ID   AT5EL_HUMAN             Reviewed;          51 AA.
AC   Q5VTU8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=ATP synthase subunit epsilon-like protein, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase F1 subunit epsilon pseudogene 2 {ECO:0000312|HGNC:HGNC:34026};
GN   Name=ATP5F1EP2 {ECO:0000312|HGNC:HGNC:34026};
GN   Synonyms=ATP5EP2 {ECO:0000312|HGNC:HGNC:34026};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND CAUTION.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17924679; DOI=10.1021/pr070152u;
RA   Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT   "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT   and high confident phosphopeptide identification by cross-validation of
RT   MS/MS and MS/MS/MS spectra.";
RL   J. Proteome Res. 6:4150-4162(2007).
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).
CC       {ECO:0000250|UniProtKB:P56381}.
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) (By similarity).
CC       {ECO:0000250|UniProtKB:P56381}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P56381}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase epsilon family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Defined as a pseudogene by HGNC. However, proteomic data on a
CC       specific peptide suggest the existence of this protein.
CC       {ECO:0000305|PubMed:17924679}.
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DR   EMBL; AL591024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q5VTU8; -.
DR   SMR; Q5VTU8; -.
DR   ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR   IntAct; Q5VTU8; 18.
DR   STRING; 9606.ENSP00000370414; -.
DR   BioMuta; ATP5EP2; -.
DR   DMDM; 74746994; -.
DR   EPD; Q5VTU8; -.
DR   jPOST; Q5VTU8; -.
DR   MassIVE; Q5VTU8; -.
DR   MaxQB; Q5VTU8; -.
DR   PaxDb; Q5VTU8; -.
DR   PeptideAtlas; Q5VTU8; -.
DR   PRIDE; Q5VTU8; -.
DR   ProteomicsDB; 65358; -.
DR   TopDownProteomics; Q5VTU8; -.
DR   UCSC; uc001uru.4; human.
DR   GeneCards; ATP5F1EP2; -.
DR   HGNC; HGNC:34026; ATP5F1EP2.
DR   neXtProt; NX_Q5VTU8; -.
DR   eggNOG; KOG3495; Eukaryota.
DR   HOGENOM; CLU_187039_4_0_1; -.
DR   InParanoid; Q5VTU8; -.
DR   PhylomeDB; Q5VTU8; -.
DR   TreeFam; TF300278; -.
DR   PathwayCommons; Q5VTU8; -.
DR   SignaLink; Q5VTU8; -.
DR   ChiTaRS; ATP5EP2; human.
DR   Pharos; Q5VTU8; Tdark.
DR   PRO; PR:Q5VTU8; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q5VTU8; protein.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IC:ComplexPortal.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IC:ComplexPortal.
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; Hydrolase;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Transport.
FT   CHAIN           1..51
FT                   /note="ATP synthase subunit epsilon-like protein,
FT                   mitochondrial"
FT                   /id="PRO_0000347182"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P56381"
SQ   SEQUENCE   51 AA;  5807 MW;  3352CE8EC90F6DCE CRC64;
     MVAYWRQAGL SYIRYSQICA KVVRDALKTE FKANAKKTSG NSVKIVKVKK E