ANO7 Membrane Protein Introduction

Introduction of ANO7

ANO7 is encoded by the ANO7 gene. It is also known as TMEM16G and is a member of transmembrane protein 16 (TMEM16) family, which is responsible for a variety of physiological functions, such as ion transport, phospholipid scrambling and regulating other ion channels. The crystal structure of ANO7 has not been solved so far. The proposed structural model according to the amino acid sequence indicates that ANO7 possesses eight predicted transmembrane helices. Meanwhile, ANO7 is also known as Dresden-transmembrane protein of the prostate (D-TMPP).

Basic Information of ANO7
Protein Name	Anoctamin-7
Gene Name	ANO7
Aliases	Dresden transmembrane protein of the prostate, D-TMPP, IPCA-5, Prostate cancer-associated protein 5, Transmembrane protein 16G, TMEM16G
Organism	Homo sapiens (Human)
UniProt ID	Q6IWH7
Transmembrane Times	8
Length (aa)	933
Sequence	MRMAATAWAGLQGPPLPTLCPAVRTGLYCRDQAHAERWAMTSETSSGSHCARSRMLRRRAQEEDSTVLIDVSPPEAEKRGSYGSTAHASEPGGQQAAACRAGSPAKPRIADFVLVWEEDLKLDRQQDSAARDRTDMHRTWRETFLDNLRAAGLCVDQQDVQDGNTTVHYALLSASWAVLCYYAEDLRLKLPLQELPNQASNWSAGLLAWLGIPNVLLEVVPDVPPEYYSCRFRVNKLPRFLGSDNQDTFFTSTKRHQILFEILAKTPYGHEKKNLLGIHQLLAEGVLSAAFPLHDGPFKTPPEGPQAPRLNQRQVLFQHWARWGKWNKYQPLDHVRRYFGEKVALYFAWLGFYTGWLLPAAVVGTLVFLVGCFLVFSDIPTQELCGSKDSFEMCPLCLDCPFWLLSSACALAQAGRLFDHGGTVFFSLFMALWAVLLLEYWKRKSATLAYRWDCSDYEDTEERPRPQFAASAPMTAPNPITGEDEPYFPERSRARRMLAGSVVIVVMVAVVVMCLVSIILYRAIMAIVVSRSGNTLLAAWASRIASLTGSVVNLVFILILSKIYVSLAHVLTRWEMHRTQTKFEDAFTLKVFIFQFVNFYSSPVYIAFFKGRFVGYPGNYHTLFGVRNEECAAGGCLIELAQELLVIMVGKQVINNMQEVLIPKLKGWWQKFRLRSKKRKAGASAGASQGPWEDDYELVPCEGLFDEYLEMVLQFGFVTIFVAACPLAPLFALLNNWVEIRLDARKFVCEYRRPVAERAQDIGIWFHILAGLTHLAVISNAFLLAFSSDFLPRAYYRWTRAHDLRGFLNFTLARAPSSFAAAHNRTCRYRAFRDDDGHYSQTYWNLLAIRLAFVIVFEHVVFSVGRLLDLLVPDIPESVEIKVKREYYLAKQALAENEVLFGTNGTKDEQPEGSELSSHWTPFTVPKASQLQQ

Function of ANO7 Membrane Protein

ANO7 is expressed in many different cell types, including epithelia and neurons. ANO7 functions as ion channels like the majority of TMEM16 proteins. It is involved in epithelial Cl^- transport, smooth muscle contraction and neuronal signal processing. ANO7 is reported to conduct Cl^- influx or Cl^- efflux, and the balance is regulated by the dynamic system of intracellular chloride, which is decided by the various Cl^-/cation co-transporters and their regulatory proteins. Moreover, ANO7 can work as lipid scramblases and catalyze the diffusion of lipids between the two leaflets of a bilayer. Even though the activity of TMEM16 has been implemented in a number of diseases including hypertension, asthma, diarrhoea, cancer and more recently ischaemia-induced arrhythmia, there is no non-selective nature of the pharmacology surrounding TMEM16 has impeded our knowledge of these proteins.

Fig.1 Proposed structure of ANO7 membrane protein (Brunner, 2014).

Application of ANO7 Membrane Protein in Literature

Brunner J.D., et al. X-ray structure of a calcium-activated TMEM16 lipid scramblase. Nature. 2014, 516:207. PubMed ID: 25383531

This article reveals the general architecture of the TMEM16 family and its mode of Ca²⁺ activation. It serves as a framework to unravel the conduction of ions in certain TMEM16 proteins.
Pedemonte N., et al. Structure and Function of TMEM16 Proteins (Anoctamins). Physiol. Rev. 2014, 94(2):419-459. PubMed ID: 24692353

The article reports that some mutations in anoctamin genes (ANO3, ANO5, ANO6, ANO7 and ANO10) result in various genetic diseases and suggests the involvement of anoctamins in a variety of cell functions whose link with ion transport and/or lipid scrambling.
Katoh, M., et al. Characterization of human TMEM16G gene in silico. International Journal of Molecular Medicine. 2004, 759-823. PubMed ID: 15375614

The authors in this article apply the bioinformatic method to characterize the human ANO7 gene, which is consisted of 25 exons and located at human chromosome 2q37.3.
Kiessling A., et al. D-TMPP: A novel androgen-regulated gene preferentially expressed in prostate and prostate cancer that is the first characterized member of an eukaryotic gene family. The Prostate. 2005, 64(4):387-400. PubMed ID: 15761874

This article reveals that the mRNA of ANO7 encodes a putative multiple transmembrane protein of 883 amino acids and is selectively overexpressed in prostate tissue.
Picollo A., et al. TMEM16 proteins: unknown structure and confusing functions. J. Mol. Biol. 2015, 427(1):94-105. PubMed ID: 25451786

This article reviews the unknown structure and confusing functions of the TMEM16 family of membrane proteins and the links between TMEM16 functions and human physiology and pathologies need to be investigated.

ANO7 Preparation Options

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Reference

Brunner JD., et al. (2014) X-ray structure of a calcium-activated TMEM16 lipid scramblase. Nature 516:207.

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