ATP synthase subunit O, mitochondrial

Details

Name
ATP synthase subunit O, mitochondrial
Synonyms
  • ATPO
  • Oligomycin sensitivity conferral protein
  • OSCP
Gene Name
ATP5O
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049903|ATP synthase subunit O, mitochondrial
MAAPAVSGLSRQVRCFSTSVVRPFAKLVRPPVQVYGIEGRYATALYSAASKQNKLEQVEK
ELLRVAQILKEPKVAASVLNPYVKRSIKVKSLNDITAKERFSPLTTNLINLLAENGRLSN
TQGVVSAFSTMMSVHRGEVPCTVTSASPLEEATLSELKTVLKSFLSQGQVLKLEAKTDPS
ILGGMIVRIGEKYVDMSVKTKIQKLGRAMREIV
Number of residues
213
Molecular Weight
23277.12
Theoretical pI
Not Available
GO Classification
Functions
ATPase activity / drug binding / proton-transporting ATP synthase activity, rotational mechanism / transmembrane transporter activity / transporter activity
Processes
ATP biosynthetic process / mitochondrial ATP synthesis coupled proton transport / proton transport
Components
extracellular exosome / extracellular matrix / mitochondrial inner membrane / mitochondrial proton-transporting ATP synthase complex / mitochondrion / nucleus / plasma membrane
General 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.
Specific Function
Atpase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion
Gene sequence
>lcl|BSEQ0049904|ATP synthase subunit O, mitochondrial (ATP5O)
ATGGCTGCCCCAGCAGTGTCCGGGCTCTCCCGGCAGGTGCGATGCTTCAGTACCTCTGTG
GTCAGACCATTTGCCAAGCTTGTGAGGCCTCCTGTTCAGGTATACGGTATTGAAGGTCGC
TATGCCACAGCTCTTTATTCTGCTGCATCAAAACAGAATAAGCTGGAGCAAGTAGAAAAG
GAGTTGTTGAGAGTAGCACAAATCCTGAAGGAACCCAAAGTGGCTGCTTCTGTTTTGAAT
CCCTATGTGAAGCGTTCCATTAAAGTGAAAAGCCTAAATGACATCACAGCAAAAGAGAGG
TTCTCTCCCCTCACTACCAATCTGATCAATTTGCTTGCTGAAAATGGTCGATTAAGCAAT
ACCCAAGGAGTCGTTTCTGCCTTTTCTACCATGATGAGTGTCCATCGCGGAGAGGTACCT
TGCACAGTGACCTCTGCATCTCCTTTAGAAGAAGCCACACTCTCTGAATTAAAAACTGTC
CTCAAGAGCTTCCTAAGTCAAGGCCAAGTATTGAAATTGGAGGCTAAGACTGATCCGTCA
ATCTTGGGTGGAATGATTGTGCGCATTGGCGAGAAATATGTTGACATGTCTGTCAAGACC
AAGATTCAGAAGCTGGGCAGGGCTATGCGGGAGATTGTCTAA
Chromosome Location
21
Locus
21q22.11
External Identifiers
ResourceLink
UniProtKB IDP48047
UniProtKB Entry NameATPO_HUMAN
HGNC IDHGNC:850
General References
  1. 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. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB11638Artenimolapproved, experimental, investigationalunknownligandDetails
DB01119DiazoxideapprovedunknowninhibitorDetails