Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q06185 (ATP5I_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 99. 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 residue321Phosphotyrosine 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, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-32, MASS SPECTROMETRY.
Tissue: Brain.
+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.
IPIIPI00111770.
PIRJC1412.
RefSeqNP_031533.2. NM_007507.2.
UniGeneMm.136093.

3D structure databases

ProteinModelPortalQ06185.
ModBaseSearch...

Protein-protein interaction databases

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.
OrthoDBEOG45758D.

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.
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: May 29, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families