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ATP6V0A2 Membrane Protein Introduction

Introduction of ATP6V0A2

V-type proton ATPase 116 kDa subunit a isoform 2 (ATP6V0A2), encoded by the ATP6V0A2 gene (mapped to chromosome 12q24), is a component of the vacuolar ATPase (V-ATPase). The multisubunit V-ATPase is comprised of a peripheral V1 domain and an integral membrane V0 domain, while ATP6V0A2 is a component of the V0 domain. It was reported that ATP6V0A2 has a hydrophobic N terminus and 3 potential N-glycosylation sites and it is expressed at the cell membrane and intracellularly in the JEG-3 human choriocarcinoma cell line. In mice, abundant expression of ATP6V0A2 in the T cell hybridoma cells and in thymus have been detected.

Basic Information of ATP6V0A2
Protein Name V-type proton ATPase 116 kDa subunit a isoform 2
Gene Name ATP6V0A2
Aliases Lysosomal H(+)-transporting ATPase V0 subunit a2, Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2, TJ6
Organism Homo sapiens (Human)
UniProt ID Q9Y487
Transmembrane Times 8
Length (aa) 856
Sequence MGSLFRSETMCLAQLFLQSGTAYECLSALGEKGLVQFRDLNQNVSSFQRKFVGEVKRCEELERILVYLVQEINRADIPLPEGEASPPAPPLKQVLEMQEQLQKLEVELREVTKNKEKLRKNLLELIEYTHMLRVTKTFVKRNVEFEPTYEEFPSLESDSLLDYSCMQRLGAKLGFVSGLINQGKVEAFEKMLWRVCKGYTIVSYAELDESLEDPETGEVIKWYVFLISFWGEQIGHKVKKICDCYHCHVYPYPNTAEERREIQEGLNTRIQDLYTVLHKTEDYLRQVLCKAAESVYSRVIQVKKMKAIYHMLNMCSFDVTNKCLIAEVWCPEADLQDLRRALEEGSRESGATIPSFMNIIPTKETPPTRIRTNKFTEGFQNIVDAYGVGSYREVNPALFTIITFPFLFAVMFGDFGHGFVMFLFALLLVLNENHPRLNQSQEIMRMFFNGRYILLLMGLFSVYTGLIYNDCFSKSVNLFGSGWNVSAMYSSSHPPAEHKKMVLWNDSVVRHNSILQLDPSIPGVFRGPYPLGIDPIWNLATNRLTFLNSFKMKMSVILGIIHMTFGVILGIFNHLHFRKKFNIYLVSIPELLFMLCIFGYLIFMIFYKWLVFSAETSRVAPSILIEFINMFLFPASKTSGLYTGQEYVQRVLLVVTALSVPVLFLGKPLFLLWLHNGRSCFGVNRSGYTLIRKDSEEEVSLLGSQDIEEGNHQVEDGCREMACEEFNFGEILMTQVIHSIEYCLGCISNTASYLRLWALSLAHAQLSDVLWAMLMRVGLRVDTTYGVLLLLPVIALFAVLTIFILLIMEGLSAFLHAIRLHWVEFQNKFYVGAGTKFVPFSFSLLSSKFNNDDSVA

Function of ATP6V0A2 Membrane Protein

V-ATPase is essential for acidification of diverse cellular components, including endosomes, lysosomes, clathrin-coated vesicles, secretory vesicles, and chromaffin granules. As a key component of the V0 domain, ATP6V0A2 acts as a part of the proton channel of V-ATPases and it is indispensable for the entire vacuolar ATPase to act normally. Researches have shown that upon cell stimulation, ATP6V0A2 migrates to the cell membrane, and the remaining 20-kD N-terminal domain is secreted into the extracellular environment, which may increase the secretion of IL1B, and decrease the expression of type I and II interleukin receptors IL1R1 and IL1R2 in human peripheral blood mononuclear cells cocultured with JEG-3 cells. In addition, ATP6V0A2 may have an influence in keeping the Golgi good functions, such as glycosylation maturation, by mediating the Golgi pH. It is documented that ATP6V0A2 is involved in intracellular iron homeostasis in aerobic conditions, and has the ability to trigger the activity of Fe2+ prolyl hydroxylase (PHD) enzymes and lead to hydroxylation of HIFI1A and subsequent degradation of proteasome. ATP6V0A2 single-nucleotide polymorphisms (SNPs) can lead to both wrinkly skin syndrome and cutis laxa type II.

V-type proton ATPase subunit composition and structure. Fig.1 V-type proton ATPase subunit composition and structure. (Tresguerres, 2016)

Application of ATP6V0A2 Membrane Protein in Literature

  1. Udono M., et al. Impaired ATP6V0A2 expression contributes to Golgi dispersion and glycosylation changes in senescent cells. Sci Rep. 2015, 5: 17342. PubMed ID: 26611489

    This article suggests that senescence-associated blocked expression of ATP6V0A2 leads to changes in Golgi structure and glycosylation in old TIG-1 cells, which demonstrates the regulation of ATP6V0A2 in cellular senescence program.

  2. Bahena-Bahena D., et al. ATP6V0A2 mutations present in two Mexican Mestizo children with an autosomal recessive cutis laxa syndrome type IIA. Mol Genet Metab Rep. 2014, 1: 203-212. PubMed ID: 27896089

    This report firstly describes Mestizo patients with molecular diagnosis of ARCL-IIA/ATP6V0A2-CDG. And then further confirms that their variants are detected in patients from all over the world and with various genetic backgrounds for the first time.

  3. Hucthagowder V., et al. Loss-of-function mutations in ATP6V0A2 impair vesicular trafficking, tropoelastin secretion, and cell survival. Hum Mol Genet. 2009, 18(12): 2149-65. PubMed ID: 19321599

    This article confirms that loss-of-function variations of ATP6V0A2 contribute to the aggregation of tropoelastin in the Golgi, blocked clearance of tropoelastin aggregates and increased apoptosis of elastogenic cells. The loss of ATP6V0A2 either in ARCL2 cells or by siRNA knockdown can lead to distended Golgi cisternae, multivesicular bodies, and accumulation of abnormal lysosomes.

  4. Kornak U., et al. Impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2. Nat Genet. 2008; 40(1): 32-4. PubMed ID: 18157129

    This report suggests that loss-of-function mutations in ATP6V0A2 can lead to an impairment of Golgi trafficking in fibroblasts from affected individuals and result in anomalous glycosylation of serum proteins (CDG-II), indicating that ATP6V0A2 has a significant role in Golgi function.

  5. Jaiswal M.K., et al. Male fertility and apoptosis in normal spermatogenesis are regulated by vacuolar-ATPase isoform a2. J Reprod Immunol. 2015, 112: 38-45. PubMed ID: 26226211

    This article reveals that ATP6V0A2 can mediate the apoptotic pathways essential feature for testicular, and is necessary for sufficient spermatogenesis.

ATP6V0A2 Preparation Options

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Reference

  1. Tresguerres M. (2016). Novel and potential physiological roles of vacuolar-type H+-ATPase in marine organisms. J Exp Biol. 219(Pt 14): 2088-97.

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