Literature summary for 7.2.2.9 extracted from

LeShane, E.S.; Shinde, U.; Walker, J.M.; Barry, A.N.; Blackburn, N.J.; Ralle, M.; Lutsenko, S.
Interactions between copper-binding sites determine the redox status and conformation of the regulatory N-terminal domain of ATP7B (2010), J. Biol. Chem., 285, 6327-6336.

Search for more literature for 7.2.2.9

Protein Variants

Protein Variants	Comment	Organism
additional information	mutations of copper-coordinating Cys to Ala in any metal-binding domains 2, 3, 4, or 6 change the N-ATP7B conformation and have distinct functional consequences, overview. The Cys-to-Ser mutation in MBD2 preserves the conformation and reduced state of N-ATP7B	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	ATP7B is a 165-kDa protein with eight transmembrane segments and most of the soluble parts exposed to the cytosol	Homo sapiens	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
165000	-	-	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + Cu2+/in	Homo sapiens	ATP7B has six N-terminal metal-binding domains, MBDs, that sense cytosolic copper levels and regulate ATP7B, mechanism, overview. Mutating MBD2 or MBD3 causes Cys oxidation in other MBDs and loss of copper binding. In contrast, mutation of MBD4 and MBD6 does not alter the redox status and function of other sites. MBD2 and MBD3 work together to regulate access to other metal-binding sites, whereas MBD4 and MBD6 receive copper independently, downstream of MBD2 and MBD3. Structure modeling and molecular dynamics simulations, overview, hydrogen bonding may play a role in the N-ATP7B folding and redox state, overview	ADP + phosphate + Cu2+/out	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P35670	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + Cu2+/in	-	Homo sapiens	ADP + phosphate + Cu2+/out	-	?
ATP + H2O + Cu2+/in	ATP7B has six N-terminal metal-binding domains, MBDs, that sense cytosolic copper levels and regulate ATP7B, mechanism, overview. Mutating MBD2 or MBD3 causes Cys oxidation in other MBDs and loss of copper binding. In contrast, mutation of MBD4 and MBD6 does not alter the redox status and function of other sites. MBD2 and MBD3 work together to regulate access to other metal-binding sites, whereas MBD4 and MBD6 receive copper independently, downstream of MBD2 and MBD3. Structure modeling and molecular dynamics simulations, overview, hydrogen bonding may play a role in the N-ATP7B folding and redox state, overview	Homo sapiens	ADP + phosphate + Cu2+/out	-	?

Subunits

Subunits	Comment	Organism
More	small changes in individual sites, induced by copper binding or mutation, result in stabilization of distinct conformations of the entire N-ATP7B and altered exposure of sites for interactions with regulatory proteins. Structure modeling and molecular dynamics simulations, hydrogen bonding may play a role in the N-ATP7B folding and redox state, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
ATP7B	-	Homo sapiens
copper-transporting ATPase	-	Homo sapiens
Cu-ATPase	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	ATP7B is essential for human copper homeostasis and normal liver function	Homo sapiens

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Release 2023.1 (January 2023)