Atp5f1a ATP synthase F1 subunit alpha [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Atp5f1aprovided by MGI
Official Full Name: ATP synthase F1 subunit alphaprovided by MGI
Primary source: MGI:MGI:88115
See related: Ensembl:ENSMUSG00000025428 AllianceGenome:MGI:88115
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Atpm; Mom2; Atp5a1; D18Ertd206e
Summary: Enables ATP binding activity and proton-transporting ATP synthase activity, rotational mechanism. Acts upstream of or within lipid metabolic process. Located in membrane and mitochondrion. Is expressed in several structures, including alimentary system; heart; nervous system; respiratory system; and sensory organ. Human ortholog(s) of this gene implicated in combined oxidative phosphorylation deficiency 22; mitochondrial complex V (ATP synthase) deficiency nuclear type 4A; and mitochondrial complex V (ATP synthase) deficiency nuclear type 4B. Orthologous to human ATP5F1A (ATP synthase F1 subunit alpha). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in heart adult (RPKM 1425.7), kidney adult (RPKM 741.8) and 28 other tissues See more
Orthologs: human all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 18 E3; 18 52.38 cM

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	18	NC_000084.7 (77861468..77870569)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	18	NC_000084.6 (77773768..77782869)

Chromosome 18 - NC_000084.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Overexpression of ATP5F1A in Cardiomyocytes Promotes Cardiac Reverse Remodeling.
Title: Overexpression of ATP5F1A in Cardiomyocytes Promotes Cardiac Reverse Remodeling.
Cardiac-derived extracellular vesicles improve mitochondrial function to protect the heart against ischemia/reperfusion injury by delivering ATP5a1.
Title: Cardiac-derived extracellular vesicles improve mitochondrial function to protect the heart against ischemia/reperfusion injury by delivering ATP5a1.
Growth arrest and DNA damage-inducible alpha regulates muscle repair and fat infiltration through ATP synthase F1 subunit alpha.
Title: Growth arrest and DNA damage-inducible alpha regulates muscle repair and fat infiltration through ATP synthase F1 subunit alpha.
Loss of ATP5A1 enhances proliferation and predicts poor prognosis of colon adenocarcinoma.
Title: Loss of ATP5A1 enhances proliferation and predicts poor prognosis of colon adenocarcinoma.
Interaction between extracellular ATP5A1 and LPS alleviates LPS-induced neuroinflammation in mice.
Title: Interaction between extracellular ATP5A1 and LPS alleviates LPS-induced neuroinflammation in mice.
Poly(GR) bound preferentially to the mitochondrial complex V component ATP5A1 and enhanced its ubiquitination and degradation, consistent with reduced ATP5A1 protein level in both (GR)80 mouse neurons and amyotrophic lateral sclerosis and frontotemporal dementia patient brains.
Title: C9ORF72-ALS/FTD-associated poly(GR) binds Atp5a1 and compromises mitochondrial function in vivo.
Upregulation of ATP5A1 increased ATP5A1 and ATP synthase activity, prevented mitochondrial ROS generation and oxidative damage, and reduced cardiomyopathic changes in diabetic mice.
Title: Mitochondrial Calpain-1 Disrupts ATP Synthase and Induces Superoxide Generation in Type 1 Diabetic Hearts: A Novel Mechanism Contributing to Diabetic Cardiomyopathy.
ATP5alpha1 is an interacting subunit of the ATP synthase complex localized to the mitochondria with aryl hydrocarbon receptor in the absence of ligand.
Title: The aryl hydrocarbon receptor interacts with ATP5α1, a subunit of the ATP synthase complex, and modulates mitochondrial function.
The polyp-resistant Mom2R phenotype results from a spontaneous mutation; linkage analysis localizes Mom2 to distal chromosome 18.
Title: The modifier of Min 2 (Mom2) locus: embryonic lethality of a mutation in the Atp5a1 gene suggests a novel mechanism of polyp suppression.
Tumor analyses reveals a novel mechanism of polyp suppression by Mom2R (duplication of four nucleotides within exon 3).
Title: The modifier of Min 2 (Mom2) locus: embryonic lethality of a mutation in the Atp5a1 gene suggests a novel mechanism of polyp suppression.

Submit: New GeneRIF Correction

Variation

Go to the top of the page Help

Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Spontaneous (1) 1 citation
Targeted (1)

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Markers

RH126428 (e-PCR)
- UniSTS:163136

Atp5a1 (e-PCR), detects polymorphism
- UniSTS:546672

AI035633 (e-PCR)
- UniSTS:166104

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables ADP binding	IBA Inferred from Biological aspect of Ancestor more info
enables ADP binding	IEA Inferred from Electronic Annotation more info
enables ADP binding	ISO Inferred from Sequence Orthology more info
enables ATP binding	IBA Inferred from Biological aspect of Ancestor more info
enables ATP binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables ATP binding	ISO Inferred from Sequence Orthology more info
enables ATP hydrolysis activity	IEA Inferred from Electronic Annotation more info
contributes_to ATP hydrolysis activity	ISO Inferred from Sequence Orthology more info
enables MHC class I protein binding	IEA Inferred from Electronic Annotation more info
enables MHC class I protein binding	ISO Inferred from Sequence Orthology more info
enables angiostatin binding	IEA Inferred from Electronic Annotation more info
enables angiostatin binding	ISO Inferred from Sequence Orthology more info
enables protease binding	IEA Inferred from Electronic Annotation more info
enables protease binding	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
contributes_to proton-transporting ATP synthase activity, rotational mechanism	IBA Inferred from Biological aspect of Ancestor more info
enables proton-transporting ATP synthase activity, rotational mechanism	IMP Inferred from Mutant Phenotype more info	PubMed
contributes_to proton-transporting ATP synthase activity, rotational mechanism	ISO Inferred from Sequence Orthology more info
enables proton-transporting ATP synthase activity, rotational mechanism	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in ATP biosynthetic process	ISO Inferred from Sequence Orthology more info
involved_in cellular response to dexamethasone stimulus	IEA Inferred from Electronic Annotation more info
involved_in cellular response to nitric oxide	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within embryo development	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within lipid metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of endothelial cell proliferation	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of endothelial cell proliferation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of blood vessel endothelial cell migration	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of blood vessel endothelial cell migration	ISO Inferred from Sequence Orthology more info
involved_in proton motive force-driven ATP synthesis	IBA Inferred from Biological aspect of Ancestor more info
involved_in proton motive force-driven mitochondrial ATP synthesis	IEA Inferred from Electronic Annotation more info
involved_in proton motive force-driven mitochondrial ATP synthesis	ISO Inferred from Sequence Orthology more info
involved_in proton transmembrane transport	IEA Inferred from Electronic Annotation more info
involved_in response to ethanol	IEA Inferred from Electronic Annotation more info
involved_in response to muscle activity	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of COP9 signalosome	IEA Inferred from Electronic Annotation more info
part_of COP9 signalosome	ISO Inferred from Sequence Orthology more info
located_in cell surface	IEA Inferred from Electronic Annotation more info
located_in cell surface	ISO Inferred from Sequence Orthology more info
located_in membrane	IMP Inferred from Mutant Phenotype more info	PubMed
located_in membrane	ISO Inferred from Sequence Orthology more info
located_in membrane raft	IEA Inferred from Electronic Annotation more info
located_in membrane raft	ISO Inferred from Sequence Orthology more info
located_in mitochondrial inner membrane	HDA more info	PubMed
located_in mitochondrial inner membrane	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in myelin sheath	HDA more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
part_of proton-transporting ATP synthase complex	ISO Inferred from Sequence Orthology more info
part_of proton-transporting ATP synthase complex	ISS Inferred from Sequence or Structural Similarity more info
part_of proton-transporting ATP synthase complex, catalytic core F(1)	IBA Inferred from Biological aspect of Ancestor more info
part_of proton-transporting ATP synthase complex, catalytic core F(1)	IEA Inferred from Electronic Annotation more info
part_of proton-transporting ATP synthase complex, catalytic core F(1)	ISO Inferred from Sequence Orthology more info

General protein information

Go to the top of the page Help

Preferred Names: ATP synthase subunit alpha, mitochondrial

Names: ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1; modifier of Min 2

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_007505.2 → NP_031531.1 ATP synthase subunit alpha, mitochondrial precursor

See identical proteins and their annotated locations for NP_031531.1

Status: VALIDATED

Source sequence(s)

AK159540, BY465601, CJ155200

Consensus CDS

CCDS29358.1

UniProtKB/Swiss-Prot

Q03265, Q3TFN0, Q3THN8, Q3TPR0, Q3TPV3, Q3TZU3, Q3UIR7, Q543Y6

UniProtKB/TrEMBL

D3Z6F5

Related

ENSMUSP00000026495.9, ENSMUST00000026495.15

Conserved Domains (4) summary

PRK09281
Location:49 → 553

PRK09281; F0F1 ATP synthase subunit alpha; Validated

cd01132
Location:137 → 418

F1_ATPase_alpha; F1 ATP synthase alpha, central domain. The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to ...

pfam00306
Location:427 → 518

ATP-synt_ab_C; ATP synthase alpha/beta chain, C terminal domain

pfam02874
Location:69 → 135

ATP-synt_ab_N; ATP synthase alpha/beta family, beta-barrel domain