Q9DB20 (ATPO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit O, mitochondrial

Alternative name(s):
Oligomycin sensitivity conferral protein
Short name=OSCP

Gene names

Name:	Atp5o
Synonyms:	D12Wsu28e

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.
Post-translational modification	Acetylation of Lys-70 and Lys-158 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	Belongs to the ATPase delta chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial ATP synthesis coupled proton transport Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial proton-transporting ATP synthase complex Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	drug binding Inferred from electronic annotation. Source: Compara proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro steroid binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 23	23	Mitochondrion By similarity
	Chain	24 – 213	190	ATP synthase subunit O, mitochondrial		PRO_0000002647
Amino acid modifications
	Modified residue	54	1	N6-acetyllysine By similarity
	Modified residue	60	1	N6-acetyllysine Ref.4
	Modified residue	70	1	N6-acetyllysine Ref.4
	Modified residue	158	1	N6-acetyllysine Ref.4
	Modified residue	162	1	N6-acetyllysine Ref.4
	Modified residue	172	1	N6-acetyllysine Ref.4
	Modified residue	176	1	N6-acetyllysine Ref.4
	Modified residue	192	1	N6-acetyllysine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9DB20 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 1B0DAD4CCFCCB086	FASTA	213	23,364
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[4]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-70; LYS-158; LYS-162; LYS-172; LYS-176 AND LYS-192, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK005309 mRNA. Translation: BAB23945.1. BC012241 mRNA. Translation: AAH12241.1.
IPI	IPI00118986.
RefSeq	NP_613063.1. NM_138597.2. XP_001478145.1. XM_001478095.4.
UniGene	Mm.41.
3D structure databases
ProteinModelPortal	Q9DB20.
SMR	Q9DB20. Positions 24-212.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9DB20. 1 interaction.
PTM databases
PhosphoSite	Q9DB20.
Proteomic databases
PaxDb	Q9DB20.
PRIDE	Q9DB20.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023677; ENSMUSP00000023677; ENSMUSG00000022956.
GeneID	100047429. 28080.
KEGG	mmu:100047429. mmu:28080.
UCSC	uc007zys.1. mouse.
Organism-specific databases
CTD	539.
MGI	MGI:106341. Atp5o.
Phylogenomic databases
eggNOG	COG0712.
GeneTree	ENSGT00390000015060.
HOGENOM	HOG000075825.
HOVERGEN	HBG004309.
InParanoid	Q9DB20.
KO	K02137.
OMA	ARNRRLF.
Gene expression databases
ArrayExpress	Q9DB20.
Bgee	Q9DB20.
Genevestigator	Q9DB20.
GermOnline	ENSMUSG00000022956. Mus musculus.
Family and domain databases
Gene3D	1.10.520.20. 1 hit.
InterPro	IPR000711. ATPase_F1-cplx_OSCP/dsu. IPR020781. ATPase_F1-cplx_OSCP/dsu_CS. IPR026015. ATPase_OSCP/delta_N. [Graphical view]
PANTHER	PTHR11910. PTHR11910. 1 hit.
Pfam	PF00213. OSCP. 1 hit. [Graphical view]
PRINTS	PR00125. ATPASEDELTA.
SUPFAM	SSF47928. ATPsynt_OSCP. 1 hit.
TIGRFAMs	TIGR01145. ATP_synt_delta. 1 hit.
PROSITE	PS00389. ATPASE_DELTA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ATP5O. mouse.
NextBio	306620.
SOURCE	Search...

Entry information

Entry name

ATPO_MOUSE

Accession

Primary (citable) accession number: Q9DB20

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program