UniProt:P25705 ATP5F1A

chain
  • transit peptide:1-43
  • chain:44-553
checksum AA47BBB8EDA77EAC
comment
  • 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 (Probable). 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). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain (PubMed:37244256). Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (Probable). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed:30146159).SUBUNIT Homotrimer (PubMed:37244256). Component of the ATP synthase complex composed at least of ATP5F1A/subunit alpha, ATP5F1B/subunit beta, ATP5MC1/subunit c (homooctamer), MT-ATP6/subunit a, MT-ATP8/subunit 8, ATP5ME/subunit e, ATP5MF/subunit f, ATP5MG/subunit g, ATP5MK/subunit k, ATP5MJ/subunit j, ATP5F1C/subunit gamma, ATP5F1D/subunit delta, ATP5F1E/subunit epsilon, ATP5PF/subunit F6, ATP5PB/subunit b, ATP5PD/subunit d, ATP5PO/subunit OSCP (PubMed:37244256). ATP synthase complex consists of a soluble F(1) head domain (subunits alpha(3) and beta(3)) - the catalytic core - and a membrane F(0) domain - the membrane proton channel (subunits c, a, 8, e, f, g, k and j) (PubMed:37244256). These two domains are linked by a central stalk (subunits gamma, delta, and epsilon) rotating inside the F1 region and a stationary peripheral stalk (subunits F6, b, d, and OSCP) (PubMed:37244256). Interacts with ATPAF2 (PubMed:11410595). Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro) (PubMed:19285951). Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin (PubMed:10077593). Interacts with BLOC1S1 (PubMed:22309213). Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F(1)F(0) ATP synthase and enhances neurons metabolic efficiency (By similarity). Interacts with CLN5 and PPT1 (By similarity). Interacts with S100A1; this interaction increases F1-ATPase activity (By similarity). Interacts with ABCB7; this interaction allows the regulation of cellular iron homeostasis and cellular reactive oxygen species (ROS) levels in cardiomyocytes (By similarity).INTERACTION Colocalizes with HRG on the cell surface of T-cells (PubMed:19285951).ALTERNATIVE PRODUCTS Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord.PTM The N-terminus is blocked.PTM Acetylated on lysine residues. BLOC1S1 is required for acetylation.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.MISCELLANEOUS The siderophore enterobactin (Ent) produced by enteric bacteria binds Fe(3+) and helps bacteria scavenge iron ions from the environment (PubMed:30146159). As a consequence, the mammalian siderocalin LCN2 plays an important role in defense against bacterial infections by sequestering iron bound to microbial siderophores. LCN2 can also bind iron bound to endogenous or nutrient-derived iron chelators and plays an important role in cellular iron homeostasis. Enterobactin produced by non-pathogenic E.coli strains can facilitate mitochondrial iron assimilation, suggesting that iron bound to siderophores from non-pathogenic bacteria may contribute to iron absorption by the host (PubMed:30146159).SIMILARITY Belongs to the ATPase alpha/beta chains family.
crossReference
databaseName UniProt
dbId 50503
description
  • recommendedName: fullName evidence="18"ATP synthase F(1) complex subunit alpha, mitochondrial alternativeName: fullName evidence="20"ATP synthase F1 subunit alpha
displayName UniProt:P25705 ATP5F1A
geneName
  • ATP5F1A
  • ATP5A
  • ATP5A1
  • ATP5AL2
  • ATPM
identifier P25705
isSequenceChanged false
keyword
  • 3D-structure
  • Acetylation
  • Alternative splicing
  • ATP synthesis
  • ATP-binding
  • Cell membrane
  • CF(1)
  • Direct protein sequencing
  • Disease variant
  • Glycoprotein
  • Hydrogen ion transport
  • Ion transport
  • Membrane
  • Methylation
  • Mitochondrion
  • Mitochondrion inner membrane
  • Nucleotide-binding
  • Phosphoprotein
  • Primary mitochondrial disease
  • Proteomics identification
  • Reference proteome
  • Transit peptide
  • Translocase
  • Transport
modified [InstanceEdit:9983091] Weiser, Joel, 2026-02-20
moleculeType Protein
name
  • ATP5F1A
otherIdentifier
  • 11728637_a_at
  • 11753328_a_at
  • 11753329_x_at
  • 11756890_s_at
  • 16734670
  • 16854926
  • 16854928
  • 16909411
  • 213738_PM_s_at
  • 213738_s_at
  • 2603023
  • 3206246
  • 3206249
  • 3206267
  • 3206269
  • 3206653
  • 3566579
  • 3603600
  • 3697993
  • 3698012
  • 3806248
  • 3806250
  • 3806252
  • 3806254
  • 3806255
  • 3806256
  • 3806257
  • 3806258
  • 3806259
  • 3806260
  • 3806261
  • 3806262
  • 3806263
  • 3806264
  • 3806265
  • 3806266
  • 3806267
  • 3806268
  • 3806269
  • 3806270
  • 3806271
  • 3806272
  • 3806273
  • 3806274
  • 3806275
  • 3806276
  • 3806277
  • 3806278
  • 3806279
  • 3806282
  • 3806283
  • 3806284
  • 3806285
  • 3806286
  • 3806288
  • 40096_at
  • 498
  • 67371_at
  • 7945892
  • 8023061
  • 8023063
  • 8059648
  • A_19_P00802407
  • A_24_P245358
  • D14710_at
  • GE57089
  • GE584414
  • GE792903
  • GO:0000166
  • GO:0001937
  • GO:0002020
  • GO:0003723
  • GO:0005515
  • GO:0005524
  • GO:0005737
  • GO:0005739
  • GO:0005743
  • GO:0005759
  • GO:0005886
  • GO:0006629
  • GO:0006754
  • GO:0006811
  • GO:0009986
  • GO:0014850
  • GO:0015986
  • GO:0016020
  • GO:0016469
  • GO:0016787
  • GO:0016874
  • GO:0016887
  • GO:0032559
  • GO:0042288
  • GO:0042776
  • GO:0043531
  • GO:0043532
  • GO:0043536
  • GO:0045121
  • GO:0045259
  • GO:0045471
  • GO:0046034
  • GO:0046933
  • GO:0055085
  • GO:0055086
  • GO:0070062
  • GO:0071549
  • GO:0071732
  • GO:1901135
  • GO:1902495
  • GO:1902600
  • HMNXSV003042184
  • Hs.155101.3.A1_3p_a_at
  • ILMN_1764494
  • ILMN_1874613
  • ILMN_2341363
  • PH_hs_0038681
  • TC14001175.hg
  • TC15000736.hg
  • TC18000479.hg
  • TC18000480.hg
  • TC18000481.hg
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • ATPA_HUMAN
  • A8K092
  • B4DY56
  • K7ENP3
  • Q53XX6
  • Q8IXV2
  • Q96FB4
  • Q96HW2
  • Q96IR6
  • Q9BTV8
sequenceLength 553
species [Species:48887] Homo sapiens
stId uniprot:P25705
url http://purl.uniprot.org/uniprot/P25705
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