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Protein

ATP synthase subunit e, mitochondrial

Gene

Atp5i

Organism
Mus musculus (Mouse)
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. Minor subunit located with subunit a in the membrane.

GO - Molecular functioni

  1. ATPase activity Source: Ensembl
  2. hydrogen ion transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. ATP synthesis coupled proton transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_287909. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit e, mitochondrial
Short name:
ATPase subunit e
Gene namesi
Name:Atp5i
Synonyms:Atp5k, Lfm-1, Lfm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:106636. Atp5k.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  2. mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) Source: InterPro
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 7170ATP synthase subunit e, mitochondrialPRO_0000071685Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ06185.
PaxDbiQ06185.
PRIDEiQ06185.

PTM databases

PhosphoSiteiQ06185.

Expressioni

Tissue specificityi

Mammary gland, liver, kidney, heart, spleen, brain and lung.

Gene expression databases

BgeeiQ06185.
ExpressionAtlasiQ06185. baseline and differential.
GenevestigatoriQ06185.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198259. 1 interaction.
IntActiQ06185. 1 interaction.
MINTiMINT-1840518.
STRINGi10090.ENSMUSP00000051222.

Structurei

3D structure databases

ProteinModelPortaliQ06185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase e subunit family.Curated

Phylogenomic databases

eggNOGiNOG81326.
GeneTreeiENSGT00390000005102.
HOGENOMiHOG000231826.
HOVERGENiHBG050613.
InParanoidiQ06185.
KOiK02129.
OMAiEQERIYK.
OrthoDBiEOG7MD4T1.
PhylomeDBiQ06185.
TreeFamiTF314719.

Family and domain databases

InterProiIPR008386. ATPase_F0-cplx_esu_mt.
[Graphical view]
PfamiPF05680. ATP-synt_E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q06185-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPPVQVSPL IKFGRYSALI IGMAYGAKRY SYLKPRAEEE RRIAAEEKKR
60 70
LDELKRIERE LAEAQDDSIL K
Length:71
Mass (Da):8,236
Last modified:January 23, 2007 - v2
Checksum:i0379C3E14C098F12
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131F → S in AAC52713 (PubMed:8702853).Curated
Sequence conflicti48 – 481K → R in AAC52713 (PubMed:8702853).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S52977 mRNA. Translation: AAB24947.1.
U59283 Genomic DNA. Translation: AAC52713.1.
BC028438 mRNA. Translation: AAH28438.1.
CCDSiCCDS39204.1.
PIRiJC1412.
RefSeqiNP_031533.2. NM_007507.2.
UniGeneiMm.136093.

Genome annotation databases

EnsembliENSMUST00000049628; ENSMUSP00000051222; ENSMUSG00000050856.
GeneIDi11958.
KEGGimmu:11958.
UCSCiuc008yoa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S52977 mRNA. Translation: AAB24947.1.
U59283 Genomic DNA. Translation: AAC52713.1.
BC028438 mRNA. Translation: AAH28438.1.
CCDSiCCDS39204.1.
PIRiJC1412.
RefSeqiNP_031533.2. NM_007507.2.
UniGeneiMm.136093.

3D structure databases

ProteinModelPortaliQ06185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198259. 1 interaction.
IntActiQ06185. 1 interaction.
MINTiMINT-1840518.
STRINGi10090.ENSMUSP00000051222.

PTM databases

PhosphoSiteiQ06185.

Proteomic databases

MaxQBiQ06185.
PaxDbiQ06185.
PRIDEiQ06185.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049628; ENSMUSP00000051222; ENSMUSG00000050856.
GeneIDi11958.
KEGGimmu:11958.
UCSCiuc008yoa.1. mouse.

Organism-specific databases

CTDi11958.
MGIiMGI:106636. Atp5k.

Phylogenomic databases

eggNOGiNOG81326.
GeneTreeiENSGT00390000005102.
HOGENOMiHOG000231826.
HOVERGENiHBG050613.
InParanoidiQ06185.
KOiK02129.
OMAiEQERIYK.
OrthoDBiEOG7MD4T1.
PhylomeDBiQ06185.
TreeFamiTF314719.

Enzyme and pathway databases

ReactomeiREACT_287909. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

NextBioi280081.
PROiQ06185.
SOURCEiSearch...

Gene expression databases

BgeeiQ06185.
ExpressionAtlasiQ06185. baseline and differential.
GenevestigatoriQ06185.

Family and domain databases

InterProiIPR008386. ATPase_F0-cplx_esu_mt.
[Graphical view]
PfamiPF05680. ATP-synt_E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "F1F0-ATPase subunit e gene isolated in a screen for diet regulated genes."
    Elliott T.S., Swartz D.A., Paisley E.A., Mangian H.J., Visek W.J., Kaput J.
    Biochem. Biophys. Res. Commun. 190:167-174(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Mammary gland.
  2. "The e subunit gene of murine F1F0-ATP synthase. Genomic sequence, chromosomal mapping, and diet regulation."
    Swartz D.A., Park E.I., Visek W.J., Kaput J.
    J. Biol. Chem. 271:20942-20948(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
  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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 16-28 AND 60-71, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiATP5I_MOUSE
AccessioniPrimary (citable) accession number: Q06185
Secondary accession number(s): P70342
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 114 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.