Tag | Content |
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CPLM ID | CPLM-040510 |
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 | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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5 | ***MATLKDITRRLK | acetylation | [1] | 12 | KDITRRLKSIKNIQK | acetylation | [1] | 15 | TRRLKSIKNIQKITK | acetylation | [1] | 19 | KSIKNIQKITKSMKM | acetylation | [1] | 25 | QKITKSMKMVAAAKY | acetylation | [1] | 31 | MKMVAAAKYARAERE | acetylation | [1] | 59 | LYEKAEIKGPEDKKK | acetylation | [1] | 91 | SSVAKQMKNDMAALT | acetylation | [1] | 102 | AALTAAGKEVMIVGI | acetylation | [1] | 114 | VGIGEKIKSILYRTH | acetylation | [1] | 130 | DQFLVSFKDVGRKPP | acetylation | [1] | 173 | FKSVISYKTEEKPIF | acetylation | [1] | 238 | TAMDNASKNASDMID | acetylation | [1] | 246 | NASDMIDKLTLTFNR | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
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); Complete proteome; Hydrogen ion transport; Ion transport; Reference proteome; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 274 AA |
Protein Sequence | MATLKDITRR LKSIKNIQKI TKSMKMVAAA KYARAERELK PARVYGTGSL ALYEKAEIKG 60 PEDKKKHLII GVSSDRGLCG AIHSSVAKQM KNDMAALTAA GKEVMIVGIG EKIKSILYRT 120 HSDQFLVSFK DVGRKPPTFG DASVIALELL NSGYEFDEGS IIFNQFKSVI SYKTEEKPIF 180 SFSTVVAAEN MSIYDDIDAD VLQNYQEYNL ANIIYYSLKE STTSEQSARM TAMDNASKNA 240 SDMIDKLTLT FNRTRQAVIT KELIEIISGA AALD 274 |
Gene Ontology | 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 | |