ATP5E_BOVIN
ID ATP5E_BOVIN Reviewed; 51 AA.
AC P05632; Q32PE5;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 182.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=2137333; DOI=10.1042/bj2650321;
RA Vinas O., Powell S.J., Runswick M.J., Iacobazzi V., Walker J.E.;
RT "The epsilon-subunit of ATP synthase from bovine heart mitochondria.
RT Complementary DNA sequence, expression in bovine tissues and evidence of
RT homologous sequences in man and rat.";
RL Biochem. J. 265:321-326(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-51.
RX PubMed=2864455; DOI=10.1016/0022-2836(85)90313-4;
RA Walker J.E., Fearnley I.M., Gay N.J., Gibson B.W., Northrop F.D.,
RA Powell S.J., Runswick M.J., Saraste M., Tybulewicz V.L.J.;
RT "Primary structure and subunit stoichiometry of F1-ATPase from bovine
RT mitochondria.";
RL J. Mol. Biol. 184:677-701(1985).
RN [4]
RP PROTEIN SEQUENCE OF 2-7.
RC TISSUE=Heart;
RX PubMed=1827992; DOI=10.1021/bi00236a007;
RA Walker J.E., Lutter R., Dupuis A., Runswick M.J.;
RT "Identification of the subunits of F1F0-ATPase from bovine heart
RT mitochondria.";
RL Biochemistry 30:5369-5378(1991).
RN [5]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8065448; DOI=10.1038/370621a0;
RA Abrahams J.P., Leslie A.G.W., Lutter R., Walker J.E.;
RT "Structure at 2.8-A resolution of F1-ATPase from bovine heart
RT mitochondria.";
RL Nature 370:621-628(1994).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-50 IN COMPLEX WITH ATPIF1;
RP ATP5F1A; ATP5F1B; ATP5F1C AND ATP5F1D.
RX PubMed=17895376; DOI=10.1073/pnas.0707326104;
RA Gledhill J.R., Montgomery M.G., Leslie A.G., Walker J.E.;
RT "How the regulatory protein, IF(1), inhibits F(1)-ATPase from bovine
RT mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15671-15676(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.
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.
CC {ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:17895376,
CC ECO:0000269|PubMed:25851905}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase epsilon family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA34849.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X16978; CAA34849.1; ALT_INIT; mRNA.
DR EMBL; BC108146; AAI08147.1; -; mRNA.
DR PIR; S08239; PWBOE.
DR RefSeq; NP_001137213.1; NM_001143741.1.
DR RefSeq; XP_002697025.2; XM_002696979.4.
DR RefSeq; XP_005193391.1; XM_005193334.3.
DR PDB; 1E79; X-ray; 2.40 A; I=2-51.
DR PDB; 1H8E; X-ray; 2.00 A; I=2-51.
DR PDB; 2CK3; X-ray; 1.95 A; I=2-51.
DR PDB; 2JDI; X-ray; 1.90 A; I=2-51.
DR PDB; 2V7Q; X-ray; 2.10 A; I=2-51.
DR PDB; 2W6H; X-ray; 5.00 A; I=1-51.
DR PDB; 2W6I; X-ray; 4.00 A; I=1-51.
DR PDB; 2W6J; X-ray; 3.84 A; I=1-51.
DR PDB; 2WSS; X-ray; 3.20 A; I/R=2-51.
DR PDB; 2XND; X-ray; 3.50 A; I=2-48.
DR PDB; 4ASU; X-ray; 2.60 A; I=2-51.
DR PDB; 4YXW; X-ray; 3.10 A; I=2-51.
DR PDB; 5ARA; EM; 6.70 A; I=2-51.
DR PDB; 5ARE; EM; 7.40 A; I=2-51.
DR PDB; 5ARH; EM; 7.20 A; I=2-51.
DR PDB; 5ARI; EM; 7.40 A; I=2-51.
DR PDB; 5FIJ; EM; 7.40 A; I=2-51.
DR PDB; 5FIK; EM; 6.40 A; I=2-51.
DR PDB; 5FIL; EM; 7.10 A; I=2-51.
DR PDB; 6YY0; EM; 3.23 A; I=2-51.
DR PDB; 6Z1R; EM; 3.29 A; I=2-51.
DR PDB; 6Z1U; EM; 3.47 A; I=2-51.
DR PDB; 6ZG7; EM; 3.49 A; I=2-51.
DR PDB; 6ZG8; EM; 3.49 A; I=2-51.
DR PDB; 6ZIK; EM; 3.66 A; I=2-51.
DR PDB; 6ZPO; EM; 4.00 A; I=2-51.
DR PDB; 6ZQM; EM; 3.29 A; I=2-51.
DR PDB; 6ZQN; EM; 4.00 A; I=2-51.
DR PDB; 7AJB; EM; 9.20 A; AI/I=2-51.
DR PDB; 7AJC; EM; 11.90 A; AI/I=2-51.
DR PDB; 7AJD; EM; 9.00 A; AI/I=2-51.
DR PDB; 7AJE; EM; 9.40 A; AI/I=2-51.
DR PDB; 7AJF; EM; 8.45 A; AI/I=2-51.
DR PDB; 7AJG; EM; 10.70 A; AI/I=2-51.
DR PDB; 7AJH; EM; 9.70 A; AI/I=2-51.
DR PDB; 7AJI; EM; 11.40 A; AI/I=2-51.
DR PDB; 7AJJ; EM; 13.10 A; AI/I=2-51.
DR PDBsum; 1E79; -.
DR PDBsum; 1H8E; -.
DR PDBsum; 2CK3; -.
DR PDBsum; 2JDI; -.
DR PDBsum; 2V7Q; -.
DR PDBsum; 2W6H; -.
DR PDBsum; 2W6I; -.
DR PDBsum; 2W6J; -.
DR PDBsum; 2WSS; -.
DR PDBsum; 2XND; -.
DR PDBsum; 4ASU; -.
DR PDBsum; 4YXW; -.
DR PDBsum; 5ARA; -.
DR PDBsum; 5ARE; -.
DR PDBsum; 5ARH; -.
DR PDBsum; 5ARI; -.
DR PDBsum; 5FIJ; -.
DR PDBsum; 5FIK; -.
DR PDBsum; 5FIL; -.
DR PDBsum; 6YY0; -.
DR PDBsum; 6Z1R; -.
DR PDBsum; 6Z1U; -.
DR PDBsum; 6ZG7; -.
DR PDBsum; 6ZG8; -.
DR PDBsum; 6ZIK; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P05632; -.
DR SMR; P05632; -.
DR CORUM; P05632; -.
DR DIP; DIP-46312N; -.
DR IntAct; P05632; 7.
DR MINT; P05632; -.
DR STRING; 9913.ENSBTAP00000051455; -.
DR BindingDB; P05632; -.
DR ChEMBL; CHEMBL612444; -.
DR PaxDb; P05632; -.
DR PRIDE; P05632; -.
DR Ensembl; ENSBTAT00000056576; ENSBTAP00000051455; ENSBTAG00000039208.
DR Ensembl; ENSBTAT00000085877; ENSBTAP00000063027; ENSBTAG00000051801.
DR GeneID; 617230; -.
DR KEGG; bta:617230; -.
DR CTD; 514; -.
DR VEuPathDB; HostDB:ENSBTAG00000039208; -.
DR VEuPathDB; HostDB:ENSBTAG00000051801; -.
DR VGNC; VGNC:103015; ATP5F1E.
DR eggNOG; KOG3495; Eukaryota.
DR GeneTree; ENSGT00390000015470; -.
DR HOGENOM; CLU_187039_4_0_1; -.
DR InParanoid; P05632; -.
DR OMA; SQICANA; -.
DR OrthoDB; 1628103at2759; -.
DR TreeFam; TF300278; -.
DR Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-BTA-8949613; Cristae formation.
DR EvolutionaryTrace; P05632; -.
DR PRO; PR:P05632; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000039208; Expressed in semen and 104 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IEA:InterPro.
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 PANTHER; PTHR12448; PTHR12448; 1.
DR Pfam; PF04627; ATP-synt_Eps; 1.
DR SUPFAM; SSF48690; SSF48690; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1827992,
FT ECO:0000269|PubMed:2864455"
FT CHAIN 2..51
FT /note="ATP synthase subunit epsilon, mitochondrial"
FT /id="PRO_0000071661"
FT MOD_RES 21
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56381"
FT MOD_RES 21
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT MOD_RES 37
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:6YY0"
SQ SEQUENCE 51 AA; 5783 MW; E0D70FA7C9191CAE CRC64;
MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAMKTSG STIKIVKVKK E
