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Protein

ATP synthase subunit O, mitochondrial

Gene

ATP5O

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-163210. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit O, mitochondrial
Alternative name(s):
Oligomycin sensitivity conferral protein
Short name:
OSCP
Gene namesi
Name:ATP5O
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • myelin sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Protein family/group databases

Allergomei1548. Bos d OSCP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323Mitochondrion1 PublicationAdd
BLAST
Chaini24 – 213190ATP synthase subunit O, mitochondrialPRO_0000002645Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-acetyllysineBy similarity
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei70 – 701N6-acetyllysineBy similarity
Modified residuei73 – 731N6-acetyllysineBy similarity
Modified residuei90 – 901N6-succinyllysineBy similarity
Modified residuei100 – 1001N6-acetyllysine; alternateBy similarity
Modified residuei100 – 1001N6-succinyllysine; alternateBy similarity
Modified residuei158 – 1581N6-acetyllysine; alternateBy similarity
Modified residuei158 – 1581N6-succinyllysine; alternateBy similarity
Modified residuei162 – 1621N6-acetyllysine; alternateBy similarity
Modified residuei162 – 1621N6-succinyllysine; alternateBy similarity
Modified residuei172 – 1721N6-acetyllysineBy similarity
Modified residuei176 – 1761N6-acetyllysineBy similarity
Modified residuei192 – 1921N6-acetyllysineBy similarity
Modified residuei199 – 1991N6-succinyllysineBy similarity

Post-translational modificationi

Acetylation at Lys-162 decreases ATP production. Deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP13621.
PeptideAtlasiP13621.
PRIDEiP13621.

Interactioni

Subunit structurei

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 MP68.1 Publication

Protein-protein interaction databases

DIPiDIP-39019N.
IntActiP13621. 2 interactions.
MINTiMINT-5006978.
STRINGi9913.ENSBTAP00000024326.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 383Combined sources
Helixi42 – 487Combined sources
Turni49 – 535Combined sources
Helixi55 – 6814Combined sources
Beta strandi69 – 713Combined sources
Helixi75 – 784Combined sources
Turni81 – 855Combined sources
Turni90 – 934Combined sources
Helixi94 – 974Combined sources
Turni98 – 1003Combined sources
Beta strandi103 – 1064Combined sources
Helixi107 – 1148Combined sources
Helixi118 – 1203Combined sources
Helixi121 – 13212Combined sources
Turni133 – 1353Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi152 – 1543Combined sources
Turni155 – 1628Combined sources
Turni165 – 1673Combined sources
Turni194 – 20512Combined sources
Turni207 – 2115Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BO5NMR-A24-143[»]
2JMXNMR-A24-143[»]
2WSSX-ray3.20S/W24-213[»]
4B2Qelectron microscopy37.00W/w24-143[»]
5ARAelectron microscopy6.70S24-213[»]
5AREelectron microscopy7.40S24-213[»]
5ARHelectron microscopy7.20S24-213[»]
5ARIelectron microscopy7.40S24-213[»]
5FIJelectron microscopy7.40S24-213[»]
5FIKelectron microscopy6.40S24-213[»]
5FILelectron microscopy7.10S24-213[»]
ProteinModelPortaliP13621.
SMRiP13621. Positions 24-143.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13621.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase delta chain family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1662. Eukaryota.
COG0712. LUCA.
GeneTreeiENSGT00390000015060.
HOGENOMiHOG000075825.
HOVERGENiHBG004309.
InParanoidiP13621.
KOiK02137.
OMAiMNPHVKR.
OrthoDBiEOG7DZ8M3.
TreeFamiTF106241.

Family and domain databases

Gene3Di1.10.520.20. 1 hit.
HAMAPiMF_01416. ATP_synth_delta_bact.
InterProiIPR020781. ATPase_OSCP/d_CS.
IPR026015. ATPase_OSCP/delta_N.
IPR000711. ATPase_OSCP/dsu.
[Graphical view]
PANTHERiPTHR11910. PTHR11910. 1 hit.
PfamiPF00213. OSCP. 1 hit.
[Graphical view]
PRINTSiPR00125. ATPASEDELTA.
SUPFAMiSSF47928. SSF47928. 1 hit.
TIGRFAMsiTIGR01145. ATP_synt_delta. 1 hit.
PROSITEiPS00389. ATPASE_DELTA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13621-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALAVSGLS QQVRCFSTSV VRPFAKLVRP PVQIYGIEGR YATALYSAAS
60 70 80 90 100
KQNKLEQVEK ELLRVGQILK EPKMAASLLN PYVKRSVKVK SLSDMTAKEK
110 120 130 140 150
FSPLTSNLIN LLAENGRLTN TPAVISAFST MMSVHRGEVP CTVTTASALD
160 170 180 190 200
EATLTELKTV LKSFLSKGQV LKLEVKIDPS IMGGMIVRIG EKYVDMSAKT
210
KIQKLSRAMR EIL
Length:213
Mass (Da):23,320
Last modified:April 3, 2007 - v2
Checksum:iC769EC7B778069DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521A → T in AAA30676 (PubMed:2894843).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18753 mRNA. Translation: AAA30676.1.
BC102204 mRNA. Translation: AAI02205.1.
PIRiA27382.
RefSeqiNP_776669.1. NM_174244.1.
UniGeneiBt.49172.

Genome annotation databases

EnsembliENSBTAT00000024326; ENSBTAP00000024326; ENSBTAG00000018278.
GeneIDi281640.
KEGGibta:281640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18753 mRNA. Translation: AAA30676.1.
BC102204 mRNA. Translation: AAI02205.1.
PIRiA27382.
RefSeqiNP_776669.1. NM_174244.1.
UniGeneiBt.49172.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BO5NMR-A24-143[»]
2JMXNMR-A24-143[»]
2WSSX-ray3.20S/W24-213[»]
4B2Qelectron microscopy37.00W/w24-143[»]
5ARAelectron microscopy6.70S24-213[»]
5AREelectron microscopy7.40S24-213[»]
5ARHelectron microscopy7.20S24-213[»]
5ARIelectron microscopy7.40S24-213[»]
5FIJelectron microscopy7.40S24-213[»]
5FIKelectron microscopy6.40S24-213[»]
5FILelectron microscopy7.10S24-213[»]
ProteinModelPortaliP13621.
SMRiP13621. Positions 24-143.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-39019N.
IntActiP13621. 2 interactions.
MINTiMINT-5006978.
STRINGi9913.ENSBTAP00000024326.

Protein family/group databases

Allergomei1548. Bos d OSCP.

Proteomic databases

PaxDbiP13621.
PeptideAtlasiP13621.
PRIDEiP13621.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000024326; ENSBTAP00000024326; ENSBTAG00000018278.
GeneIDi281640.
KEGGibta:281640.

Organism-specific databases

CTDi539.

Phylogenomic databases

eggNOGiKOG1662. Eukaryota.
COG0712. LUCA.
GeneTreeiENSGT00390000015060.
HOGENOMiHOG000075825.
HOVERGENiHBG004309.
InParanoidiP13621.
KOiK02137.
OMAiMNPHVKR.
OrthoDBiEOG7DZ8M3.
TreeFamiTF106241.

Enzyme and pathway databases

ReactomeiR-BTA-163210. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

EvolutionaryTraceiP13621.

Family and domain databases

Gene3Di1.10.520.20. 1 hit.
HAMAPiMF_01416. ATP_synth_delta_bact.
InterProiIPR020781. ATPase_OSCP/d_CS.
IPR026015. ATPase_OSCP/delta_N.
IPR000711. ATPase_OSCP/dsu.
[Graphical view]
PANTHERiPTHR11910. PTHR11910. 1 hit.
PfamiPF00213. OSCP. 1 hit.
[Graphical view]
PRINTSiPR00125. ATPASEDELTA.
SUPFAMiSSF47928. SSF47928. 1 hit.
TIGRFAMsiTIGR01145. ATP_synt_delta. 1 hit.
PROSITEiPS00389. ATPASE_DELTA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ATP synthase from bovine mitochondria: sequences of imported precursors of oligomycin sensitivity conferral protein, factor 6, and adenosinetriphosphatase inhibitor protein."
    Walker J.E., Gay N.J., Powell S.J., Kostina M., Dyer M.R.
    Biochemistry 26:8613-8619(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  3. "Identification of the subunits of F1F0-ATPase from bovine heart mitochondria."
    Walker J.E., Lutter R., Dupuis A., Runswick M.J.
    Biochemistry 30:5369-5378(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-28.
    Tissue: Heart.
  4. "Association of two proteolipids of unknown function with ATP synthase from bovine heart mitochondria."
    Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.
    FEBS Lett. 581:3145-3148(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.

Entry informationi

Entry nameiATPO_BOVIN
AccessioniPrimary (citable) accession number: P13621
Secondary accession number(s): Q3T0Y7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 3, 2007
Last modified: July 6, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.