ATP7B Membrane Protein Introduction

Introduction of ATP7B

ATP7B gene (mapped to chromosome 13q14.3) encodes the protein Copper-transporting ATPase 2, also known as Human epididymis-specific protein 6 (HE6) or G-protein coupled receptor 64 (GPR64), which is a member of the family of P-type cation transport ATPase. Widely expressed in liver, brain, and kidney, ATP7B shows 62% amino acid homology to the Menkes disease gene. ATP7B is predicted to possess several membrane-spanning domains, an ATPase consensus sequence, a hinge domain, a phosphorylation site, and at least 2 putative copper-binding sites by sequence analysis.

Basic Information of ATP7B
Protein Name Copper-transporting ATPase 2
Gene Name ATP7B
Aliases Copper pump 2, Wilson disease-associated protein
Organism Homo sapiens (Human)
UniProt ID P35670
Transmembrane Times 8
Length (aa) 1465

Function of ATP7B Membrane Protein

P-type cation transport ATPase family is a large group of evolutionarily related lipid and ion pumps. As a member of P-type cation transport ATPase family, ATP7B functions as a monomer, having the ability of ATP binding and copper-transporting. ATP7B is an orphan receptor, with no endogenous ligand been found. It is characterized by a long N-terminus, which may be highly glycosylated. Studies have shown that the long N-terminus is cleaved at the GPS domain to allow for trafficking to the plasma membrane. It is documented that ATP7B is transported along liver cell microtubules in a copper-dependent manner via interaction with the p62 dynactin subunit. Alternative splicing of transcripts of ATP7B variants, encoding distinct isoforms with different cellular localizations, have been found. Single-nucleotide polymorphism in ATP7B gene can lead to Wilson disease (WD).

Schematic representation of ATP7B structure in the cell membrane. Fig.1 Schematic representation of ATP7B structure in the cell membrane.

Application of ATP7B Membrane Protein in Literature

  1. Gomes A and Dedoussis G.V. Geographic distribution of ATP7B mutations in Wilson disease. Ann Hum Biol. 2016, 43(1): 1-8. PubMed ID: 26207595

    This article reviews lots of ATP7B mutations from different populations, which may be of great value for the development of time-saving methods and accelerating the process of genetic analysis of Wilson Disease.

  2. Huster D., et al. Structural and metabolic changes in Atp7b-/- mouse liver and potential for new interventions in Wilson's disease. Ann N Y Acad Sci. 2014, 1315: 37-44. PubMed ID: 24697742

    This article finds that there are many structural and metabolic changes in Atp7b-/- mouse liver, which may contribute to the development of specific therapies to ameliorate Wilson Disease progression.

  3. Patil M., et al. A review and current perspective on Wilson disease. J Clin Exp Hepatol. 2013, 3(4): 321-36. PubMed ID: 25755520

    This article provides a summary of different aspects of Wilson disease, including geographical differences in clinical management and the limitations of currently available tests, which may give us a deeper understanding of Wilson disease.

  4. Bingham M.J., et al. Physiologic function of the Wilson disease gene product, ATP7B. Am J Clin Nutr. 1998, 67(5 Suppl): 982S-987S. PubMed ID: 9587140

    This article presents evidence suggesting that ATP7B is located intracellularly in the liver, and may also on the canalicular membrane, which makes significant advances in the understanding of copper metabolism in the liver, contributing to the basic knowledge development of ATP7B physiologic function.

  5. Li Y.Q., et al. Copper efflux transporters ATP7A and ATP7B: Novel biomarkers for platinum drug resistance and targets for therapy. IUBMB Life. 2018, 70(3): 183-191. PubMed ID: 29394468

    This article provides novel strategies for overcoming this resistance since the possible mechanisms of platinum drug resistance regulated by ATP7A/7B have been found, which gives a further understanding of the roles of ATP7A and ATP7B in platinum drug resistance.

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