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Protein

ATP synthase-coupling factor 6, mitochondrial

Gene

Atp5j

Organism
Rattus norvegicus (Rat)
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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 11

Organism-specific databases

RGDi621376. Atp5j.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  • mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: RGD
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 – 3232Mitochondrion1 PublicationAdd
BLAST
Chaini33 – 10876ATP synthase-coupling factor 6, mitochondrialPRO_0000002531Add
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 – 1081PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP21571.
PRIDEiP21571.

2D gel databases

UCD-2DPAGEP21571.

PTM databases

iPTMnetiP21571.
PhosphoSiteiP21571.

Expressioni

Gene expression databases

GenevisibleiP21571. RN.

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

BioGridi250190. 1 interaction.
STRINGi10116.ENSRNOP00000002116.

Structurei

3D structure databases

ProteinModelPortaliP21571.
SMRiP21571. Positions 33-108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG4634. Eukaryota.
ENOG41122G1. LUCA.
GeneTreeiENSGT00390000008902.
HOGENOMiHOG000261672.
HOVERGENiHBG062261.
InParanoidiP21571.
KOiK02131.
OMAiEDPKFEA.
OrthoDBiEOG754HRZ.
PhylomeDBiP21571.
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.

P21571-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVQRIFRLS SVLRSAVSVH LRRNIGVTAV AFNKELDPVQ KLFLDKIREY
60 70 80 90 100
KAKRLASGGP VDTGPEYQQE VDRELFKLKQ MYGKGEMDKF PTFNFEDPKF

EVLDKPQS
Length:108
Mass (Da):12,494
Last modified:May 1, 1991 - v1
Checksum:iFF1177C9681B5F51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73030 mRNA. Translation: AAA40954.1.
X54510 mRNA. Translation: CAA38369.1.
BC059121 mRNA. Translation: AAH59121.1.
PIRiJC1167.
RefSeqiNP_446054.1. NM_053602.2.
XP_008766824.1. XM_008768602.1.
XP_008766825.1. XM_008768603.1.
UniGeneiRn.5790.

Genome annotation databases

EnsembliENSRNOT00000002116; ENSRNOP00000002116; ENSRNOG00000001551.
GeneIDi94271.
KEGGirno:94271.
UCSCiRGD:621376. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73030 mRNA. Translation: AAA40954.1.
X54510 mRNA. Translation: CAA38369.1.
BC059121 mRNA. Translation: AAH59121.1.
PIRiJC1167.
RefSeqiNP_446054.1. NM_053602.2.
XP_008766824.1. XM_008768602.1.
XP_008766825.1. XM_008768603.1.
UniGeneiRn.5790.

3D structure databases

ProteinModelPortaliP21571.
SMRiP21571. Positions 33-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250190. 1 interaction.
STRINGi10116.ENSRNOP00000002116.

PTM databases

iPTMnetiP21571.
PhosphoSiteiP21571.

2D gel databases

UCD-2DPAGEP21571.

Proteomic databases

PaxDbiP21571.
PRIDEiP21571.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000002116; ENSRNOP00000002116; ENSRNOG00000001551.
GeneIDi94271.
KEGGirno:94271.
UCSCiRGD:621376. rat.

Organism-specific databases

CTDi522.
RGDi621376. Atp5j.

Phylogenomic databases

eggNOGiKOG4634. Eukaryota.
ENOG41122G1. LUCA.
GeneTreeiENSGT00390000008902.
HOGENOMiHOG000261672.
HOVERGENiHBG062261.
InParanoidiP21571.
KOiK02131.
OMAiEDPKFEA.
OrthoDBiEOG754HRZ.
PhylomeDBiP21571.
TreeFamiTF318998.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi617909.
PROiP21571.

Gene expression databases

GenevisibleiP21571. RN.

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. "cDNA cloning and sequencing for the import precursor of coupling factor 6 in H(+)-ATP synthase from rat liver mitochondria."
    Higuti T., Osaka F., Yoshihara Y., Tsurumi C., Kawamura Y., Tani I., Toda H., Kakuno T., Sakiyama F., Tanaka K., Ichihara A.
    Biochem. Biophys. Res. Commun. 171:1079-1086(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Rat mitochondrial coupling factor 6: molecular cloning of a cDNA encoding the imported precursor."
    Tracer H.L., Loh Y.P., Birch N.P.
    Gene 116:291-292(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pituitary anterior lobe.
  3. "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: Pituitary.
  4. "A simple, rapid method for purification of epsilon-subunit, coupling factor 6, subunit d, and subunit e from rat liver H(+)-ATP synthase and determination of the complete amino acid sequence of epsilon-subunit."
    Higuti T., Yoshihara Y., Kuroiwa K., Kawamura Y., Toda H., Sakiyama F.
    J. Biol. Chem. 267:22658-22661(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-66.
    Tissue: Liver.
  5. "Identification of two proteins associated with mammalian ATP synthase."
    Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.
    Mol. Cell. Proteomics 6:1690-1699(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiATP5J_RAT
AccessioniPrimary (citable) accession number: P21571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: January 20, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.