Tag | Content |
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CPLM ID | CPLM-004781 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ATP synthase subunit b, mitochondrial |
Protein Synonyms/Alias | ATPase subunit b |
Gene Name | Atp5f1 |
Gene Synonyms/Alias | Atp5f |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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126 | SIGEFIDKLNEEKIA | acetylation | [1] | 131 | IDKLNEEKIAQLEEI | acetylation | [1] | 139 | IAQLEEIKQSSMKQI | acetylation | [1] | 144 | EIKQSSMKQIQDAIN | acetylation | [1] | 154 | QDAINREKAQQALVQ | acetylation | [1] | 162 | AQQALVQKRHYLFDV | acetylation | [1] | 188 | TYRERLHKAYKEVKN | acetylation | [1] | 194 | HKAYKEVKNRLDYHI | acetylation | [1] | 210 | VQDMMRRKEGEHMIN | acetylation | [1] | 221 | HMINWVEKHVIQSIS | acetylation | [1] | 233 | SISAQQEKETIAKCI | acetylation | [1] | 238 | QEKETIAKCIGDLKM | acetylation | [1] | 244 | AKCIGDLKMLAKKAQ | 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(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. |
Sequence Annotation | MOD_RES 115 115 N6-acetyllysine (By similarity). MOD_RES 131 131 N6-acetyllysine (By similarity). MOD_RES 162 162 N6-acetyllysine (By similarity). MOD_RES 188 188 N6-acetyllysine (By similarity). MOD_RES 221 221 N6-acetyllysine (By similarity). MOD_RES 233 233 N6-acetyllysine (By similarity). |
Keyword | Acetylation; CF(0); 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 | 256 AA |
Protein Sequence | MLSRVVLSAA ATAAPCLKNA AVLGPGVLQA TRVFHTGQPR LAPLPPLPEY GGKVRLGLIP 60 EEFFQFLYPK TGVTGPYVLG TGLSLYFLSK EIYVITPETF STISVVGLIV YVIKKYGASI 120 GEFIDKLNEE KIAQLEEIKQ SSMKQIQDAI NREKAQQALV QKRHYLFDVQ RNNIALALEV 180 TYRERLHKAY KEVKNRLDYH ISVQDMMRRK EGEHMINWVE KHVIQSISAQ QEKETIAKCI 240 GDLKMLAKKA QAQPIM 256 |
Gene Ontology | GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IDA:RGD. GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:RefGenome. GO:0015986; P:ATP synthesis coupled proton transport; IBA:RefGenome. |
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