Atp5f1a
entrez
11946
canonical
uniprot
Q03265
canonical
ensembl
ENSMUSG00000025428
resolver
ensp
ENSMUSP00000026495
resolver
enst
ENSMUST00000026495
resolver
genesymbol
Atp5f1a
resolver
genesymbol_syn
Atp5a1
resolver
uniprot
Q3TFN0
resolver
uniprot
Q3THN8
resolver
uniprot
Q3TPR0
resolver
uniprot
Q3TPV3
resolver
uniprot
Q3TZU3
resolver
uniprot
Q3UIR7
resolver
uniprot
Q543Y6
resolver
uniprot_entry
ATPA_MOUSE
resolver
uniprot_sec
Q3TFN0
resolver
uniprot_sec
Q3THN8
resolver
uniprot_sec
Q3TPR0
resolver
uniprot_sec
Q3TPV3
resolver
uniprot_sec
Q3TZU3
resolver
uniprot_sec
Q3UIR7
resolver
uniprot_sec
Q543Y6
resolver
amino_acid_sequence
MLSVRVAAAVARALPRRAGLVSKNALGSSFVGARNLHASNTRLQKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDVVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGFEP
uniprot
proteins
function
FUNCTION: Subunit alpha, 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. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary 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 (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). {ECO:0000250|UniProtKB:P19483, ECO:0000250|UniProtKB:P25705}.
uniprot
proteins
mass_dalton
59753
uniprot
proteins
post_translational_modification
PTM: Acetylated on lysine residues. BLOC1S1 is required for acetylation (By similarity). Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice. {ECO:0000250|UniProtKB:P25705}.
uniprot
proteins
protein_family
ATPase alpha/beta chains family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15648052
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17438143
uniprot
proteins
pubmed
19941651
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
7916601
uniprot
proteins
sequence_length
553
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17438143}; Peripheral membrane protein {ECO:0000269|PubMed:17438143}; Matrix side {ECO:0000250|UniProtKB:P19483}. Cell membrane {ECO:0000250|UniProtKB:P25705}; Peripheral membrane protein {ECO:0000250|UniProtKB:P25705}; Extracellular side {ECO:0000250|UniProtKB:P25705}. Note=Colocalizes with HRG on the cell surface of T-cells. {ECO:0000250|UniProtKB:P25705}.
uniprot
proteins