MT-ATP8

ATP8

Identifiers

ATP8, ATPase8, MTMT-ATP synthase F0 subunit 8

External IDs

Gene ontology
Molecular function	• ATPase activity • transmembrane transporter activity • hydrogen ion transmembrane transporter activity
Cellular component	• integral component of membrane • mitochondrial inner membrane • mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) • mitochondrial proton-transporting ATP synthase complex • mitochondrion • membrane • mitochondrial membrane • proton-transporting ATP synthase complex, coupling factor F(o)
Biological process	• response to hyperoxia • mitochondrial ATP synthesis coupled proton transport • ATP synthesis coupled proton transport • ion transport • proton transport • transport • ATP biosynthetic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


4509


n/a

Ensembl


ENSG00000228253


n/a

UniProt


P03928


n/a

RefSeq (mRNA)


n/a


n/a

RefSeq (protein)


n/a


n/a

Location (UCSC)

Chr M: 0.01 – 0.01 Mb

n/a

PubMed search

^[1]

n/a

Wikidata

View/Edit Human

Location of the MT-ATP8 gene in the human mitochondrial genome. MT-ATP8 is one of the two ATP synthase mitochondrial genes (red boxes).

The 46-nucleotide overlap in the reading frames of the human mitochondrial genes MT-ATP8 and MT-ATP6. For each nucleotide triplet (square brackets), the corresponding amino acid is given (one-letter code), either in the +1 frame for MT-ATP8 (in red) or in the +3 frame for MT-ATP6 (in blue).

ATP synthase protein 8 (metazoa)

Identifiers

Symbol

ATP-synt_8

Pfam clan

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Plant ATP synthase F0 subunit 8

Identifiers

Symbol

YMF19

Pfam clan

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Fungal ATP synthase protein 8 (A6L)

Identifiers

Symbol

Fun_ATP-synt_8

Pfam clan

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

The protein

ATP synthase protein 8 is a subunit of mitochondrial ATP synthase.

This protein subunit appears to be an integral component of the stator stalk in yeast mitochondrial F-ATPases.^[2] The stator stalk is anchored in the membrane, and acts to prevent futile rotation of the ATPase subunits relative to the rotor during coupled ATP synthesis/hydrolysis. This subunit may have an analogous function in Metazoa.

Subunit 8 differs in sequence between Metazoa, plants and Fungi.

The gene

The ATP synthase protein 8 of human and other mammals is encoded in the mitochondrial genome by the MT-ATP8 gene. When the complete human mitochondrial genome was first published, the MT-ATP8 gene was described as the unidentified reading frame URF A6L.^[3]

An unusual feature of the MT-ATP8 gene is its 46-nucleotide overlap with the MT-ATP6 gene. With respect to the reading frame (+1) of MT-ATP8, the MT-ATP6 gene starts on the +3 reading frame.

References

↑ "Human PubMed Reference:".
↑ Stephens AN, Khan MA, Roucou X, Nagley P, Devenish RJ (May 2003). "The molecular neighborhood of subunit 8 of yeast mitochondrial F1F0-ATP synthase probed by cysteine scanning mutagenesis and chemical modification". J. Biol. Chem. 278 (20): 17867–75. doi:10.1074/jbc.M300967200. PMID 12626501.
↑ Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG (April 1981). "Sequence and organization of the human mitochondrial genome". Nature. 290 (5806): 457–65. doi:10.1038/290457a0. PMID 7219534.

Torroni A, Achilli A, Macaulay V, et al. (2006). "Harvesting the fruit of the human mtDNA tree.". Trends Genet. 22 (6): 339–45. doi:10.1016/j.tig.2006.04.001. PMID 16678300.
Bodenteich A, Mitchell LG, Polymeropoulos MH, Merril CR (1993). "Dinucleotide repeat in the human mitochondrial D-loop.". Hum. Mol. Genet. 1 (2): 140. doi:10.1093/hmg/1.2.140-a. PMID 1301157.
Lu X, Walker T, MacManus JP, Seligy VL (1992). "Differentiation of HT-29 human colonic adenocarcinoma cells correlates with increased expression of mitochondrial RNA: effects of trehalose on cell growth and maturation.". Cancer Res. 52 (13): 3718–25. PMID 1377597.
Marzuki S, Noer AS, Lertrit P, et al. (1992). "Normal variants of human mitochondrial DNA and translation products: the building of a reference data base.". Hum. Genet. 88 (2): 139–45. doi:10.1007/bf00206061. PMID 1757091.
Moraes CT, Andreetta F, Bonilla E, et al. (1991). "Replication-competent human mitochondrial DNA lacking the heavy-strand promoter region.". Mol. Cell. Biol. 11 (3): 1631–7. PMC 369459. PMID 1996112.
Attardi G, Chomyn A, Doolittle RF, et al. (1987). "Seven unidentified reading frames of human mitochondrial DNA encode subunits of the respiratory chain NADH dehydrogenase.". Cold Spring Harb. Symp. Quant. Biol. 51 (1): 103–14. doi:10.1101/sqb.1986.051.01.013. PMID 3472707.
Chomyn A, Cleeter MW, Ragan CI, et al. (1986). "URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit.". Science. 234 (4776): 614–8. doi:10.1126/science.3764430. PMID 3764430.
Chomyn A, Mariottini P, Cleeter MW, et al. (1985). "Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase.". Nature. 314 (6012): 592–7. doi:10.1038/314592a0. PMID 3921850.
Anderson S, Bankier AT, Barrell BG, et al. (1981). "Sequence and organization of the human mitochondrial genome.". Nature. 290 (5806): 457–65. doi:10.1038/290457a0. PMID 7219534.
Montoya J, Ojala D, Attardi G (1981). "Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs.". Nature. 290 (5806): 465–70. doi:10.1038/290465a0. PMID 7219535.
Horai S, Hayasaka K, Kondo R, et al. (1995). "Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs.". Proc. Natl. Acad. Sci. U.S.A. 92 (2): 532–6. doi:10.1073/pnas.92.2.532. PMC 42775. PMID 7530363.
Rieder MJ, Taylor SL, Tobe VO, Nickerson DA (1998). "Automating the identification of DNA variations using quality-based fluorescence re-sequencing: analysis of the human mitochondrial genome.". Nucleic Acids Res. 26 (4): 967–73. doi:10.1093/nar/26.4.967. PMC 147367. PMID 9461455.
Andrews RM, Kubacka I, Chinnery PF, et al. (1999). "Reanalysis and revision of the Cambridge reference sequence for human mitochondrial DNA.". Nat. Genet. 23 (2): 147. doi:10.1038/13779. PMID 10508508.
Ingman M, Kaessmann H, Pääbo S, Gyllensten U (2001). "Mitochondrial genome variation and the origin of modern humans.". Nature. 408 (6813): 708–13. doi:10.1038/35047064. PMID 11130070.
Finnilä S, Lehtonen MS, Majamaa K (2001). "Phylogenetic network for European mtDNA.". Am. J. Hum. Genet. 68 (6): 1475–84. doi:10.1086/320591. PMC 1226134. PMID 11349229.
Maca-Meyer N, González AM, Larruga JM, et al. (2003). "Major genomic mitochondrial lineages delineate early human expansions.". BMC Genet. 2: 13. doi:10.1186/1471-2156-2-13. PMC 55343. PMID 11553319.
Herrnstadt C, Elson JL, Fahy E, et al. (2002). "Reduced-median-network analysis of complete mitochondrial DNA coding-region sequences for the major African, Asian, and European haplogroups.". Am. J. Hum. Genet. 70 (5): 1152–71. doi:10.1086/339933. PMC 447592. PMID 11938495.
Silva WA, Bonatto SL, Holanda AJ, et al. (2002). "Mitochondrial genome diversity of Native Americans supports a single early entry of founder populations into America.". Am. J. Hum. Genet. 71 (1): 187–92. doi:10.1086/341358. PMC 384978. PMID 12022039.
Mishmar D, Ruiz-Pesini E, Golik P, et al. (2003). "Natural selection shaped regional mtDNA variation in humans.". Proc. Natl. Acad. Sci. U.S.A. 100 (1): 171–6. doi:10.1073/pnas.0136972100. PMC 140917. PMID 12509511.
Ingman M, Gyllensten U (2003). "Mitochondrial genome variation and evolutionary history of Australian and New Guinean aborigines.". Genome Res. 13 (7): 1600–6. doi:10.1101/gr.686603. PMC 403733. PMID 12840039.

Mitochondrial proteins

Outer membrane

fatty acid degradation	Carnitine palmitoyltransferase I Long-chain-fatty-acid—CoA ligase

tryptophan metabolism	Kynureninase

monoamine neurotransmitter metabolism	Monoamine oxidase

Intermembrane space

Inner membrane

oxidative phosphorylation	Coenzyme Q – cytochrome c reductase Cytochrome c NADH dehydrogenase Succinate dehydrogenase

pyrimidine metabolism	Dihydroorotate dehydrogenase

mitochondrial shuttle	Malate-aspartate shuttle Glycerol phosphate shuttle

other	Glutamate aspartate transporter Glycerol-3-phosphate dehydrogenase ATP synthase Carnitine palmitoyltransferase II Uncoupling protein

Matrix

citric acid cycle	Citrate synthase Aconitase Isocitrate dehydrogenase Oxoglutarate dehydrogenase complex Succinyl coenzyme A synthetase Fumarase Malate dehydrogenase

anaplerotic reactions	Aspartate transaminase Glutamate dehydrogenase Pyruvate dehydrogenase complex

urea cycle	Carbamoyl phosphate synthetase I Ornithine transcarbamylase N-Acetylglutamate synthase

alcohol metabolism	ALDH2

PMPCB

Other/to be sorted

steroidogenesis	Cholesterol side-chain cleavage enzyme Steroid 11-beta-hydroxylase Aldosterone synthase Frataxin

Mitochondrial membrane transport protein Mitochondrial permeability transition pore Mitochondrial carrier

Mitochondrial DNA

Complex I	MT-ND1 MT-ND2 MT-ND3 MT-ND4 MT-ND4L MT-ND5 MT-ND6

Complex III	MT-CYB

Complex IV	MT-CO1 MT-CO2 MT-CO3

ATP synthase	MT-ATP6 MT-ATP8

tRNA	MT-TA MT-TC MT-TD MT-TE MT-TF MT-TG MT-TH MT-TI MT-TK MT-TL1 MT-TL2 MT-TM MT-TN MT-TP MT-TQ MT-TR MT-TS1 MT-TS2 MT-TT MT-TV MT-TW MT-TY

see also mitochondrial diseases

This article incorporates text from the public domain Pfam and InterPro IPR001421

This article is issued from Wikipedia - version of the 8/30/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

MT-ATP8

The protein

The gene

References

Further reading