plasma membranes are the prime producers of ATP.sing the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases) are primarily found in eukaryotic vacuoles.atalysing ATP hydrolysis to transport solutes and lower pH in organelles.A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases.P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles.nd function to transport a variety of different ions across membranes.E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs.ncluding extracellular ATP.P-ATPases (sometime known as E1-E2 ATPases) () are found in bacteria and in a number of eukaryotic plasma membranes and organelles . P-ATPases function to transport a variety of different compounds.ncluding ions and phospholipids.cross a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases.ach of which transports a specific type of ion: H+.a+.+.g2+.a2+.g+ and Ag2+.n2+.o2+.b2+.i2+.d2+.u+ and Cu2+. P-ATPases can be composed of one or two polypeptides.nd can usually assume two main conformations called E1 and E2. This entry represents the several classes of P-type ATPases.ncluding those that transport K+ ().g2+ ().d2+ ().u 2+ ().n2+ ().a+ ().a2+ ().a+/K+ ().nd H+/K+ (). These P-ATPases are found in both prokaryotes and eukaryotes.More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR001757:ATPase, P-type, K/Mg/Cd/Cu/Zn/Na/Ca/Na/H-transporter
Proteins that transport heavy metals in micro-organisms and mammals share similarities in their sequences and structures. Some of these proteins are involved in bacterial resistance to toxic metals.uch as lead and cadmium.hile others are involved in inherited human syndromes.uch as Wilson and Menkes diseases .A conserved 30-residue domain has been found in a number of these heavy metal transport or detoxification proteins. The domain.hich has been termed Heavy-Metal-Associated (HMA).ontains two conserved cysteines that are probably involved in metal binding. The HMA domain has been identified in the N-terminal regions of a variety of cation-transporting ATPases (E1-E2 ATPases). The structure of the mercuric ion-binding protein MerP from Shigellaflexneri has been determined. The fold has been classed as a ferredoxin-likealpha-beta sandwich.aving a beta-alpha beta-beta alpha-beta architecture.ith the two alpha-helices overlaying a four-stranded anti-parallel beta-sheet . Structural differences between the reduced and mercury-bound forms of merP are localised to the metal-binding loop containing the consensus sequence GMTCXXC.he two cysteines of which are involved inbi-coordination of Hg(2+) .Copper-transporting ATPase 1 (ATP7A and ATP7B) is thought to function inthe export of copper.nd possibly other metals.rom the cytoplasm to anintracellular organelle. The protein functions as a monomer and is anintegral membrane protein.ith 8 predicted transmembrane (TM) domains.ossibly inserted into the membrane of a subcellular compartment. ATP7A isfound in most tissues.xcept liver. Defects in the protein.esulting indefective absorption and transport of copper.re associated with Menkessyndrome (also known as kinky hair disease).n X-linked recessive diseasecharacterised by progressive neurodegeneration and connective-tissuedisturbances.ocal cerebral and cerebellar degeneration.arly retardationin growth.eculiar hair.ipopigmentation.ascular complications and deathin early childhood.Defects in ATP7B are associated with Wilson disease.n autosomal recessivedisorder of copper metabolism in which copper cannot be incorporated intoceruloplasmin in liver.nd cannot be excreted from the liver into the bile.Copper thus accumulates in the liver.nd ultimately in the brain and kidney.eading to neurological manifestations and signs of cirrhosis.
  IPR001877:Copper-transporting ATPase 1
Proteins that transport heavy metals in micro-organisms and eukaryotes share similarities in their sequences and structures. These proteins provide an important focus for research.ome being involved in bacterial resistance to toxic metals.uch as lead and cadmium.hile others are involved in inherited human syndromes.uch as Wilsons and Menkes diseases . A conserved 30-residue domain has been found in a number of these heavy metal transport or detoxification proteins . The domain.hich has been termed Heavy-Metal-Associated (HMA).ontains two conserved cysteines that are probably involved in metal binding. This sub-domain is found in copper-binding proteins.
  IPR006122:Copper ion-binding
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient.sing the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse.sing the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases.hich can differ in function (ATP synthesis and/or hydrolysis).tructure (F-.- and A-ATPases contain rotary motors) and in the type of ions they transport . F-ATPases (F1F0-ATPases) in mitochondria.hloroplasts and bacterial plasma membranes are the prime producers of ATP.sing the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).V-ATPases (V1V0-ATPases) are primarily found in eukaryotic vacuoles.atalysing ATP hydrolysis to transport solutes and lower pH in organelles.A-ATPases (A1A0-ATPases) are found in Archaea and function like F-ATPases.P-ATPases (E1E2-ATPases) are found in bacteria and in eukaryotic plasma membranes and organelles.nd function to transport a variety of different ions across membranes.E-ATPases are cell-surface enzymes that hydrolyse a range of NTPs.ncluding extracellular ATP.P-ATPases (sometime known as E1-E2 ATPases) () are found in bacteria and in a number of eukaryotic plasma membranes and organelles . P-ATPases function to transport a variety of different compounds.ncluding ions and phospholipids.cross a membrane using ATP hydrolysis for energy. There are many different classes of P-ATPases.ach of which transports a specific type of ion: H+.a+.+.g2+.a2+.g+ and Ag2+.n2+.o2+.b2+.i2+.d2+.u+ and Cu2+. P-ATPases can be composed of one or two polypeptides.nd can usually assume two main conformations called E1 and E2.This entry represents P-type ATPases that specialize in cation and copper transport; those transporting copper () have been classified as belonging to the IB subfamily . These proteins are involved in a variety of processes in both prokaryotes and eukaryotes. Some of these P-ATPases import copper into cells.uch as in Arabidopsis sp..hich require copper to create functional hormone receptors for ethylene signalling. Other P-ATPases are involved in copper export out of cells.uch as occurs with the efflux of hepatic copper into the bile in eukaryotes. In bacteria.ome of these P-ATPases play a role in osmotic adaptation. Certain copper ATPases have been implicated in both Wilson and Menkes diseases .More information about this protein can be found at Protein of the Month: ATP Synthases .
  IPR006403:ATPase, P type cation/copper-transporter
This group encompasses the copper and cadmium-type heavy metal transporting P-type ATPases as well as those which cannot be assigned to one or other of the groups.
  IPR006416:Heavy metal translocating P-type ATPase
IPR008250:E1-E2_ATPase 
Evalue:-99.3098068237305 
Location:769-1017IPR005834:Hydrolase 
Evalue:-32.6777801513672 
Location:1021-1288IPR006121:HMA 
Evalue:-13.8538722991943 
Location:362-426IPR006121:HMA 
Evalue:-13.7695512771606 
Location:146-210IPR006121:HMA 
Evalue:-12.1249389648438 
Location:567-631IPR006121:HMA 
Evalue:-10.958607673645 
Location:260-324IPR006121:HMA 
Evalue:-10.8239088058472 
Location:61-125IPR006121:HMA 
Evalue:-10.6020603179932 
Location:491-555IPR001877:CUATPASEI 
Evalue:0 
Location:712-737IPR001877:CUATPASEI 
Evalue:0 
Location:654-675
SequencesProtein: ATP7B_HUMAN (1465 aa)
mRNA: NM_000053
Local Annotation
Synapse Ontology
endosome of the presynaptic compartment. A cellular structure that is involved in the transport of proteins in the neuron after the proteins are endocytosed from the outside to the inside of the cell.
sdb:0088 endosome  (Evidence:keywords)
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords)
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
endosomal intermediate functions as a sorting station before be redirected into the recycling vesicle population.
sdb:0150 endosomal intermediate  (Evidence:keywords)
KO assignmentK01533
  Level 3 annotation:
    Cu2+-exporting ATPase
  Level 2 annotation:
    ATPases
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 788 residues, 51404805-51407166Exon2: 36 residues, 51407729-51407832Exon3: 41 residues, 51409412-51409530Exon4: 70 residues, 51409612-51409816Exon5: 49 residues, 51411187-51411330Exon6: 50 residues, 51413217-51413361Exon7: 58 residues, 51414522-51414691Exon8: 63 residues, 51416245-51416428Exon9: 67 residues, 51418420-51418615Exon10: 47 residues, 51421798-51421933Exon11: 53 residues, 51422143-51422298Exon12: 44 residues, 51422408-51422536Exon13: 32 residues, 51429652-51429744Exon14: 80 residues, 51430447-51430681Exon15: 60 residues, 51432284-51432459Exon16: 27 residues, 51433973-51434050Exon17: 56 residues, 51437008-51437170Exon18: 56 residues, 51440580-51440744Exon19: 88 residues, 51442628-51442886Exon20: 413 residues, 51446071-51447305Exon21: 71 residues, 51483423-51483631Exon22: 2 residues, -Jump to ATP7B_HUMAN  
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