ATP synthase subunit O, mitochondrial (ATP5O)
The protein contains 213 amino acids for an estimated molecular weight of 23277 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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. (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.
- 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:rs4842 |
Biological Process
ATP biosynthetic process
ATP synthesis coupled proton transport
Cellular metabolic process
Cristae formation
Mitochondrial ATP synthesis coupled proton transport
Proton transmembrane transport
Proton transport
Respiratory electron transport chain
Small molecule metabolic process
Cellular Component
Extracellular exosome
Extracellular matrix
Mitochondrial inner membrane
Mitochondrial proton-transporting ATP synthase complex
Mitochondrial proton-transporting ATP synthase, stator stalk
Mitochondrion
Nucleus
Plasma membrane
Proton-transporting ATP synthase complex, catalytic core F(1)
The reference OMIM entry for this protein is 600828
Atp synthase, h+ transporting, mitochondrial f1 complex, o subunit; atp5o
Mitochondrial atp synthase, o subunit
Oligomycin sensitivity-conferring protein; oscp
DESCRIPTION
ATP synthase (complex V of the mitochondrial respiratory chain) is a multimeric complex consisting of at least 16 different polypeptides, 2 of which are mitochondrially encoded and the remainder produced by nuclear genes. One of these nuclear genes (ATP5O) encodes the oligomycin sensitivity-conferring protein (OSCP) of ATP synthase and has been described from yeast, cow, and mouse. OSCP is a component of the 'stalk' region connecting the F1 and Fo domains of the ATP synthase complex (summary by Chen et al., 1995).CLONING
Chen et al. (1995) cloned a cDNA corresponding to human ATP5O. The authors used exon trapping from pools of chromosome 21-specific cosmids to identify a portion of the gene, which was then used to screen a fetal brain cDNA library. The predicted polypeptide is 213 amino acids long with more than 80% identity to the bovine and mouse homologs. Northern blot analysis detected expression in all human tissues examined and at highest levels in muscle and heart.MAPPING
Chen et al. (1995) mapped the ATP5O gene to chromosome 21q22.1-q22.2 by fluorescence in situ hybridization and by hybridization to somatic cell hybrid DNAs containing defined portions of chromosome 21. ... 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600828 was added.