Phospholipid-transporting ATPase IH (ATP11A)
The protein contains 1134 amino acids for an estimated molecular weight of 129756 Da.
Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane (PubMed:25315773, PubMed:25947375, PubMed:26567335, PubMed:29799007, PubMed:30018401). Contributes to the maintenance of membrane lipid asymmetry with a specific role in morphogenesis of muscle cells. In myoblasts, mediates PS enrichment at the inner leaflet of plasma membrane, triggering PIEZO1-dependent Ca2+ influx and Rho GTPases signal transduction, subsequently leading to the assembly of cortical actomyosin fibers and myotube formation (PubMed:29799007). May be involved in the uptake of farnesyltransferase inhibitor drugs, such as lonafarnib. (updated: April 7, 2021)
Protein identification was indicated in the following studies:
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, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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| Variant | Description |
|---|---|
| dbSNP:rs368865 | |
| dbSNP:rs11616795 |
No binding partner found
Biological Process
In utero embryonic development
Neutrophil degranulation
Phospholipid translocation
Positive regulation of myotube differentiation
Cellular Component
Early endosome
Endoplasmic reticulum
Endoplasmic reticulum membrane
Integral component of membrane
Integral component of plasma membrane
Intracellular membrane-bounded organelle
Lysosomal membrane
Membrane
Phospholipid-translocating ATPase complex
Plasma membrane
Recycling endosome
Specific granule membrane
Tertiary granule membrane
Trans-Golgi network
The reference OMIM entry for this protein is 605868
Atpase, class vi, type 11a; atp11a
Atpis
Atpih, mouse, homolog of; atpih
DESCRIPTION
P-type ATPases, such as ATP11A, are phosphorylated in their intermediate state and drive uphill transport of ions across membranes. Several subfamilies of P-type ATPases have been identified. One subfamily transports heavy metal ions, such as Cu(2+) or Cd(2+). Another subfamily transports non-heavy metal ions, such as H(+), Na(+), K(+), or Ca(+). A third subfamily transports amphipaths, such as phosphatidylserine.CLONING
Kikuno et al. (1999) isolated a partial cDNA encoding ATP11A, which they called KIAA1021, from a brain cDNA library. Based on homology analysis, they predicted that the KIAA1021 protein is a probable calcium-transporting ATPase. RT-PCR analysis detected wide but moderate expression, with lowest levels in spleen, pancreas, testis, and most brain regions. Halleck et al. (1999) stated that the human ATP11A protein, which they called ATPIS, shares 91% amino acid identity with the mouse Atpih protein. By in situ hybridization analysis, they detected expression of Atpih in tissues from a number of organ systems in newborn and embryonic mice. Northern blot analysis revealed expression of an approximately 8-kb Atpih transcript that was strongest in mouse heart, followed by muscle, liver, and brain. Nesbit et al. (2004) reported that the ATP11A protein contains 10 transmembrane domains and the conserved DKTGTLT sequence found in P-type ATPases. By database analysis, they identified exon 29 splice variants that result in proteins with different C termini.GENE STRUCTURE
Nesbit et al. (2004) determined that the ATP9A gene contains at least 30 exons.MAPPING
Kikuno et al. (1999) stated that the ATP11A gene, or KIAA1021, maps to chromosome 13. By genomic sequence analysis, Halleck et al. (1999) confirmed that the ATP11A gene, or ATPIS, maps to chromosome 13. Nesbit et al. (2004) stated that the ATP11A gene maps to chromosome 13q34. ... More on the omim web site
April 10, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 605868 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).