ATP5PO
entrez
539
canonical
uniprot
P48047
canonical
ensembl
ENSG00000241837
resolver
ensp
ENSP00000290299
resolver
enst
ENST00000290299
resolver
genesymbol
ATP5PO
resolver
genesymbol_syn
ATP5O
resolver
genesymbol_syn
ATPO
resolver
hgnc
HGNC:850
resolver
uniprot
B2R4E2
resolver
uniprot
Q5U042
resolver
uniprot
Q6IBI2
resolver
uniprot_entry
ATPO_HUMAN
resolver
uniprot_sec
B2R4E2
resolver
uniprot_sec
Q5U042
resolver
uniprot_sec
Q6IBI2
resolver
amino_acid_sequence
MAAPAVSGLSRQVRCFSTSVVRPFAKLVRPPVQVYGIEGRYATALYSAASKQNKLEQVEKELLRVAQILKEPKVAASVLNPYVKRSIKVKSLNDITAKERFSPLTTNLINLLAENGRLSNTQGVVSAFSTMMSVHRGEVPCTVTSASPLEEATLSELKTVLKSFLSQGQVLKLEAKTDPSILGGMIVRIGEKYVDMSVKTKIQKLGRAMREIV
uniprot
proteins
disease_involvement
DISEASE: Mitochondrial complex V deficiency, nuclear type 7 (MC5DN7) [MIM:620359]: An autosomal recessive, severe, mitochondrial disorder apparent soon after birth. It is characterized by multisystemic features that include hypotonia, developmental delay, progressive epileptic encephalopathy, progressive cerebral atrophy, white matter abnormalities on brain imaging, and hypertrophic cardiomyopathy in some patients. Death in infancy or early childhood may occur. {ECO:0000269|PubMed:34954817}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Subunit OSCP, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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 (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). 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 (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (PubMed:37244256). 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 (By similarity). {ECO:0000250|UniProtKB:P13621, ECO:0000250|UniProtKB:P19483, ECO:0000269|PubMed:37244256, ECO:0000305|PubMed:37244256}.
uniprot
proteins
mass_dalton
23277
uniprot
proteins
mutagenesis
MUTAGEN 162; /note="K->R: Increased ATP levels."; /evidence="ECO:0000269|Ref.11
uniprot
proteins
post_translational_modification
PTM: Acetylation at Lys-162 decreases ATP production. Deacetylated by SIRT3. {ECO:0000269|Ref.11}.; PTM: In response to mitochondrial stress, the precursor protein is ubiquitinated by the SIFI complex in the cytoplasm before mitochondrial import, leading to its degradation (PubMed:38297121). Within the SIFI complex, UBR4 initiates ubiquitin chain that are further elongated or branched by KCMF1 (PubMed:38297121). {ECO:0000269|PubMed:38297121}.
uniprot
proteins
protein_family
ATPase delta chain family
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
34954817
uniprot
proteins
pubmed
37244256
uniprot
proteins
pubmed
38297121
uniprot
proteins
pubmed
7490082
uniprot
proteins
sequence_length
213
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}.
uniprot
proteins