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Identification
HMDB Protein ID HMDBP01275
Secondary Accession Numbers
  • 6571
Name ATP synthase subunit O, mitochondrial
Synonyms
  1. OSCP
  2. Oligomycin sensitivity conferral protein
Gene Name ATP5O
Protein Type Enzyme
Biological Properties
General Function Involved in hydrogen ion transporting ATP synthase activity, rotational mechanism
Specific Function Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements
Pathways Not Available
Reactions Not Available
GO Classification
Component
membrane
cell part
proton-transporting atp synthase complex, catalytic core f(1)
proton-transporting two-sector atpase complex, catalytic domain
plasma membrane
macromolecular complex
protein complex
Function
hydrogen ion transporting atp synthase activity, rotational mechanism
transmembrane transporter activity
substrate-specific transmembrane transporter activity
ion transmembrane transporter activity
cation transmembrane transporter activity
inorganic cation transmembrane transporter activity
monovalent inorganic cation transmembrane transporter activity
hydrogen ion transmembrane transporter activity
transporter activity
Process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
purine nucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate biosynthetic process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
atp synthesis coupled proton transport
atp biosynthetic process
Cellular Location
  1. Mitochondrion
  2. Mitochondrion inner membrane
Gene Properties
Chromosome Location Chromosome:2
Locus 21q22.1-q22.2|21q22.11
SNPs ATP5O
Gene Sequence
>642 bp
ATGGCTGCCCCAGCAGTGTCCGGGCTCTCCCGGCAGGTGCGATGCTTCAGTACCTCTGTG
GTCAGACCATTTGCCAAGCTTGTGAGGCCTCCTGTTCAGGTATACGGTATTGAAGGTCGC
TATGCCACAGCTCTTTATTCTGCTGCATCAAAACAGAATAAGCTGGAGCAAGTAGAAAAG
GAGTTGTTGAGAGTAGCACAAATCCTGAAGGAACCCAAAGTGGCTGCTTCTGTTTTGAAT
CCCTATGTGAAGCGTTCCATTAAAGTGAAAAGCCTAAATGACATCACAGCAAAAGAGAGG
TTCTCTCCCCTCACTACCAACCTGATCAATTTGCTTGCTGAAAATGGTCGATTAAGCAAT
ACCCAAGGAGTCGTTTCTGCCTTTTCTACCATGATGAGTGTCCATCGCGGAGAGGTACCT
TGCACAGTGACCTCTGCATCTCCTTTAGAAGAAGCCACACTCTCTGAATTAAAAACTGTC
CTCAAGAGCTTCCTAAGTCAAGGCCAAGTATTGAAATTGGAGGCTAAGACTGATCCGTCA
ATCTTGGGTGGAATGATTGTGCGCATTGGCGAGAAATATGTTGACATGTCTGTCAAGACC
AAGATTCAGAAGCTGGGCAGGGCTATGCGGGAGATTGTCTAA
Protein Properties
Number of Residues 213
Molecular Weight 23277.1
Theoretical pI 10.61
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>ATP synthase subunit O, mitochondrial
MAAPAVSGLSRQVRCFSTSVVRPFAKLVRPPVQVYGIEGRYATALYSAASKQNKLEQVEK
ELLRVAQILKEPKVAASVLNPYVKRSIKVKSLNDITAKERFSPLTTNLINLLAENGRLSN
TQGVVSAFSTMMSVHRGEVPCTVTSASPLEEATLSELKTVLKSFLSQGQVLKLEAKTDPS
ILGGMIVRIGEKYVDMSVKTKIQKLGRAMREIV
GenBank ID Protein 1008080
UniProtKB/Swiss-Prot ID P48047
UniProtKB/Swiss-Prot Entry Name ATPO_HUMAN
PDB IDs Not Available
GenBank Gene ID X83218
GeneCard ID ATP5O
GenAtlas ID ATP5O
HGNC ID HGNC:850
References
General References
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  2. 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. [PubMed:15489334 ]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
  5. Chen H, Morris MA, Rossier C, Blouin JL, Antonarakis SE: Cloning of the cDNA for the human ATP synthase OSCP subunit (ATP5O) by exon trapping and mapping to chromosome 21q22.1-q22.2. Genomics. 1995 Aug 10;28(3):470-6. [PubMed:7490082 ]