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Protein

ATP synthase subunit O, mitochondrial

Gene

ATP5O

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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

Keywordsi

Biological processATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-BTA-163210 Formation of ATP by chemiosmotic coupling
R-BTA-8949613 Cristae formation

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Transit peptidei1 – 23Mitochondrion1 PublicationAdd BLAST23
ChainiPRO_000000264524 – 213ATP synthase subunit O, mitochondrialAdd BLAST190

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei54N6-acetyllysineBy similarity1
Modified residuei60N6-acetyllysineBy similarity1
Modified residuei70N6-acetyllysineBy similarity1
Modified residuei73N6-acetyllysineBy similarity1
Modified residuei90N6-succinyllysineBy similarity1
Modified residuei100N6-acetyllysine; alternateBy similarity1
Modified residuei100N6-succinyllysine; alternateBy similarity1
Modified residuei158N6-acetyllysine; alternateBy similarity1
Modified residuei158N6-succinyllysine; alternateBy similarity1
Modified residuei162N6-acetyllysine; alternateBy similarity1
Modified residuei162N6-succinyllysine; alternateBy similarity1
Modified residuei172N6-acetyllysineBy similarity1
Modified residuei176N6-acetyllysineBy similarity1
Modified residuei192N6-acetyllysineBy similarity1
Modified residuei199N6-succinyllysineBy similarity1

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

Expressioni

Gene expression databases

BgeeiENSBTAG00000018278

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, ATP5MC1, ATP5F1E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5O, ATP5L, USMG5 and MP68.1 Publication

Protein-protein interaction databases

CORUMiP13621
DIPiDIP-39019N
IntActiP13621, 3 interactors
MINTiP13621
STRINGi9913.ENSBTAP00000024326

Structurei

Secondary structure

1213
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi37 – 52Combined sources16
Helixi55 – 70Combined sources16
Helixi72 – 75Combined sources4
Turni76 – 79Combined sources4
Beta strandi81 – 83Combined sources3
Beta strandi85 – 87Combined sources3
Helixi88 – 96Combined sources9
Beta strandi97 – 100Combined sources4
Beta strandi102 – 105Combined sources4
Helixi108 – 112Combined sources5
Turni113 – 116Combined sources4
Beta strandi118 – 120Combined sources3
Helixi122 – 137Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
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
OMAiMVDNIQD
OrthoDBiEOG091G0L4M
TreeFamiTF106241

Family and domain databases

Gene3Di1.10.520.20, 1 hit
HAMAPiMF_01416 ATP_synth_delta_bact, 1 hit
InterProiView protein in InterPro
IPR026015 ATP_synth_OSCP/delta_N_sf
IPR020781 ATPase_OSCP/d_CS
IPR000711 ATPase_OSCP/dsu
PANTHERiPTHR11910 PTHR11910, 1 hit
PfamiView protein in Pfam
PF00213 OSCP, 1 hit
PRINTSiPR00125 ATPASEDELTA
SUPFAMiSSF47928 SSF47928, 1 hit
TIGRFAMsiTIGR01145 ATP_synt_delta, 1 hit
PROSITEiView protein in PROSITE
PS00389 ATPASE_DELTA, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti152A → T in AAA30676 (PubMed:2894843).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiATPO_BOVIN
AccessioniPrimary (citable) accession number: P13621
Secondary accession number(s): Q3T0Y7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 3, 2007
Last modified: April 25, 2018
This is version 147 of the entry and version 2 of the sequence. See 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

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