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Protein

ATP synthase-coupling factor 6, mitochondrial

Gene

ATP5J

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. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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-coupling factor 6, mitochondrial
Short name:
ATPase subunit F6
Gene namesi
Name:ATP5J
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3232Mitochondrion2 PublicationsAdd
BLAST
Chaini33 – 10876ATP synthase-coupling factor 6, mitochondrialPRO_0000002526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411N6-acetyllysineBy similarity
Modified residuei46 – 461N6-acetyllysineBy similarity
Modified residuei79 – 791N6-acetyllysineBy similarity
Modified residuei84 – 841N6-acetyllysine; alternateBy similarity
Modified residuei84 – 841N6-succinyllysine; alternateBy similarity
Modified residuei99 – 991N6-acetyllysine; alternateBy similarity
Modified residuei99 – 991N6-succinyllysine; alternateBy similarity
Modified residuei105 – 1051N6-acetyllysineBy similarity
Modified residuei108 – 1081PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP02721.
PRIDEiP02721.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). 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-39023N.
IntActiP02721. 2 interactions.
MINTiMINT-5007070.
STRINGi9913.ENSBTAP00000032359.

Structurei

Secondary structure

1
108
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 403Combined sources
Helixi41 – 5414Combined sources
Beta strandi58 – 625Combined sources
Helixi66 – 8217Combined sources
Beta strandi87 – 893Combined sources
Beta strandi95 – 973Combined sources
Helixi98 – 1003Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VZSNMR-A33-108[»]
2CLYX-ray2.80C/F32-108[»]
2WSSX-ray3.20V/Z33-108[»]
4B2Qelectron microscopy37.00V/v36-101[»]
5ARAelectron microscopy6.70V32-108[»]
5AREelectron microscopy7.40V32-108[»]
5ARHelectron microscopy7.20V32-108[»]
5ARIelectron microscopy7.40V32-108[»]
5FIJelectron microscopy7.40V32-108[»]
5FIKelectron microscopy6.40V32-108[»]
5FILelectron microscopy7.10V32-108[»]
DisProtiDP00201.
ProteinModelPortaliP02721.
SMRiP02721. Positions 33-108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02721.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4634. Eukaryota.
ENOG41122G1. LUCA.
GeneTreeiENSGT00390000008902.
HOGENOMiHOG000261672.
HOVERGENiHBG062261.
InParanoidiP02721.
KOiK02131.
OMAiDIREYRT.
OrthoDBiEOG754HRZ.
TreeFamiTF318998.

Family and domain databases

InterProiIPR008387. ATPase_F0-cplx_f6su_mt.
IPR016349. ATPase_F0-cplx_f6su_mt_subgr.
[Graphical view]
PANTHERiPTHR12441. PTHR12441. 1 hit.
PfamiPF05511. ATP-synt_F6. 1 hit.
[Graphical view]
PIRSFiPIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
SUPFAMiSSF111357. SSF111357. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P02721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILQRLFRLS SAVQSAISVS WRRNIGITAV AFNKELDPVQ KLFVDKIREY
60 70 80 90 100
RTKRQTSGGP VDAGPEYQQD LDRELFKLKQ MYGKADMNTF PNFTFEDPKF

EVVEKPQS
Length:108
Mass (Da):12,532
Last modified:January 1, 1990 - v2
Checksum:iE5376A0518C3E1C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941T → F AA sequence (PubMed:6149548).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19217 mRNA. Translation: AAA30511.1.
BC103429 mRNA. Translation: AAI03430.1.
PIRiB27382. JLBO6.
RefSeqiNP_777142.1. NM_174717.3.
XP_005201201.1. XM_005201144.3.
XP_005201202.1. XM_005201145.3.
XP_005201203.1. XM_005201146.3.
XP_010799229.1. XM_010800927.1.
UniGeneiBt.404.

Genome annotation databases

EnsembliENSBTAT00000032427; ENSBTAP00000032359; ENSBTAG00000000605.
ENSBTAT00000066011; ENSBTAP00000054675; ENSBTAG00000000605.
GeneIDi282690.
KEGGibta:282690.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19217 mRNA. Translation: AAA30511.1.
BC103429 mRNA. Translation: AAI03430.1.
PIRiB27382. JLBO6.
RefSeqiNP_777142.1. NM_174717.3.
XP_005201201.1. XM_005201144.3.
XP_005201202.1. XM_005201145.3.
XP_005201203.1. XM_005201146.3.
XP_010799229.1. XM_010800927.1.
UniGeneiBt.404.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VZSNMR-A33-108[»]
2CLYX-ray2.80C/F32-108[»]
2WSSX-ray3.20V/Z33-108[»]
4B2Qelectron microscopy37.00V/v36-101[»]
5ARAelectron microscopy6.70V32-108[»]
5AREelectron microscopy7.40V32-108[»]
5ARHelectron microscopy7.20V32-108[»]
5ARIelectron microscopy7.40V32-108[»]
5FIJelectron microscopy7.40V32-108[»]
5FIKelectron microscopy6.40V32-108[»]
5FILelectron microscopy7.10V32-108[»]
DisProtiDP00201.
ProteinModelPortaliP02721.
SMRiP02721. Positions 33-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-39023N.
IntActiP02721. 2 interactions.
MINTiMINT-5007070.
STRINGi9913.ENSBTAP00000032359.

Proteomic databases

PaxDbiP02721.
PRIDEiP02721.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000032427; ENSBTAP00000032359; ENSBTAG00000000605.
ENSBTAT00000066011; ENSBTAP00000054675; ENSBTAG00000000605.
GeneIDi282690.
KEGGibta:282690.

Organism-specific databases

CTDi522.

Phylogenomic databases

eggNOGiKOG4634. Eukaryota.
ENOG41122G1. LUCA.
GeneTreeiENSGT00390000008902.
HOGENOMiHOG000261672.
HOVERGENiHBG062261.
InParanoidiP02721.
KOiK02131.
OMAiDIREYRT.
OrthoDBiEOG754HRZ.
TreeFamiTF318998.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP02721.
NextBioi20806358.

Family and domain databases

InterProiIPR008387. ATPase_F0-cplx_f6su_mt.
IPR016349. ATPase_F0-cplx_f6su_mt_subgr.
[Graphical view]
PANTHERiPTHR12441. PTHR12441. 1 hit.
PfamiPF05511. ATP-synt_F6. 1 hit.
[Graphical view]
PIRSFiPIRSF002455. ATP_synthase_coupling_factor_6. 1 hit.
SUPFAMiSSF111357. SSF111357. 1 hit.
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. Cited for: PROTEIN SEQUENCE OF 33-108.
  4. "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 33-37.
    Tissue: Heart.
  5. "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 nameiATP5J_BOVIN
AccessioniPrimary (citable) accession number: P02721
Secondary accession number(s): Q3ZBD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: April 13, 2016
This is version 121 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.