Reviewed, UniProtKB/Swiss-Prot P48047 (ATPO_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
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
Gene Ontology (GO)
Biological process	ATP catabolic process Inferred from direct assay. Source: UniProtKB mitochondrial ATP synthesis coupled proton transport Inferred from mutant phenotype. Source: UniProtKB
Cellular component	plasma membrane Inferred from direct assay. Source: UniProtKB proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: InterPro
Molecular function	drug binding Inferred from direct assay. Source: UniProtKB hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
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.10
	Modified residue	60	1	N6-acetyllysine Ref.10
	Modified residue	70	1	N6-acetyllysine Ref.10
	Modified residue	158	1	N6-acetyllysine By similarity
	Modified residue	162	1	N6-acetyllysine Ref.10
	Modified residue	172	1	N6-acetyllysine Ref.10
	Modified residue	176	1	N6-acetyllysine By similarity
	Modified residue	192	1	N6-acetyllysine Ref.10
Natural variations
	Natural variant	98	1	K → R: dbSNP rs4842. Ref.2 Ref.5		VAR_011930

Sequences

	Sequence		Length	Mass (Da)
	P48047-1 [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: 7490082] [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: 14702039] [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: 15489334] [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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 24-40. Tissue: Platelet.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-60; LYS-70; LYS-162; LYS-172 AND LYS-192, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Hs.409140
3D structure databases
SMR	P48047. Positions 24-143.
ModBase	Search...
Protein-protein interaction databases
IntAct	P48047. 11 interactions.
STRING	P48047.
PTM databases
PhosphoSite	P48047.
2-D gel databases
OGP	P48047.
Proteomic databases
PeptideAtlas	P48047.
PRIDE	P48047.
Genome annotation databases
Ensembl	ENST00000290299; ENSP00000290299; ENSG00000241837; Homo sapiens. [Genome view]
GeneID	539.
KEGG	hsa:539.
UCSC	uc002ytl.1. human.
Organism-specific databases
CTD	539.
GeneCards	GC21M034197.
H-InvDB	HIX0016083.
HGNC	HGNC:850. ATP5O.
HPA	CAB016209.
MIM	600828. gene.
PharmGKB	PA25144.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P48047.
HOVERGEN	P48047.
OMA	FIAICGE
Enzyme and pathway databases
Reactome	REACT_1505. Integration of energy metabolism. REACT_15380. Diabetes pathways. REACT_1698. Metablism of nucleotides.
Gene expression databases
ArrayExpress	P48047.
Bgee	P48047.
CleanEx	HS_ATP5O.
Genevestigator	P48047.
GermOnline	ENSG00000159186. Homo sapiens.
Family and domain databases
InterPro	IPR000711. ATPase_F1-cplx_OSCP/dsu. IPR020781. ATPase_F1-cplx_OSCP/dsu_CS. [Graphical view]
Gene3D	G3DSA:1.10.520.20. ATPase_F1_OSCP/d. 1 hit.
PANTHER	PTHR11910. ATPase_F1_OSCP/d. 1 hit.
Pfam	PF00213. OSCP. 1 hit. [Graphical view]
PRINTS	PR00125. ATPASEDELTA.
TIGRFAMs	TIGR01145. ATP_synt_delta. 1 hit.
PROSITE	PS00389. ATPASE_DELTA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	November 24, 2009
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.