ATP5I_MOUSE
ID ATP5I_MOUSE Reviewed; 71 AA.
AC Q06185; P70342;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000305};
DE Short=ATPase subunit e;
DE AltName: Full=ATP synthase membrane subunit e {ECO:0000305};
GN Name=Atp5me {ECO:0000250|UniProtKB:P56385};
GN Synonyms=Atp5i, Atp5k, Lfm-1, Lfm1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Mammary gland;
RX PubMed=7678489; DOI=10.1006/bbrc.1993.1026;
RA Elliott T.S., Swartz D.A., Paisley E.A., Mangian H.J., Visek W.J.,
RA Kaput J.;
RT "F1F0-ATPase subunit e gene isolated in a screen for diet regulated
RT genes.";
RL Biochem. Biophys. Res. Commun. 190:167-174(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=8702853; DOI=10.1074/jbc.271.34.20942;
RA Swartz D.A., Park E.I., Visek W.J., Kaput J.;
RT "The e subunit gene of murine F1F0-ATP synthase. Genomic sequence,
RT chromosomal mapping, and diet regulation.";
RL J. Biol. Chem. 271:20942-20948(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-12; 16-28 AND 60-71, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Part of the complex
CC F(0) domain. Minor subunit located with subunit a in the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
CC ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- TISSUE SPECIFICITY: Mammary gland, liver, kidney, heart, spleen, brain
CC and lung.
CC -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR EMBL; S52977; AAB24947.1; -; mRNA.
DR EMBL; U59283; AAC52713.1; -; Genomic_DNA.
DR EMBL; BC028438; AAH28438.1; -; mRNA.
DR CCDS; CCDS39204.1; -.
DR PIR; JC1412; JC1412.
DR RefSeq; NP_031533.2; NM_007507.2.
DR AlphaFoldDB; Q06185; -.
DR SMR; Q06185; -.
DR BioGRID; 198259; 76.
DR IntAct; Q06185; 4.
DR STRING; 10090.ENSMUSP00000051222; -.
DR iPTMnet; Q06185; -.
DR PhosphoSitePlus; Q06185; -.
DR EPD; Q06185; -.
DR jPOST; Q06185; -.
DR MaxQB; Q06185; -.
DR PaxDb; Q06185; -.
DR PeptideAtlas; Q06185; -.
DR PRIDE; Q06185; -.
DR ProteomicsDB; 277089; -.
DR TopDownProteomics; Q06185; -.
DR Antibodypedia; 22135; 186 antibodies from 28 providers.
DR DNASU; 11958; -.
DR Ensembl; ENSMUST00000049628; ENSMUSP00000051222; ENSMUSG00000050856.
DR GeneID; 11958; -.
DR KEGG; mmu:11958; -.
DR UCSC; uc008yoa.1; mouse.
DR CTD; 11958; -.
DR MGI; MGI:106636; Atp5k.
DR VEuPathDB; HostDB:ENSMUSG00000050856; -.
DR eggNOG; KOG4326; Eukaryota.
DR GeneTree; ENSGT00390000005102; -.
DR HOGENOM; CLU_180903_0_0_1; -.
DR InParanoid; Q06185; -.
DR OMA; GAFHQNR; -.
DR OrthoDB; 1640426at2759; -.
DR PhylomeDB; Q06185; -.
DR TreeFam; TF314719; -.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR BioGRID-ORCS; 11958; 26 hits in 71 CRISPR screens.
DR ChiTaRS; Atp5k; mouse.
DR PRO; PR:Q06185; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q06185; protein.
DR Bgee; ENSMUSG00000050856; Expressed in facial nucleus and 246 other tissues.
DR ExpressionAtlas; Q06185; baseline and differential.
DR Genevisible; Q06185; MM.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:MGI.
DR InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR PANTHER; PTHR12427; PTHR12427; 1.
DR Pfam; PF05680; ATP-synt_E; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P56385"
FT CHAIN 2..71
FT /note="ATP synthase subunit e, mitochondrial"
FT /id="PRO_0000071685"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29419"
FT CONFLICT 13
FT /note="F -> S (in Ref. 2; AAC52713)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="K -> R (in Ref. 2; AAC52713)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 71 AA; 8236 MW; 0379C3E14C098F12 CRC64;
MVPPVQVSPL IKFGRYSALI IGMAYGAKRY SYLKPRAEEE RRIAAEEKKR LDELKRIERE
LAEAQDDSIL K
