Q9CQQ7 (AT5F1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 91.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: ATP synthase subunit b, mitochondrial Short name=ATPase subunit b | ||
| Gene names |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 256 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| 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. Part of the complex F0 domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements. |
| Subunit structure | 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. CF0 has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the eukaryotic ATPase B chain family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Hydrogen ion transport Ion transport Transport |
| Cellular component | CF(0) Membrane Mitochondrion Mitochondrion inner membrane |
| Domain | Transit peptide |
| PTM | Acetylation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | ATP synthesis coupled proton transport Inferred from Biological aspect of Ancestor. Source: RefGenome |
| Cellular_component | mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Inferred from Biological aspect of Ancestor. Source: RefGenome |
| Molecular_function | proton-transporting ATP synthase activity, rotational mechanism Inferred from Biological aspect of Ancestor. Source: RefGenome |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 42 | 42 | Mitochondrion By similarity | ||||||
| Chain | 43 – 256 | 214 | ATP synthase subunit b, mitochondrial | PRO_0000002514 | |||||
Amino acid modifications | |||||||||
| Modified residue | 115 | 1 | N6-acetyllysine Ref.3 | ||||||
| Modified residue | 131 | 1 | N6-acetyllysine Ref.3 | ||||||
| Modified residue | 162 | 1 | N6-acetyllysine Ref.3 | ||||||
| Modified residue | 188 | 1 | N6-acetyllysine Ref.3 | ||||||
| Modified residue | 221 | 1 | N6-acetyllysine Ref.3 | ||||||
| Modified residue | 225 | 1 | N6-acetyllysine Ref.3 | ||||||
| Modified residue | 233 | 1 | N6-acetyllysine Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.  Hayashizaki Y.Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Brain and Embryo. |
| [2] | Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 71-90; 115-139; 145-154; 164-183 AND 195-221, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain. |
| [3] | "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-115; LYS-131; LYS-162; LYS-188; LYS-221; LYS-225 AND LYS-233, MASS SPECTROMETRY. Tissue: Liver. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK002960 mRNA. Translation: BAB22481.1. AK011312 mRNA. Translation: BAB27538.1. |
| IPI | IPI00341282. |
| RefSeq | NP_033855.2. NM_009725.3. |
| UniGene | Mm.251152. |
3D structure databases | |
| ProteinModelPortal | Q9CQQ7. |
| SMR | Q9CQQ7. Positions 121-249. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9CQQ7. 1 interaction. |
| STRING | 10090.ENSMUSP00000088168. |
PTM databases | |
| PhosphoSite | Q9CQQ7. |
Proteomic databases | |
| PaxDb | Q9CQQ7. |
| PRIDE | Q9CQQ7. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000118209; ENSMUSP00000113022; ENSMUSG00000000563. |
| GeneID | 11950. |
| KEGG | mmu:11950. |
Organism-specific databases | |
| CTD | 515. |
| MGI | MGI:1100495. Atp5f1. |
Phylogenomic databases | |
| eggNOG | NOG245616. |
| GeneTree | ENSGT00390000001958. |
| HOGENOM | HOG000007163. |
| HOVERGEN | HBG050604. |
| InParanoid | Q9CQQ7. |
| KO | K02127. |
| OMA | VINHETF. |
| OrthoDB | EOG4K3KXB. |
Gene expression databases | |
| ArrayExpress | Q9CQQ7. |
| Bgee | Q9CQQ7. |
| Genevestigator | Q9CQQ7. |
| GermOnline | ENSMUSG00000000563. Mus musculus. |
Family and domain databases | |
| InterPro | IPR008688. ATPase_B_chain/sub_B/MI25. IPR013837. ATPase_F0_sub_B/B_chain. [Graphical view] |
| PANTHER | PTHR12733. PTHR12733. 1 hit. |
| Pfam | PF05405. Mt_ATP-synt_B. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | ATP5F1. mouse. |
| NextBio | 280069. |
| SOURCE | Search... |
Entry information
| Entry name | AT5F1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9CQQ7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |