ID   ATP5I_CRILO             Reviewed;          69 AA.
AC   P12633;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 90.
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};
DE   AltName: Full=UV-inducible PU4 protein;
GN   Name=ATP5ME {ECO:0000250|UniProtKB:P56385}; Synonyms=ATP5I;
OS   Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2463464; DOI=10.1128/mcb.8.11.4716-4720.1988;
RA   Fornace A.J. Jr., Schalch H., Alamo I. Jr.;
RT   "Coordinate induction of metallothioneins I and II in rodent cells by UV
RT   irradiation.";
RL   Mol. Cell. Biol. 8:4716-4720(1988).
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   -!- INDUCTION: By UV light.
CC   -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR   EMBL; M22350; AAA37028.1; -; mRNA.
DR   AlphaFoldDB; P12633; -.
DR   SMR; P12633; -.
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); IEA:InterPro.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR   PANTHER; PTHR12427; PTHR12427; 1.
DR   Pfam; PF05680; ATP-synt_E; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Transport.
FT   CHAIN           1..69
FT                   /note="ATP synthase subunit e, mitochondrial"
FT                   /id="PRO_0000071683"
FT   MOD_RES         34
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06185"
SQ   SEQUENCE   69 AA;  7930 MW;  1C5375A967B7E95F CRC64;
     MVPPVQVSPL IKLGRYSALV LGMAYGAKRY SYLKPRAEEE RRVAAEEKKR LDELKRIERE
     LAEGDTILK