V-type proton ATPase subunit d 1

Details

Name
V-type proton ATPase subunit d 1
Synonyms
  • 32 kDa accessory protein
  • ATP6D
  • p39
  • V-ATPase 40 kDa accessory protein
  • V-ATPase AC39 subunit
  • V-ATPase subunit d 1
  • Vacuolar proton pump subunit d 1
  • VPATPD
Gene Name
ATP6V0D1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0052421|V-type proton ATPase subunit d 1
MSFFPELYFNVDNGYLEGLVRGLKAGVLSQADYLNLVQCETLEDLKLHLQSTDYGNFLAN
EASPLTVSVIDDRLKEKMVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQR
SIAELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEI
IRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKL
FPHCGRLYPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVK
LNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF
Number of residues
351
Molecular Weight
40328.66
Theoretical pI
Not Available
GO Classification
Functions
protein-containing complex binding / proton-exporting ATPase activity, phosphorylative mechanism / proton-transporting ATPase activity, rotational mechanism
Processes
brain development / cellular iron ion homeostasis / cellular response to increased oxygen levels / cilium assembly / insulin receptor signaling pathway / ion transmembrane transport / IRE1-mediated unfolded protein response / phagosome acidification / proton transmembrane transport / regulation of macroautophagy / transferrin transport / vacuolar acidification / vacuolar transport
Components
apical plasma membrane / axon terminus / cell / early endosome / endosome membrane / extracellular exosome / lysosomal membrane / membrane / phagocytic vesicle membrane / plasma membrane proton-transporting V-type ATPase complex / proton-transporting V-type ATPase, V0 domain / synaptic vesicle / vacuolar proton-transporting V-type ATPase complex
General Function
Subunit of the integral membrane V0 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. May play a role in coupling of proton transport and ATP hydrolysis (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633).
Specific Function
Protein-containing complex binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0052422|V-type proton ATPase subunit d 1 (ATP6V0D1)
ATGTCGTTCTTCCCGGAGCTTTACTTTAACGTGGACAATGGCTACTTGGAGGGACTGGTG
CGCGGCCTGAAGGCCGGGGTGCTCAGCCAGGCCGACTACCTCAACCTGGTGCAGTGCGAG
ACGCTAGAGGACTTGAAACTGCATCTGCAGAGCACTGATTATGGTAACTTCCTGGCCAAC
GAGGCATCACCTCTGACGGTGTCAGTCATCGATGACCGGCTCAAGGAGAAGATGGTGGTG
GAGTTCCGCCACATGAGGAACCATGCCTATGAGCCACTCGCCAGCTTCCTAGACTTCATT
ACTTACAGTTACATGATCGACAACGTGATCCTGCTCATCACAGGCACGCTGCACCAGCGC
TCCATCGCTGAGCTCGTGCCCAAGTGCCACCCACTAGGCAGCTTCGAGCAGATGGAGGCC
GTGAACATTGCTCAGACACCTGCTGAGCTCTACAATGCCATTCTGGTGGACACGCCTCTT
GCGGCTTTTTTCCAGGACTGCATTTCAGAGCAGGACCTTGACGAGATGAACATCGAGATC
ATCCGCAACACCCTCTACAAGGCCTACCTGGAGTCCTTCTACAAGTTCTGCACCCTACTG
GGCGGGACTACGGCTGATGCCATGTGCCCCATCCTGGAGTTTGAAGCAGACCGCCGCGCC
TTCATCATCACCATCAATTCTTTCGGCACAGAGCTGTCCAAAGAGGACCGTGCCAAGCTC
TTTCCACACTGTGGGCGGCTCTACCCTGAGGGCCTGGCGCAGCTGGCTCGGGCTGACGAC
TATGAACAGGTCAAGAACGTGGCCGATTACTACCCGGAGTACAAGCTGCTCTTCGAGGGT
GCAGGTAGCAACCCTGGAGACAAGACGCTGGAGGACCGATTCTTTGAGCACGAGGTAAAG
CTGAACAAGTTGGCCTTCCTGAACCAGTTCCACTTTGGTGTCTTCTATGCCTTCGTGAAG
CTCAAGGAGCAGGAGTGTCGCAACATCGTGTGGATCGCTGAATGTATCGCCCAGCGCCAC
CGCGCCAAAATCGACAACTACATCCCTATCTTCTAG
Chromosome Location
16
Locus
16q22.1
External Identifiers
ResourceLink
UniProtKB IDP61421
UniProtKB Entry NameVA0D1_HUMAN
HGNC IDHGNC:13724
General References
  1. van Hille B, Vanek M, Richener H, Green JR, Bilbe G: Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase. Biochem Biophys Res Commun. 1993 Nov 30;197(1):15-21. [Article]
  2. Agarwal AK, White PC: Structure of the VPATPD gene encoding subunit D of the human vacuolar proton ATPase. Biochem Biophys Res Commun. 2000 Dec 20;279(2):543-7. doi: 10.1006/bbrc.2000.4003. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Smith AN, Borthwick KJ, Karet FE: Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis. Gene. 2002 Sep 4;297(1-2):169-77. [Article]
  5. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  6. Chen Y, Wu B, Xu L, Li H, Xia J, Yin W, Li Z, Shi D, Li S, Lin S, Shu X, Pei D: A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in vivo. Cell Res. 2012 Feb;22(2):333-45. doi: 10.1038/cr.2011.134. Epub 2011 Aug 16. [Article]
  7. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  8. Miles AL, Burr SP, Grice GL, Nathan JA: The vacuolar-ATPase complex and assembly factors, TMEM199 and CCDC115, control HIF1alpha prolyl hydroxylation by regulating cellular iron levels. Elife. 2017 Mar 15;6. doi: 10.7554/eLife.22693. [Article]
  9. Hashimoto Y, Shirane M, Nakayama KI: TMEM55B contributes to lysosomal homeostasis and amino acid-induced mTORC1 activation. Genes Cells. 2018 Jun;23(6):418-434. doi: 10.1111/gtc.12583. Epub 2018 Apr 27. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01133Tiludronic acidapproved, investigational, vet_approvedunknowninhibitorDetails