ID   ATP5E_CAEEL             Reviewed;          54 AA.
AC   P34539;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Putative ATP synthase subunit epsilon, mitochondrial;
DE            Short=ATPase subunit epsilon;
GN   ORFNames=R05D3.6;
GN   and
GN   ORFNames=ZC262.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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.
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}.
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; FO081667; CCD73192.1; -; Genomic_DNA.
DR   EMBL; FO081113; CCD69197.1; -; Genomic_DNA.
DR   PIR; S44879; S44879.
DR   RefSeq; NP_498839.1; NM_066438.1.
DR   RefSeq; NP_498841.1; NM_066440.1.
DR   AlphaFoldDB; P34539; -.
DR   SMR; P34539; -.
DR   BioGRID; 41382; 1.
DR   BioGRID; 55681; 5.
DR   IntAct; P34539; 1.
DR   STRING; 6239.R05D3.6; -.
DR   EPD; P34539; -.
DR   PaxDb; P34539; -.
DR   PeptideAtlas; P34539; -.
DR   EnsemblMetazoa; R05D3.6.1; R05D3.6.1; WBGene00019880.
DR   EnsemblMetazoa; ZC262.5.1; ZC262.5.1; WBGene00022582.
DR   GeneID; 176178; -.
DR   GeneID; 191132; -.
DR   KEGG; cel:CELE_ZC262.5; -.
DR   UCSC; ZC262.5; c. elegans.
DR   CTD; 176178; -.
DR   CTD; 191132; -.
DR   WormBase; R05D3.6; CE00285; WBGene00019880; -.
DR   WormBase; ZC262.5; CE00285; WBGene00022582; -.
DR   eggNOG; KOG3495; Eukaryota.
DR   GeneTree; ENSGT00970000196975; -.
DR   HOGENOM; CLU_187039_3_1_1; -.
DR   InParanoid; P34539; -.
DR   OrthoDB; 1628103at2759; -.
DR   PhylomeDB; P34539; -.
DR   PRO; PR:P34539; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00019880; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
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   Pfam; PF04627; ATP-synt_Eps; 1.
DR   SUPFAM; SSF48690; SSF48690; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transport.
FT   CHAIN           1..54
FT                   /note="Putative ATP synthase subunit epsilon,
FT                   mitochondrial"
FT                   /id="PRO_0000071665"
SQ   SEQUENCE   54 AA;  5926 MW;  D7DD07AD9F1CB578 CRC64;
     MVAWRAAGLN YVRYSQIAAQ VVRQCTKGGA NVKKPQATLK TTAWENGKMV SKSQ