V-type proton ATPase 16 kDa proteolipid subunit (ATP6V0C)

The protein contains 155 amino acids for an estimated molecular weight of 15736 Da.

 

Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. (updated: Feb. 4, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  4. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is annotated as membranous in Gene Ontology, is predicted to be membranous by TOPCONS.

Topcons

Interpro domains
Total structural coverage: 0%
Model score: 0
MODL_ROSETTA-3.4

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The reference OMIM entry for this protein is 108745

Atpase, h+ transporting, lysosomal, 16-kd, v0 subunit c; atp6v0c
Atpase, h+ transporting, lysosomal; atp6l
Vacuolar proton pump, subunit c; vppc

CLONING

In an attempt to isolate candidate genes for autosomal dominant polycystic kidney disease (PKD1; 173900), Gillespie et al. (1991) identified a number of CpG-rich islands from the PKD1 critical region on 16p13.3. Genomic fragments adjacent to 1 of these islands were used to isolate cDNAs from both HeLa cells and cultured cystic epithelium that encode a 155-amino acid peptide having 4 putative transmembrane domains. The corresponding transcript was found in all tissues tested but was most abundant in brain and kidney. The deduced amino acid sequence had 93% similarity to the 16-kD proteolipid component that is believed to be part of the proton channel of the vacuolar H(+)-ATPase. A mutated proton channel might be implicated in the pathogenesis of cystic disease. However, sequencing of cDNAs corresponding to both alleles of an affected person revealed no differences in the deduced amino acid sequence. Moreover, transcript size and abundance were not altered in cystic kidney.

GENE FUNCTION

Using a bacterial 2-hybrid assay, Sun et al. (2004) showed that the rat bile acid transporter Asbt (SLC10A2; 601295) interacted with mouse Vppc. The interaction was confirmed by in vitro pull-down assays and mammalian 2-hybrid analysis. Immunofluorescence confocal microscopy demonstrated that Asbt and Vppc colocalized in transfected COS-7 and MDCK canine kidney cells. Pharmacologic blockade of the vacuolar proton pump abrogated the apical localization of Asbt and colocalization of Asbt and Vppc, and it significantly decreased cellular uptake of the bile acid taurocholate. Sun et al. (2004) concluded that VPPC contributes to the apical membrane localization of ASBT.

MAPPING

By genomic sequence analysis, Gillespie et al. (1991) mapped the ATP6V0C gene to chromosome 16p13.3. Simckes et al. (2002) mapped the mouse Atp6v0c gene to chromosome 17, where it is closely linked to the TSC2 gene (191092). ... More on the omim web site

Subscribe to this protein entry history

May 13, 2019: Protein entry updated
Automatic update: model status changed

Nov. 17, 2018: Protein entry updated
Automatic update: model status changed

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Oct. 27, 2017: Protein entry updated
Automatic update: model status changed

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 108745 was added.

Feb. 25, 2016: Protein entry updated
Automatic update: model status changed

Feb. 24, 2016: Protein entry updated
Automatic update: model status changed

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed