ATP5E_MOUSE
ID ATP5E_MOUSE Reviewed; 52 AA.
AC P56382;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=ATP synthase subunit epsilon, mitochondrial {ECO:0000305};
DE Short=ATPase subunit epsilon;
DE AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000250|UniProtKB:P56381};
GN Name=Atp5f1e {ECO:0000250|UniProtKB:P56381}; Synonyms=Atp5e;
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 [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [2]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-21; LYS-32 AND LYS-37, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21; LYS-32; LYS-37 AND LYS-44,
RP AND IDENTIFICATION BY MASS 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(1) domain and of the central stalk which is part of the complex
CC rotary element. Rotation of the central stalk against the surrounding
CC alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate
CC catalytic sites on the beta subunits (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) seems to have
CC nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an
CC ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD,
CC ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D,
CC ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase epsilon family.
CC {ECO:0000305}.
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DR EMBL; BC024339; AAH24339.1; -; mRNA.
DR CCDS; CCDS38360.1; -.
DR RefSeq; NP_080259.1; NM_025983.3.
DR AlphaFoldDB; P56382; -.
DR BioGRID; 211960; 48.
DR STRING; 10090.ENSMUSP00000016396; -.
DR iPTMnet; P56382; -.
DR PhosphoSitePlus; P56382; -.
DR EPD; P56382; -.
DR jPOST; P56382; -.
DR PaxDb; P56382; -.
DR PeptideAtlas; P56382; -.
DR PRIDE; P56382; -.
DR ProteomicsDB; 277130; -.
DR TopDownProteomics; P56382; -.
DR Antibodypedia; 29273; 154 antibodies from 21 providers.
DR DNASU; 67126; -.
DR Ensembl; ENSMUST00000016396; ENSMUSP00000016396; ENSMUSG00000016252.
DR GeneID; 67126; -.
DR KEGG; mmu:67126; -.
DR UCSC; uc008off.1; mouse.
DR CTD; 67126; -.
DR MGI; MGI:1855697; Atp5e.
DR VEuPathDB; HostDB:ENSMUSG00000016252; -.
DR eggNOG; KOG3495; Eukaryota.
DR GeneTree; ENSGT00390000015470; -.
DR HOGENOM; CLU_187039_4_0_1; -.
DR InParanoid; P56382; -.
DR OMA; SQICANA; -.
DR OrthoDB; 1628103at2759; -.
DR PhylomeDB; P56382; -.
DR TreeFam; TF300278; -.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR BioGRID-ORCS; 67126; 17 hits in 68 CRISPR screens.
DR ChiTaRS; Atp5e; mouse.
DR PRO; PR:P56382; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P56382; protein.
DR Bgee; ENSMUSG00000016252; Expressed in hindlimb stylopod muscle and 262 other tissues.
DR ExpressionAtlas; P56382; baseline and differential.
DR Genevisible; P56382; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; ISA: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:0015986; P:proton motive force-driven ATP synthesis; ISA:MGI.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR CDD; cd12153; F1-ATPase_epsilon; 1.
DR Gene3D; 1.10.1620.20; -; 1.
DR InterPro; IPR006721; ATP_synth_F1_esu_mt.
DR InterPro; IPR036742; ATP_synth_F1_esu_sf_mt.
DR PANTHER; PTHR12448; PTHR12448; 1.
DR Pfam; PF04627; ATP-synt_Eps; 1.
DR SUPFAM; SSF48690; SSF48690; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transport.
FT CHAIN 1..52
FT /note="ATP synthase subunit epsilon, mitochondrial"
FT /id="PRO_0000071663"
FT MOD_RES 21
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 21
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 37
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 52 AA; 5838 MW; 406371C227DAA127 CRC64;
MVAYWRQAGL SYIRFSQICA KAVRDALKTE FKANAEKTSG SSIKIVKVSK KE
