Tag | Content |
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CPLM ID | CPLM-000130 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ATP synthase subunit gamma, mitochondrial |
Protein Synonyms/Alias | F-ATPase gamma subunit |
Gene Name | ATPsyn-gamma |
Gene Synonyms/Alias | CG7610 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
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56 | MKMVSAAKYARAERD | acetylation | [1] | 88 | TEIQPDEKAEPKKLL | acetylation | [1] | 128 | AQDEANTKVFCVGDK | acetylation | [1] |
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Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
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. |
Sequence Annotation | |
Keyword | ATP synthesis; CF(1); Complete proteome; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transit peptide; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 297 AA |
Protein Sequence | MMMQRTQLLL PLAMEATMLA QQQRGMATLK MISIRLKSVK NIQKITQSMK MVSAAKYARA 60 ERDLKAARPY GIGAQQFFEK TEIQPDEKAE PKKLLIAVTS DRGLCGAVHT GVARLIRGEL 120 AQDEANTKVF CVGDKSRAIL SRLYGKNILM VANEVGRLPP TFLDASKIAN EVLQTGYDYT 180 EGKIVYNRFK SVVSYQCSTL PIFSGSTVEK SEKLAVYDSL DSDVVKSYLE FSLASLIFYT 240 MKEGACSEQS SRMTAMDNAS KNAGEMIDKL TLTFNRTRQA VITRELIEII SGAAALT 297 |
Gene Ontology | GO:0005811; C:lipid particle; IDA:FlyBase. GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. 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. GO:0006911; P:phagocytosis, engulfment; IMP:FlyBase. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |