ATP synthase subunit beta, mitochondrial (ATP5B)
The protein contains 529 amino acids for an estimated molecular weight of 56560 Da.
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
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| Variant | Description |
|---|---|
| dbSNP:rs1042001 | |
| empty |
Biological Process
Angiogenesis
ATP biosynthetic process
ATP hydrolysis coupled proton transport
Cellular metabolic process
Cellular response to interleukin-7
Cristae formation
Generation of precursor metabolites and energy
Lipid metabolic process
Mitochondrial ATP synthesis coupled proton transport
Mitochondrion organization
Negative regulation of cell adhesion involved in substrate-bound cell migration
Organelle organization
Osteoblast differentiation
Positive regulation of blood vessel endothelial cell migration
Proton transmembrane transport
Proton transport
Regulation of intracellular pH
Respiratory electron transport chain
Small molecule metabolic process
Cellular Component
Cell surface
Extracellular exosome
Extracellular matrix
Membrane
Mitochondrial matrix
Mitochondrial membrane
Mitochondrial nucleoid
Mitochondrial proton-transporting ATP synthase complex
Mitochondrial proton-transporting ATP synthase, catalytic core
Mitochondrion
Myelin sheath
Nucleus
Obsolete cell
Plasma membrane
Proton-transporting ATP synthase complex
Proton-transporting ATP synthase complex, catalytic core F(1)
The reference OMIM entry for this protein is 102910
Atp synthase, h+ transporting, mitochondrial f1 complex, beta subunit; atp5b
Mitochondrial atp synthase, beta subunit; atpmb
Atpsb
DESCRIPTION
Mitochondrial ATP synthase catalyzes ATP formation, using the energy of proton flux through the inner membrane during oxidative phosphorylation. Two subunits of the enzyme are encoded by mitochondrial genes and the others by nuclear genes. The beta subunit of mitochondrial ATP synthase is encoded by a nuclear gene (summary by Ohta et al., 1988).CLONING
Ohta et al. (1988) cloned a cDNA of the human beta subunit of ATP synthase. Neckelmann et al. (1989, 1989) sequenced the human ATP synthase beta-subunit gene and demonstrated that it is preferentially expressed in heart and skeletal muscle. The gene encodes a leader peptide of 49 amino acids and a mature protein of 480 amino acids.GENE STRUCTURE
Ohta et al. (1988) determined that the ATP5B gene contains 10 exons, with the first exon corresponding to the noncoding region and most of the presequence that targets this protein to the mitochondria.MAPPING
Kudoh et al. (1989) assigned the ATPMB locus to the p13-qter region of human chromosome 12 by analysis of human-mouse somatic cell hybrid DNA and by use of flow-sorted chromosomes. They assigned 2 related sequences, ATPMBL1 and ATPMBL2, to chromosome 2 and 17, respectively.GENE FUNCTION
Martinez et al. (2003) identified ATP5B as a high affinity HDL receptor for apolipoprotein A1 (107680). They used a variety of experimental approaches to confirm this ectopic localization of components of the ATP synthase complex and the presence of ATP hydrolase activity at the hepatocyte cell surface. Receptor stimulation by apoA-I triggers the endocytosis of holo-HDL particles (protein plus lipid) by a mechanism that depends strictly on the generation of ADP. Martinez et al. (2003) confirmed this effect on endocytosis in perfused rat liver ex vivo by using a specific inhibitor of ATP synthase. Thus, Martinez et al. (2003) concluded that membrane-bound ATP synthase has a previously unsuspected role in modulating the concentrations of extracellular ADP and is regulated by a principal plasma apolipoprotein.ANIMAL MODEL
Kim et al. (2012) found that the Gsto1a isoform of Drosophila Gsto1 (605482) modified Atp5b by glutathionylation and enhanced mitochondrial ATPase synthase assembly and activity. Parkin (PARK2; 602544) mutant flies showed reduced expression of both Gsto1 and Atp5b and reduced ATPase function compared with controls. Overexpression of Gsto1 enhanced mitochondrial ATPase function and partially reversed the phenotype of parkin mutant flies, including degeneration of dopaminergic neurons and muscle, cellular tubulin (see 602529) accumulation, and endoplasmic reticulum stress. Knockdown of Atp5b in flies via RNA interference induced some of the parkin mutant phenotype. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 102910 was added.