ATP11A Membrane Protein Introduction

Introduction of ATP11A

ATP11A is encoded by ATP11A gene. It belongs to P4-ATPases family, which actively transport or flip phospholipids across cell membranes. It commonly exists in several tissues, such as liver, skeletal muscle, as well as ovary. Meanwhile, some studies conducted on ATP11B suggest that it is related to many diseases, like colorectal cancer and Leukemia. It has been regarded as a biomarker for prognosis of colorectal cancer.

Basic Information of ATP11A
Protein Name	Probable phospholipid-transporting ATPase IH
Gene Name	ATP11A
Aliases	ATPIH, ATPIS, KIAA1021
Organism	Homo sapiens (Human)
UniProt ID	P98196
Transmembrane Times	10
Length (aa)	1134
Sequence	MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHTVQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNRENHIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVERNAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEEQSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKLALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIVLLVTISLLPDVLKKVLCRQLWPTATERVQTKSQCLSVEQSTIFMLSQTSSSLSF

Function of ATP11A Membrane Protein

ATP11B, a member of P-type ATPases family, is phosphorylated in their intermediate state and drive uphill transport of ions across membranes. It plays a critical role in many cellular processes associated with the plasma membrane and intracellular membranes. ATP11A can also act as plasma membrane flippase. As with ATP11C, ATP8A2 and ATP11A localized to the plasma membrane in a CDC50A-dependent manner. Meanwhile, research during the past few decades suggest it is associated with various diseases, which provides possibilities for therapeutic applications.

Fig.1 Phylogenetic analysis and membrane topology of P4-ATPases. (Andersen, 2016)

Application of ATP11A Membrane Protein in Literature

Tsuchiya M., et al. Cell surface flip-flop of phosphatidylserine is critical for PIEZO1-mediated myotube formation. Nat Commun. 2018, 9(1): 2049. PubMed ID: 29799007

This article reports that the underlying mechanism and interaction among ATP11A, CDC50A, and PIEZO1. These results suggest that cell surface flip-flop of phosphatidylserine acts as a molecular switch for PIEZO1 activation that governs proper morphogenesis during myotube formation.
Li J., et al. Characterization of plasma proteins in children of different Mycobacterium tuberculosis infection status using label-free quantitative proteomics. Oncotarget. 2017, 8(61): 103290-103301. PubMed ID: 29262562

This article reveals that the expression level and difference of plasma proteins in ATB and latent TB infection children patients. The data show that 49 proteins are differentially expressed between LTBI and ATB.
Segawa K., et al. Human Type IV P-type ATPases That Work as Plasma Membrane Phospholipid Flippases and Their Regulation by Caspase and Calcium. J Biol Chem. 2016, 291(2): 762-72. PubMed ID: 26567335

Authors in this group analyze the expression levels of 12 human P4-ATPase, such as ATP8A2, ATP11A, and ATP11C, in an ATP11C-deficient cell line. The results indicate that the major flippases at the plasma membrane are ATP11A and ATP11C. ATP8A2 has a specific role in flipping phospholipids in the brain and testis.

ATP11A Preparation Options

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Reference

Andersen J P, et al. (2016). P4-ATPases as Phospholipid Flippases-Structure, Function, and Enigmas. Front Physiol. 7: 275.

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