P15999 · ATPA_RAT
- ProteinATP synthase subunit alpha, mitochondrial
- GeneAtp5f1a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids553 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mitochondrial membrane ATP synthase (F1F0 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, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity).
Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (By similarity).
Miscellaneous
The siderophore enterobactin (Ent) produced by enteric bacteria binds Fe3+ and helps bacteria scavenge iron ions from the environment. 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.
Features
Showing features for binding site, site.
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP synthase subunit alpha, mitochondrial
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP15999
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Peripheral membrane protein
Cell membrane ; Peripheral membrane protein
Note: Colocalizes with HRG on the cell surface of T-cells.
Keywords
- Cellular component
Phenotypes & Variants
Variants
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The viewer provides 4 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-43 | Mitochondrion | ||||
Sequence: MLSVRIAAAVARALPRRAGLVSKNALGSSFVGTRNLHASNTRL | ||||||
Chain | PRO_0000002427 | 44-553 | ATP synthase subunit alpha, mitochondrial | |||
Sequence: QKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFESAFLSHVVSQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGFEP | ||||||
Modified residue | 53 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 65 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 76 | Phosphoserine; alternate | ||||
Sequence: S | ||||||
Glycosylation | 76 | O-linked (GlcNAc) serine; alternate | ||||
Sequence: S | ||||||
Modified residue | 106 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 123 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 126 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 132 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 134 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 161 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 161 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 166 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 167 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 167 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 184 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 204 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 230 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 230 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 239 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 239 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 240 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 261 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 261 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 305 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 305 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 427 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 427 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 434 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 498 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 498 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 506 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 506 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 531 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 531 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 539 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 539 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 541 | N6-acetyllysine | ||||
Sequence: K |
Post-translational modification
Acetylated on lysine residues. BLOC1S1 is required for acetylation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in flagella of epididymal sperm.
Interaction
Subunit
F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1 (PubMed:17575325, PubMed:9736690).
CF0 has three main subunits: a, b and c (PubMed:17575325).
Interacts with ATPAF2. Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro). Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin (By similarity).
Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MPL (By similarity).
Interacts with BLOC1S1 (By similarity).
Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficiency (PubMed:21926988).
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 (PubMed:31511561).
CF0 has three main subunits: a, b and c (PubMed:17575325).
Interacts with ATPAF2. Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro). Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin (By similarity).
Component of an ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MPL (By similarity).
Interacts with BLOC1S1 (By similarity).
Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficiency (PubMed:21926988).
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 (PubMed:31511561).
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length553
- Mass (Da)59,754
- Last updated2005-12-06 v2
- ChecksumD48886ED1245302C
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F1LP05 | F1LP05_RAT | Atp5f1a | 553 | ||
A0A8I5ZXA2 | A0A8I5ZXA2_RAT | Atp5f1a | 538 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 11 | in Ref. 2; AAA40784 | ||||
Sequence: A → R | ||||||
Sequence conflict | 321 | in Ref. 4; CAA39599 | ||||
Sequence: Y → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC061830 EMBL· GenBank· DDBJ | AAH61830.1 EMBL· GenBank· DDBJ | mRNA | ||
J05266 EMBL· GenBank· DDBJ | AAA40784.1 EMBL· GenBank· DDBJ | mRNA | ||
X56133 EMBL· GenBank· DDBJ | CAA39599.1 EMBL· GenBank· DDBJ | mRNA |