P48047 (ATPO_HUMAN) 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:	ATPO

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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.
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
Coding sequence diversity	Polymorphism
Domain	Transit peptide
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay PubMed 12110673. Source: UniProtKB mitochondrial ATP synthesis coupled proton transport Inferred from mutant phenotype PubMed 15850986. Source: UniProtKB respiratory electron transport chain Traceable author statement. Source: Reactome
Cellular_component	mitochondrial proton-transporting ATP synthase complex Inferred from direct assay PubMed 12110673. Source: UniProtKB mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: Compara plasma membrane Inferred from direct assay PubMed 17851741. Source: UniProtKB
Molecular_function	drug binding Inferred from direct assay PubMed 15850986. Source: UniProtKB proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro steroid binding Inferred from electronic annotation. Source: Compara transmembrane transporter activity Inferred by curator PubMed 12110673. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 23	23	Mitochondrion Ref.8
	Chain	24 – 213	190	ATP synthase subunit O, mitochondrial		PRO_0000002646
Amino acid modifications
	Modified residue	54	1	N6-acetyllysine Ref.9
	Modified residue	60	1	N6-acetyllysine By similarity
	Modified residue	70	1	N6-acetyllysine By similarity
	Modified residue	158	1	N6-acetyllysine By similarity
	Modified residue	162	1	N6-acetyllysine Ref.9
	Modified residue	172	1	N6-acetyllysine Ref.9
	Modified residue	176	1	N6-acetyllysine By similarity
	Modified residue	192	1	N6-acetyllysine Ref.9
Natural variations
	Natural variant	98	1	K → R. Ref.2 Ref.5 Corresponds to variant rs4842 [ dbSNP | Ensembl ].		VAR_011930

Sequences

	Sequence		Length	Mass (Da)
	P48047 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 311F53576A31FC93	FASTA	213	23,277
	10 20 30 40 50 60 MAAPAVSGLS RQVRCFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS KQNKLEQVEK 70 80 90 100 110 120 ELLRVAQILK EPKVAASVLN PYVKRSIKVK SLNDITAKER FSPLTTNLIN LLAENGRLSN 130 140 150 160 170 180 TQGVVSAFST MMSVHRGEVP CTVTSASPLE EATLSELKTV LKSFLSQGQV LKLEAKTDPS 190 200 210 ILGGMIVRIG EKYVDMSVKT KIQKLGRAMR EIV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the cDNA for the human ATP synthase OSCP subunit (ATP5O) by exon trapping and mapping to chromosome 21q22.1-q22.2." Chen H.M., Morris M.A., Rossier C., Blouin J.-L., Antonarakis S.E. Genomics 28:470-476(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain and Muscle.
[2]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-98.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-98. Tissue: Heart.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Brain.
[8]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-40. Tissue: Platelet.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-162; LYS-172 AND LYS-192, MASS SPECTROMETRY.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X83218 mRNA. Translation: CAA58219.1. BT019836 mRNA. Translation: AAV38639.1. CR456822 mRNA. Translation: CAG33103.1. AK222962 mRNA. Translation: BAD96682.1. AK311796 mRNA. Translation: BAG34739.1. CH471079 Genomic DNA. Translation: EAX09802.1. BC021233 mRNA. Translation: AAH21233.1. BC022865 mRNA. Translation: AAH22865.1.
IPI	IPI00007611.
RefSeq	NP_001688.1. NM_001697.2.
UniGene	Hs.409140.
3D structure databases
ProteinModelPortal	P48047.
ModBase	Search...
Protein-protein interaction databases
IntAct	P48047. 9 interactions.
MINT	MINT-5002594.
STRING	9606.ENSP00000290299.
PTM databases
PhosphoSite	P48047.
Polymorphism databases
DMDM	1352049.
2D gel databases
OGP	P48047.
UCD-2DPAGE	P48047.
Proteomic databases
PaxDb	P48047.
PeptideAtlas	P48047.
PRIDE	P48047.
Protocols and materials databases
DNASU	539.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000290299; ENSP00000290299; ENSG00000241837.
GeneID	539.
KEGG	hsa:539.
UCSC	uc002ytl.3. human.
Organism-specific databases
CTD	539.
GeneCards	GC21M035275.
H-InvDB	HIX0158705.
HGNC	HGNC:850. ATP5O.
HPA	CAB016209.
MIM	600828. gene.
neXtProt	NX_P48047.
PharmGKB	PA25144.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0712.
HOGENOM	HOG000075825.
HOVERGEN	HBG004309.
InParanoid	P48047.
KO	K02137.
OMA	ARNRRLF.
OrthoDB	EOG4D7Z6N.
PhylomeDB	P48047.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	P48047.
Bgee	P48047.
CleanEx	HS_ATP5O.
Genevestigator	P48047.
GermOnline	ENSG00000159186. Homo sapiens.
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. human.
GenomeRNAi	539.
NextBio	2235.
SOURCE	Search...

Entry information

Entry name

ATPO_HUMAN

Accession

Primary (citable) accession number: P48047
Secondary accession number(s): B2R4E2, Q5U042, Q6IBI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.