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P48047 (ATPO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:ATPO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 at Lys-162 decreases ATP production. Deacetylated by SIRT3. Ref.11

Sequence similarities

Belongs to the ATPase delta chain family.

Ontologies

Keywords
   Biological processATP synthesis
Hydrogen ion transport
Ion transport
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Non-traceable author statement PubMed 17851741. Source: UniProtKB

ATP catabolic process

Inferred from direct assay PubMed 12110673. Source: UniProtKB

cellular metabolic process

Traceable author statement. Source: Reactome

mitochondrial ATP synthesis coupled proton transport

Inferred from mutant phenotype PubMed 15850986. Source: UniProtKB

proton transport

Non-traceable author statement PubMed 17851741. Source: UniProtKB

respiratory electron transport chain

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Traceable author statement. Source: Reactome

mitochondrial proton-transporting ATP synthase complex

Inferred from direct assay PubMed 12110673. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 12110673PubMed 17851741. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

plasma membrane

Inferred from direct assay PubMed 17851741. Source: UniProtKB

   Molecular_functiondrug binding

Inferred from direct assay PubMed 15850986. Source: UniProtKB

proton-transporting ATP synthase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

transmembrane transporter activity

Inferred by curator PubMed 12110673. Source: UniProtKB

transporter activity

Non-traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion Ref.8
Chain24 – 213190ATP synthase subunit O, mitochondrial HAMAP-Rule MF_01416
PRO_0000002646

Amino acid modifications

Modified residue541N6-acetyllysine Ref.9
Modified residue601N6-acetyllysine By similarity
Modified residue701N6-acetyllysine By similarity
Modified residue731N6-acetyllysine By similarity
Modified residue901N6-succinyllysine By similarity
Modified residue1581N6-acetyllysine; alternate By similarity
Modified residue1581N6-succinyllysine; alternate By similarity
Modified residue1621N6-acetyllysine; alternate Ref.9 Ref.11
Modified residue1621N6-succinyllysine; alternate By similarity
Modified residue1721N6-acetyllysine Ref.9
Modified residue1761N6-acetyllysine By similarity
Modified residue1921N6-acetyllysine Ref.9
Modified residue1991N6-succinyllysine By similarity

Natural variations

Natural variant981K → R. Ref.2 Ref.5
Corresponds to variant rs4842 [ dbSNP | Ensembl ].
VAR_011930

Experimental info

Mutagenesis1621K → R: Increased ATP levels. Ref.11

Sequences

Sequence LengthMass (Da)Tools
P48047 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 311F53576A31FC93

FASTA21323,277
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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].
[11]"SIRT3 deacetylates ATP synthase F1 complex proteins in response to nutrient and exercise-induced stress."
Vassilopoulos A., Pennington D.J., Andresson T., Rees D., Fearnley I., Ham A., Yan Y., Flynn C.R., Jones K., Kim H.S., Deng C., Walker J., Gius D.
Antioxid. Redox Signal. 0:0-0(2013)
Cited for: ACETYLATION AT LYS-162, DEACETYLATION BY SIRT3, MUTAGENESIS OF LYS-162.
+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.
CCDSCCDS13634.1.
RefSeqNP_001688.1. NM_001697.2.
UniGeneHs.409140.

3D structure databases

ProteinModelPortalP48047.
SMRP48047. Positions 24-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107021. 22 interactions.
IntActP48047. 12 interactions.
MINTMINT-5002594.
STRING9606.ENSP00000290299.

PTM databases

PhosphoSiteP48047.

Polymorphism databases

DMDM1352049.

2D gel databases

OGPP48047.
UCD-2DPAGEP48047.

Proteomic databases

MaxQBP48047.
PaxDbP48047.
PeptideAtlasP48047.
PRIDEP48047.

Protocols and materials databases

DNASU539.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290299; ENSP00000290299; ENSG00000241837.
GeneID539.
KEGGhsa:539.
UCSCuc002ytl.3. human.

Organism-specific databases

CTD539.
GeneCardsGC21M035275.
H-InvDBHIX0158705.
HGNCHGNC:850. ATP5O.
HPACAB016209.
HPA041394.
MIM600828. gene.
neXtProtNX_P48047.
PharmGKBPA25144.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0712.
HOGENOMHOG000075825.
HOVERGENHBG004309.
InParanoidP48047.
KOK02137.
OMATKNFLAV.
PhylomeDBP48047.
TreeFamTF106241.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP48047.
BgeeP48047.
CleanExHS_ATP5O.
GenevestigatorP48047.

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. human.
GeneWikiATP5O.
GenomeRNAi539.
NextBio2235.
PROP48047.
SOURCESearch...

Entry information

Entry nameATPO_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM