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Literature summary for 7.6.2.1 extracted from

  • Lopez-Marques, R.L.; Poulsen, L.R.; Palmgren, M.G.
    A putative plant aminophospholipid flippase, the Arabidopsis P4 ATPase ALA1, localizes to the plasma membrane following association with a beta-subunit (2012), PLoS ONE, 7, e33042.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Saccharomyces cerevisiae strain w303-1a Arabidopsis thaliana
heterologous expression of ALA1 in a enzyme-deficient Ddrs2Ddnf1Ddnf2 Saccharomyces cerevisiae mutant strain. Transient expression of N-terminally GFP-tagged ALA1 in tobacco leaves in the presence of untagged versions of three different ALIS proteins ALIS1, ALIS3, ALIS5, co-expression with any ALIS protein results in localization of GFP-ALA1 in membranes resembling either the plasma membrane or the tonoplast. Expression of GFP­-tagged ALA1 lacking its beta-subunit localizes to the endoplasmic reticulum in tobacco epidermal cells Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane ALA1 is targeted to the plasma membrane and following association in the endoplasmic reticulum with an ALIS protein beta-subunit Arabidopsis thaliana 5886
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plasma membrane the enzyme localizes to the plant plasma membrane and has a strict requirement for an ALIS protein beta-subunit to exit the endoplasmic reticulum Arabidopsis thaliana 5886
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Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
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Arabidopsis thaliana P98204
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Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
ALA1
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Arabidopsis thaliana
aminophospholipid flippase
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Arabidopsis thaliana
P4 ATPase ALA1
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Arabidopsis thaliana

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Arabidopsis thaliana

General Information

General Information Comment Organism
evolution ATP-dependent aminophospholipid translocases constitute a subfamily, P4 ATPases, in the superfamily of P-type ATPase pumps Arabidopsis thaliana
physiological function P4 ATPases are involved in establishing lipid asymmetry across plasma membranes. Asymmetric lipid distributions with aminophospholipids concentrated in the inner leaflet and sphingolipids in the outer leaflet, amongst several proposed functions, might be a prerequisite for endocytosis Arabidopsis thaliana