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TMEM30A Membrane Protein Introduction

Introduction of TMEM30A

Transmembrane Protein 30A (TMEM30A) is also known as CDC50A or C6orf67, which is encoded by TMEM30A gene. In silico expression analysis revealed that TMEM30A has a ubiquitous expression in brain, lung, adrenal, appendix, colon, thyroid, urinary bladder, and 19 other tissues. TMEM30A mutations are associated with Intrahepatic Cholestasis. An important paralog of TMEM30A gene is TMEM30B. There are three isoforms produced by alternative splicing: isoform 1, isoform 2, isoform 3, among which isoform 1 is chosen as the canonical sequence. It has documented that TMEM30A has 2 transmembrane domains and an extracellular loop with 3 cysteines and an N-glycosylation site.

Basic Information of TMEM30A
Protein Name Cell cycle control protein 50A
Gene Name TMEM30A
Aliases P4-ATPase Flippase Complex Beta Subunit TMEM30A, C6orf67, CDC50A
Organism Homo sapiens (Human)
UniProt ID Q9NV96
Transmembrane Times 2
Length (aa) 361
Sequence MAMNYNAKDEVDGGPPCAPGGTAKTRRPDNTAFKQQRLPAWQPILTAGTVLPIFFIIGLIFIPIGIGIFVTSNNIREIEIDYTGTEPSSPCNKCLSPDVTPCFCTINFTLEKSFEGNVFMYYGLSNFYQNHRRYVKSRDDSQLNGDSSALLNPSKECEPYRRNEDKPIAPCGAIANSMFNDTLELFLIGNDSYPIPIALKKKGIAWWTDKNVKFRNPPGGDNLEERFKGTTKPVNWLKPVYMLDSDPDNNGFINEDFIVWMRTAALPTFRKLYRLIERKSDLHPTLPAGRYSLNVTYNYPVHYFDGRKRMILSTISWMGGKNPFLGIAYIAVGSISFLLGVVLLVINHKYRNSSNTADITI

Function of TMEM30A Membrane Protein

TMEM30A is an accessory component of a P4-ATPase flippase complex, which controls the transport of aminophospholipids from the outer to the inner leaflet of various membranes coupled to the hydrolysis of ATP to maintain the asymmetric distribution of phospholipids. ATP8A2-TMEM30A complex may play a role in the regulation of neurite outgrowth. Whereas ATP8A1-TMEM30A flippase complex seems to be involved in the mediation of cell migration. TMEM30A is indispensable for the formation of ATP8B1, ATP8B2, and ATP8A2 P-type ATPase intermediate phosphoenzyme. Additionally, it is reported that TMEM30A is involved in the uptake of synthetic drug alkylphospholipid edelfosine and platelet-activating factor (PAF). TMEM30A also regulates the export of α subunits ATP8A1, ATP10A, ATP11A, ATP8B1, ATP8B2, ATP8B4, ATP10B, ATP10D, ATP11B and ATP11C from the endoplasmic reticulum to other membrane localizations.

Schematic representation of TMEM30A structure in the membrane. Fig.1 Schematic representation of TMEM30A structure in the membrane.

Application of TMEM30A Membrane Protein in Literature

  1. Li N., et al. Tmem30a Plays Critical Roles in Ensuring the Survival of Hematopoietic Cells and Leukemia Cells in Mice. Am J Pathol. 2018, 188(6):1457-1468. PubMed ID: 29574182

    This article reveals that Tmem30a is a potential therapeutic target for BCR/ABL1-induced chronic myeloid leukemia.

  2. Liu L., et al. Hepatic Tmem30a Deficiency Causes Intrahepatic Cholestasis by Impairing Expression and Localization of Bile Salt Transporters. Am J Pathol. 2017, 187(12):2775-2787. PubMed ID: 28919113

    This article demonstrates that TMEM30A deficiency will lead to intrahepatic cholestasis in mice by repressing the expression of BS transporters and related nuclear receptors, and blocking the localization of BS transporters, suggesting that TMEM30A may be a novel therapeutic target for intrahepatic cholestasis.

  3. Wang J., et al. A biosystems approach to identify the molecular signaling mechanisms of TMEM30A during tumor migration. PLoS One. 2017, 12(6):e0179900. PubMed ID: 28640862

    This article finds the genes, identified by computational biology methods, are indeed regulated by TMEM30A during cell migration, which gives a new understanding of the tumor invasion molecular basis.

  4. Chen R., et al. Human TMEM30a promotes uptake of antitumor and bioactive choline phospholipids into mammalian cells. J Immunol. 2011, 186(5):3215-25. PubMed ID: 21289302

    This article suggests that extracellular choline phospholipids with short sn-2 residues can have sites of metabolism and intracellular roles because they are transport substrates for a TMEM30A phospholipid import system.

  5. van der Velden L.M., et al. Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases. J Biol Chem. 2010, 285(51):40088-96. PubMed ID: 20947505

    This article reveals that interactions between class 1 P(4)-ATPases and CDC50 proteins are required for ER exit and stability of both subunits.

TMEM30A Preparation Options

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