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Q06185 (ATP5I_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit e, mitochondrial

Short name=ATPase subunit e
Gene names
Name:Atp5i
Synonyms:Atp5k, Lfm-1, Lfm1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length71 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Mitochondrion. Mitochondrion inner membrane.

Tissue specificity

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

Sequence similarities

Belongs to the ATPase e subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 7170ATP synthase subunit e, mitochondrial
PRO_0000071685

Amino acid modifications

Modified residue341N6-acetyllysine Ref.5

Experimental info

Sequence conflict131F → S in AAC52713. Ref.2
Sequence conflict481K → R in AAC52713. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q06185 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0379C3E14C098F12

FASTA718,236
        10         20         30         40         50         60 
MVPPVQVSPL IKFGRYSALI IGMAYGAKRY SYLKPRAEEE RRIAAEEKKR LDELKRIERE 

        70 
LAEAQDDSIL K 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S52977 mRNA. Translation: AAB24947.1.
U59283 Genomic DNA. Translation: AAC52713.1.
BC028438 mRNA. Translation: AAH28438.1.
PIRJC1412.
RefSeqNP_031533.2. NM_007507.2.
UniGeneMm.136093.

3D structure databases

ProteinModelPortalQ06185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ06185. 1 interaction.
MINTMINT-1840518.
STRING10090.ENSMUSP00000051222.

PTM databases

PhosphoSiteQ06185.

Proteomic databases

PaxDbQ06185.
PRIDEQ06185.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049628; ENSMUSP00000051222; ENSMUSG00000050856.
GeneID11958.
KEGGmmu:11958.
UCSCuc008yoa.1. mouse.

Organism-specific databases

CTD11958.
MGIMGI:106636. Atp5k.

Phylogenomic databases

eggNOGNOG81326.
GeneTreeENSGT00390000005102.
HOGENOMHOG000231826.
HOVERGENHBG050613.
InParanoidQ06185.
KOK02129.
OMAEQERIYK.
OrthoDBEOG7MD4T1.
PhylomeDBQ06185.
TreeFamTF314719.

Gene expression databases

ArrayExpressQ06185.
BgeeQ06185.
GenevestigatorQ06185.

Family and domain databases

InterProIPR008386. ATPase_F0-cplx_esu_mt.
[Graphical view]
PfamPF05680. ATP-synt_E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280081.
PROQ06185.
SOURCESearch...

Entry information

Entry nameATP5I_MOUSE
AccessionPrimary (citable) accession number: Q06185
Secondary accession number(s): P70342
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot