Tag | Content |
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CPLM ID | CPLM-011440 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ATP synthase subunit O, mitochondrial |
Protein Synonyms/Alias | Oligomycin sensitivity conferral protein; OSCP; Sperm flagella protein 4 |
Gene Name | Atp5o |
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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53 | YSAASKQKRLDQVEK | acetylation | [1] | 60 | KRLDQVEKELLRVGQ | acetylation | [1] | 70 | LRVGQLLKDPKVSLA | acetylation | [1] | 73 | GQLLKDPKVSLAVLN | acetylation | [1] | 84 | AVLNPYIKRSIKVKS | acetylation | [1] | 93 | SIKVKSLKDITTKEK | acetylation | [1] | 98 | SLKDITTKEKFSPLT | acetylation | [1] | 100 | KDITTKEKFSPLTAN | acetylation | [1] | 176 | QILNLEVKTDPSIMG | acetylation | [1] | 192 | MIVRIGEKYVDMSAK | acetylation | [1] | 199 | KYVDMSAKSKIQKLS | acetylation | [1] | 207 | SKIQKLSKAMRDLL* | 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 60 60 N6-acetyllysine (By similarity). MOD_RES 70 70 N6-acetyllysine (By similarity). MOD_RES 158 158 N6-acetyllysine (By similarity). MOD_RES 176 176 N6-acetyllysine (By similarity). MOD_RES 192 192 N6-acetyllysine (By similarity). |
Keyword | Acetylation; ATP synthesis; Complete proteome; Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transit peptide; Transport. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 213 AA |
Protein Sequence | MAAPATSVLS RQVRSFSTSV VRPFSKLVRP PVQVYGIEGR YATALYSAAS KQKRLDQVEK 60 ELLRVGQLLK DPKVSLAVLN PYIKRSIKVK SLKDITTKEK FSPLTANLMN LLAENGRLGN 120 TQGVISAFST IMSVHRGEVP CTVTTAFPLD EAVLSELKTV LNSFLSKGQI LNLEVKTDPS 180 IMGGMIVRIG EKYVDMSAKS KIQKLSKAMR DLL 213 |
Gene Ontology | GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IDA:RGD. GO:0005886; C:plasma membrane; IEA:Compara. GO:0008144; F:drug binding; IEA:Compara. GO:0032403; F:protein complex binding; IDA:RGD. GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro. GO:0005496; F:steroid binding; IDA:RGD. GO:0046034; P:ATP metabolic process; IDA:RGD. GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IEA:Compara. |
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PRINTS | |