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Q9DB20 (ATPO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit O, mitochondrial
Alternative name(s):
Oligomycin sensitivity conferral protein
Short name=OSCP
Gene names
Name:Atp5o
Synonyms:D12Wsu28e
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitochondrial membrane ATP synthase (F1F0 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, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha3beta3 subcomplex and subunit a/ATP6 static relative to the rotary elements. HAMAP-Rule MF_01416

Subunit structure

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 By similarity.

Subcellular location

Mitochondrion By similarity. Mitochondrion inner membrane By similarity HAMAP-Rule MF_01416.

Post-translational modification

Acetylation of Lys-70 and Lys-158 is observed in liver mitochondria from fasted mice but not from fed mice. HAMAP-Rule MF_01416

Acetylation at Lys-162 decreases ATP production. Deacetylated by SIRT3 By similarity. HAMAP-Rule MF_01416

Sequence similarities

Belongs to the ATPase delta chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion By similarity
Chain24 – 213190ATP synthase subunit O, mitochondrial HAMAP-Rule MF_01416
PRO_0000002647

Amino acid modifications

Modified residue541N6-acetyllysine Ref.5
Modified residue601N6-acetyllysine Ref.5
Modified residue701N6-acetyllysine Ref.5
Modified residue731N6-acetyllysine Ref.5
Modified residue901N6-succinyllysine Ref.4
Modified residue1001N6-acetyllysine; alternate Ref.5
Modified residue1001N6-succinyllysine; alternate Ref.4
Modified residue1581N6-acetyllysine; alternate Ref.5
Modified residue1581N6-succinyllysine; alternate Ref.4
Modified residue1621N6-acetyllysine; alternate Ref.5
Modified residue1621N6-succinyllysine; alternate Ref.4
Modified residue1721N6-acetyllysine Ref.5
Modified residue1761N6-acetyllysine Ref.5
Modified residue1921N6-acetyllysine By similarity
Modified residue1991N6-succinyllysine Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9DB20 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1B0DAD4CCFCCB086

FASTA21323,364
        10         20         30         40         50         60 
MAAPAASGLS RQVRSFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS KEKKLDQVEK 

        70         80         90        100        110        120 
ELLRVGQLLK DPKVSLAVLN PYIKRTVKVK SLNDITKREK FSPLTANLMN LLAENGRLGN 

       130        140        150        160        170        180 
TQGIISAFST IMSVHRGEVP CTVTTASPLD DAVLSELKTV LKSFLSPNQI LKLEIKTDPS 

       190        200        210 
IMGGMIVRIG EKYVDMSAKS KIQKLSKAMR EML 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[3]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 27-51; 65-84; 99-158; 163-172 AND 177-188, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-90; LYS-100; LYS-158; LYS-162 AND LYS-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-60; LYS-70; LYS-73; LYS-100; LYS-158; LYS-162; LYS-172 AND LYS-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK005309 mRNA. Translation: BAB23945.1.
BC012241 mRNA. Translation: AAH12241.1.
RefSeqNP_613063.1. NM_138597.2.
XP_006543820.1. XM_006543757.1.
UniGeneMm.41.

3D structure databases

ProteinModelPortalQ9DB20.
SMRQ9DB20. Positions 24-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205752. 1 interaction.
IntActQ9DB20. 6 interactions.
MINTMINT-1840730.

PTM databases

PhosphoSiteQ9DB20.

Proteomic databases

PaxDbQ9DB20.
PRIDEQ9DB20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023677; ENSMUSP00000023677; ENSMUSG00000022956.
GeneID102641678.
28080.
KEGGmmu:100047429.
mmu:28080.
UCSCuc007zys.1. mouse.

Organism-specific databases

CTD539.
MGIMGI:106341. Atp5o.

Phylogenomic databases

eggNOGCOG0712.
GeneTreeENSGT00390000015060.
HOGENOMHOG000075825.
HOVERGENHBG004309.
InParanoidQ9DB20.
KOK02137.
OMAAEVTSAH.
PhylomeDBQ9DB20.
TreeFamTF106241.

Gene expression databases

ArrayExpressQ9DB20.
BgeeQ9DB20.
GenevestigatorQ9DB20.

Family and domain databases

Gene3D1.10.520.20. 1 hit.
HAMAPMF_01416. ATP_synth_delta_bact.
InterProIPR000711. ATPase_F1-cplx_OSCP/dsu.
IPR020781. ATPase_F1-cplx_OSCP/dsu_CS.
IPR026015. ATPase_OSCP/delta_N.
[Graphical view]
PANTHERPTHR11910. PTHR11910. 1 hit.
PfamPF00213. OSCP. 1 hit.
[Graphical view]
PRINTSPR00125. ATPASEDELTA.
SUPFAMSSF47928. SSF47928. 1 hit.
TIGRFAMsTIGR01145. ATP_synt_delta. 1 hit.
PROSITEPS00389. ATPASE_DELTA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP5O. mouse.
NextBio306620.
PROQ9DB20.
SOURCESearch...

Entry information

Entry nameATPO_MOUSE
AccessionPrimary (citable) accession number: Q9DB20
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot