V-type proton ATPase subunit D (ATP6V1D)
The protein contains 247 amino acids for an estimated molecular weight of 28263 Da.
Subunit of the peripheral V1 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- 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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
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.
This protein is annotated as membranous in Gene Ontology.
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Biological Process
Biological process involved in interaction with host
Cellular iron ion homeostasis
Cellular response to amino acid starvation
Cilium assembly
Cilium assembly
Insulin receptor signaling pathway
Ion transmembrane transport
Neutrophil degranulation
Phagosome acidification
Phagosome maturation
Protein localization to cilium
Proton transport
Regulation of macroautophagy
Transferrin transport
Transmembrane transport
The reference OMIM entry for this protein is 609398
Atpase, h+ transporting, lysosomal, 34-kd, v1 subunit d; atp6v1d
Atp6m
DESCRIPTION
Vacuolar H(+)-ATPases (V-ATPases) acidify endosomes, lysosomes, Golgi, and secretory vesicles and transport protons across the plasma membrane into the extracellular space. The structure of the multiprotein V-ATPase complex comprises a globular head attached to the membrane by a stalk; subunit D proteins are contained in the stalk. ATP6V1D was originally named ATP6M but was renamed to conform to the revised nomenclature for mammalian vacuolar-type proton pump ATPases (Smith et al., 2003).CLONING
Using RT-PCR, Kennell et al. (2001) cloned murine Atp6v1d from spleen. Human and mouse ATP6V1D share 98% amino acid identity, with most of the variation occurring in the C terminus.GENE FUNCTION
Using phylogenetic and evolutionary analysis, Kennell et al. (2001) showed that the ATP6V1D gene has been under strong negative selection during evolution and is highly conserved among mammals, flies, worms, yeast, plants, and bacteria. Using a library of endoribonuclease-prepared short interfering RNAs (esiRNAs), Kittler et al. (2004) identified 37 genes required for cell division, one of which was ATP6V1D. These 37 genes included several splicing factors for which knockdown generates mitotic spindle defects. In addition, a putative nuclear-export terminator was found to speed up cell proliferation and mitotic progression after knockdown.GENE STRUCTURE
By sequence alignment, Kennell et al. (2001) showed that the ATP6V1D gene contains at least 9 exons.MAPPING
Kennell et al. (2001) mapped the human ATP6V1D gene by BLAST analysis to chromosome 14q24, in a region that exhibits conserved synteny with mouse chromosome 12. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 609398 was added.