Tag | Content |
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CPLM ID | CPLM-025348 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ATP synthase subunit gamma |
Protein Synonyms/Alias | |
Gene Name | Atp5c1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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29 | VRNMATLKDITRRLK | ubiquitination | [1] | 55 | MKMVAAAKYARAERE | ubiquitination | [1] | 154 | DQFLVSFKDVGRKPP | ubiquitination | [1] | 262 | TAMDNASKNASDMID | ubiquitination | [1] | 270 | NASDMIDKLTLTFNR | ubiquitination | [1] |
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Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). |
Sequence Annotation | |
Keyword | ATP synthesis; CF(1); Hydrogen ion transport; Ion transport; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 298 AA |
Protein Sequence | MFSRASVVGL SACAVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE 60 RELKPARVYG TGSLALYEKA DIKAPEDKKK HLIIGVSSDR GLCGAIHSSV AKQMKNEVAA 120 LTAAGKEVMI VGVGEKIKGI LYRTHSDQFL VSFKDVGRKP PTFGDASVIA LELLNSGYEF 180 DEGSIIFNQF KSVISYKTEE KPIFSLNTIA TAETMSIYDD IDADVLQNYQ EYNLANLIYY 240 SLKESTTSEQ SARMTAMDNA SKNASDMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD 298 |
Gene Ontology | GO:0005743; C:mitochondrial inner membrane; IDA:MGI. GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IEA:Compara. GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW. GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro. GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |