ID   ATP5E_YARLI             Reviewed;          10 AA.
AC   C0HLB1;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   11-DEC-2019, entry version 4.
DE   RecName: Full=ATP synthase subunit epsilon, mitochondrial {ECO:0000250|UniProtKB:P21306};
DE            Short=ATPase subunit epsilon {ECO:0000250|UniProtKB:P21306};
DE   Flags: Fragment;
GN   Name=ATP15 {ECO:0000250|UniProtKB:P21306};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION IN ATP SYNTHASE COMPLEX,
RP   FUNCTION OF ATP SYNTHASE COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP   SPECTROMETRY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=CLIB 122 / E 150 {ECO:0000303|PubMed:25759169};
RX   PubMed=25759169; DOI=10.1042/bj20150197;
RA   Liu S., Charlesworth T.J., Bason J.V., Montgomery M.G., Harbour M.E.,
RA   Fearnley I.M., Walker J.E.;
RT   "The purification and characterization of ATP synthase complexes from the
RT   mitochondria of four fungal species.";
RL   Biochem. J. 468:167-175(2015).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF ATP SYNTHASE F1C10 COMPLEX,
RP   STRUCTURE BY ELECTRON MICROSCOPY (7.7 ANGSTROMS) OF DIMERIC ATP SYNTHASE
RP   COMPLEX, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=27373333; DOI=10.1016/j.molcel.2016.05.037;
RA   Hahn A., Parey K., Bublitz M., Mills D.J., Zickermann V., Vonck J.,
RA   Kuehlbrandt W., Meier T.;
RT   "Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of
RT   Inner Mitochondrial Membrane Morphology.";
RL   Mol. Cell 63:445-456(2016).
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 (PubMed:25759169). F-type ATP synthases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core, and F(0) - containing the membrane
CC       proton channel, linked together by a central stalk and a peripheral
CC       stalk (PubMed:27373333). During catalysis, ATP synthesis in the
CC       catalytic domain of F(1) is coupled via a rotary mechanism of the
CC       central stalk subunits to proton translocation (PubMed:27373333). Part
CC       of the complex F(1) domain and the central stalk which is part of the
CC       complex rotary element (PubMed:27373333). Rotation of the central stalk
CC       against the surrounding alpha/ATP1(3)beta/ATP2(3) subunits leads to
CC       hydrolysis of ATP in three separate catalytic sites on the beta/ATP2
CC       subunits (PubMed:27373333). {ECO:0000269|PubMed:25759169,
CC       ECO:0000269|PubMed:27373333}.
CC   -!- SUBUNIT: F-type ATP synthases have 2 components, the catalytic core
CC       F(1) and the membrane-embedded component F(0), linked together by a
CC       central stalk and a peripheral stalk (PubMed:27373333). The central
CC       stalk, also called rotor shaft, is often seen as part of F(1)
CC       (PubMed:27373333). The peripheral stalk is seen as part of F(0)
CC       (PubMed:27373333). F(0) contains the membrane channel next to the rotor
CC       (PubMed:27373333). F-type ATP synthases form dimers but each monomer
CC       functions independently in ATP generation (PubMed:27373333). The dimer
CC       consists of 17 different polypeptides: ATP1 (subunit alpha, 3 molecules
CC       per monomer, part of F(1)), ATP2 (subunit beta, 3 copies per monomer,
CC       part of F(1)), ATP3 (subunit gamma, part of the central stalk), ATP4
CC       (subunit b, part of the peripheral stalk), ATP5/OSCP (subunit 5/OSCP,
CC       part of the peripheral stalk), ATP6 (subunit a, part of the peripheral
CC       stalk), ATP7 (subunit d, part of the peripheral stalk), ATP8 (subunit
CC       8, part of the peripheral stalk), OLI1 (subunit c, part of the rotor,
CC       10 molecules per monomer), ATP14 (subunit h, part of the peripheral
CC       stalk), ATP15 (subunit epsilon, part of the central stalk), ATP16
CC       (subunit delta, part of the central stalk), ATP17 (subunit f, part of
CC       the peripheral stalk), ATP18 (subunit i/j, part of the peripheral
CC       stalk), ATP19 (subunit k, dimer-specific, at interface between
CC       monomers), ATP20 (subunit g, at interface between monomers), TIM11
CC       (subunit e, at interface between monomers) (PubMed:27373333,
CC       PubMed:25759169). {ECO:0000269|PubMed:25759169,
CC       ECO:0000269|PubMed:27373333}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:27373333}; Peripheral membrane protein
CC       {ECO:0000305|PubMed:27373333}; Matrix side
CC       {ECO:0000305|PubMed:27373333}. Note=The F-type ATP synthase complex is
CC       anchored in the mitochondrial inner membrane via the F(0) domain with
CC       the F(1) domain and the peripheral stalk extending into the
CC       mitochondrial matrix. {ECO:0000305|PubMed:27373333}.
CC   -!- MASS SPECTROMETRY: Mass=6810.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:25759169};
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase epsilon family.
CC       {ECO:0000305}.
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DR   EMBL; CR382131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PDB; 5FL7; X-ray; 3.50 A; H=1-10.
DR   PDBsum; 5FL7; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:25759169"
FT   CHAIN           2..>10
FT                   /note="ATP synthase subunit epsilon, mitochondrial"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000445330"
FT   NON_TER         10
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   10 AA;  1074 MW;  C639F17DC5B6837D CRC64;
     MSAWMSAGFS