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Protein

ATP synthase-coupling factor 6, mitochondrial

Gene

ATP5J

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processHydrogen 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-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

Organism-specific databases

VGNCiVGNC:26304 ATP5PF

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

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 32Mitochondrion2 PublicationsAdd BLAST32
ChainiPRO_000000252633 – 108ATP synthase-coupling factor 6, mitochondrialAdd BLAST76

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei41N6-acetyllysineBy similarity1
Modified residuei46N6-acetyllysineBy similarity1
Modified residuei79N6-acetyllysineBy similarity1
Modified residuei84N6-acetyllysine; alternateBy similarity1
Modified residuei84N6-succinyllysine; alternateBy similarity1
Modified residuei99N6-acetyllysine; alternateBy similarity1
Modified residuei99N6-succinyllysine; alternateBy similarity1
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei108PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP02721
PeptideAtlasiP02721
PRIDEiP02721

Expressioni

Gene expression databases

BgeeiENSBTAG00000000605

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, 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

CORUMiP02721
DIPiDIP-39023N
IntActiP02721, 3 interactors
MINTiP02721
STRINGi9913.ENSBTAP00000032359

Structurei

Secondary structure

1108
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 40Combined sources3
Helixi41 – 54Combined sources14
Beta strandi58 – 62Combined sources5
Helixi66 – 82Combined sources17
Beta strandi95 – 97Combined sources3
Helixi98 – 100Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02721

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4634 Eukaryota
ENOG41122G1 LUCA
GeneTreeiENSGT00390000008902
HOGENOMiHOG000261672
HOVERGENiHBG062261
InParanoidiP02721
KOiK02131
OMAiSPAIEKE
OrthoDBiEOG091G10KV
TreeFamiTF318998

Family and domain databases

InterProiView protein in InterPro
IPR008387 ATP_synth_f6_mt
IPR036204 ATP_synth_f6_sf_mt
PANTHERiPTHR12441 PTHR12441, 1 hit
PfamiView protein in Pfam
PF05511 ATP-synt_F6, 1 hit
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)DescriptionActionsGraphical viewLength
Sequence conflicti94T → F AA sequence (PubMed:6149548).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiATP5J_BOVIN
AccessioniPrimary (citable) accession number: P02721
Secondary accession number(s): Q3ZBD6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1990
Last modified: April 25, 2018
This is version 137 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
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Main funding by: National Institutes of Health