ATP5E_RAT
ID ATP5E_RAT Reviewed; 51 AA.
AC P29418;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=ATP synthase subunit epsilon, mitochondrial {ECO:0000305};
DE Short=ATPase subunit epsilon;
DE AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000312|RGD:621374};
GN Name=Atp5f1e {ECO:0000312|RGD:621374}; Synonyms=Atp5e;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lo Piero A.R., Pedersen P.L.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-51.
RC TISSUE=Liver;
RX PubMed=1429613; DOI=10.1016/s0021-9258(18)41722-x;
RA Higuti T., Yoshihara Y., Kuroiwa K., Kawamura Y., Toda H., Sakiyama F.;
RT "A simple, rapid method for purification of epsilon-subunit, coupling
RT factor 6, subunit d, and subunit e from rat liver H(+)-ATP synthase and
RT determination of the complete amino acid sequence of epsilon-subunit.";
RL J. Biol. Chem. 267:22658-22661(1992).
RN [4]
RP PROTEIN SEQUENCE OF 2-25.
RA Godinot C.;
RL Submitted (FEB-1991) to the PIR data bank.
RN [5]
RP PROTEIN SEQUENCE OF 7-14, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=17575325; DOI=10.1074/mcp.m700097-mcp200;
RA Meyer B., Wittig I., Trifilieff E., Karas M., Schaegger H.;
RT "Identification of two proteins associated with mammalian ATP synthase.";
RL Mol. Cell. Proteomics 6:1690-1699(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:17575325}.
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; AF010323; AAB64162.1; -; mRNA.
DR EMBL; BC058133; AAH58133.1; -; mRNA.
DR PIR; B44300; B44300.
DR RefSeq; NP_620799.1; NM_139099.1.
DR AlphaFoldDB; P29418; -.
DR CORUM; P29418; -.
DR STRING; 10116.ENSRNOP00000067815; -.
DR iPTMnet; P29418; -.
DR PhosphoSitePlus; P29418; -.
DR jPOST; P29418; -.
DR PaxDb; P29418; -.
DR PRIDE; P29418; -.
DR GeneID; 245958; -.
DR KEGG; rno:245958; -.
DR CTD; 514; -.
DR RGD; 621374; Atp5f1e.
DR VEuPathDB; HostDB:ENSRNOG00000049912; -.
DR eggNOG; KOG3495; Eukaryota.
DR HOGENOM; CLU_187039_4_0_1; -.
DR InParanoid; P29418; -.
DR OMA; SQICANA; -.
DR OrthoDB; 1628103at2759; -.
DR PhylomeDB; P29418; -.
DR PRO; PR:P29418; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000049912; Expressed in heart and 20 other tissues.
DR Genevisible; P29418; RN.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
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); IDA:RGD.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0046034; P:ATP metabolic process; IDA:RGD.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:RGD.
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); 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:1429613, ECO:0000269|Ref.4"
FT CHAIN 2..51
FT /note="ATP synthase subunit epsilon, mitochondrial"
FT /id="PRO_0000071664"
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"
SQ SEQUENCE 51 AA; 5767 MW; DB51D26E4AA136C4 CRC64;
MVAYWRQAGL SYIRFSQICA KAVRDALKTE FKANAEKTSG TSIKTVKIKK E
