Version 5.4
Mus musculus Protein: Atp5l
Summary
InnateDB Protein IDBP-158711.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Atp5l
Protein Name ATP synthase, H+ transporting, mitochondrial F0 complex, subunit g
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000047960
InnateDB Gene IDBG-158709 (Atp5l)
Protein Structure
UniProt Annotation
Function Mitochondrial membrane ATP synthase (F(1)F(0) 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, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a 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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular Localization Mitochondrion. Mitochondrion inner membrane.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
They are also associated with 10 interaction(s) predicted by orthology.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 10 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0015078 hydrogen ion transmembrane transporter activity
Biological Process
GO:0015986 ATP synthesis coupled proton transport
Cellular Component
GO:0000276 mitochondrial proton-transporting ATP synthase complex, coupling factor F(o)
GO:0005753 mitochondrial proton-transporting ATP synthase complex
Protein Structure and Domains
PDB ID MGI:1351597
InterPro IPR006808 ATPase, F0 complex, subunit G, mitochondrial
IPR016702 Mitochondrial ATP synthase subunit g, animal
PFAM PF04718
PRINTS
PIRSF PIRSF017835
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9CPQ8
PhosphoSite PhosphoSite-Q9CPQ8
TrEMBL
UniProt Splice Variant
Entrez Gene 27425
UniGene Mm.398844
RefSeq NP_038823
MGI ID
MGI Symbol Atp5l
OMIM
CCDS CCDS40604
HPRD
IMGT
EMBL AK005175 AK005321 AK005380 AK008002 AK008012 AK008030 AK008087 AK008183 AK008251 AK008321 AK009465 AK009468 AK009471 AK009612 AK009806 AK011038 AK011046 AK011099 AK019252 AK019274 AK019320 AK019343 AK019350 AK019355 BC031384 BC086880 BC089555 BC094407 Y17223
GenPept AAH31384 AAH86880 AAH89555 AAH94407 BAB23862 BAB23952 BAB23987 BAB25401 BAB25408 BAB25420 BAB25451 BAB25516 BAB25558 BAB25600 BAB26305 BAB26308 BAB26310 BAB26392 BAB26514 BAB27351 BAB27357 BAB27396 BAB31628 BAB31641 BAB31664 BAB31670 BAB31672 BAB31676 CAA76699

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca