ATP5I_BOVIN
ID ATP5I_BOVIN Reviewed; 71 AA.
AC Q00361; Q3T0S4;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ATP synthase subunit e, mitochondrial {ECO:0000305};
DE Short=ATPase subunit e;
DE AltName: Full=ATP synthase membrane subunit e {ECO:0000305};
GN Name=ATP5ME {ECO:0000250|UniProtKB:P56385}; Synonyms=ATP5I;
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], AND PROTEIN SEQUENCE OF 2-36.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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).
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(0) domain. Minor subunit located with subunit a in the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
CC ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC ATP5PO, ATP5MG, ATP5MK and ATP5MJ. {ECO:0000269|PubMed:17570365,
CC ECO:0000269|PubMed:25851905}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR EMBL; M64751; AAA30390.1; -; mRNA.
DR EMBL; BC102279; AAI02280.1; -; mRNA.
DR PIR; A39566; A39566.
DR RefSeq; NP_788812.1; NM_176639.2.
DR PDB; 6ZBB; EM; 3.61 A; e=2-71.
DR PDB; 6ZIQ; EM; 4.33 A; e=2-71.
DR PDB; 6ZIT; EM; 3.49 A; e=2-71.
DR PDB; 6ZIU; EM; 6.02 A; e=2-71.
DR PDB; 6ZPO; EM; 4.00 A; e=2-71.
DR PDB; 6ZQM; EM; 3.29 A; e=2-71.
DR PDB; 6ZQN; EM; 4.00 A; e=2-71.
DR PDB; 7AJB; EM; 9.20 A; Ae/e=2-71.
DR PDB; 7AJC; EM; 11.90 A; Ae/e=2-71.
DR PDB; 7AJD; EM; 9.00 A; Ae/e=2-71.
DR PDB; 7AJE; EM; 9.40 A; Ae/e=2-71.
DR PDB; 7AJF; EM; 8.45 A; Ae/e=2-71.
DR PDB; 7AJG; EM; 10.70 A; Ae/e=2-71.
DR PDB; 7AJH; EM; 9.70 A; Ae/e=2-71.
DR PDB; 7AJI; EM; 11.40 A; Ae/e=2-71.
DR PDB; 7AJJ; EM; 13.10 A; Ae/e=2-71.
DR PDBsum; 6ZBB; -.
DR PDBsum; 6ZIQ; -.
DR PDBsum; 6ZIT; -.
DR PDBsum; 6ZIU; -.
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; Q00361; -.
DR SMR; Q00361; -.
DR CORUM; Q00361; -.
DR IntAct; Q00361; 3.
DR MINT; Q00361; -.
DR STRING; 9913.ENSBTAP00000023255; -.
DR PaxDb; Q00361; -.
DR PeptideAtlas; Q00361; -.
DR PRIDE; Q00361; -.
DR Ensembl; ENSBTAT00000023255; ENSBTAP00000023255; ENSBTAG00000017496.
DR GeneID; 338040; -.
DR KEGG; bta:338040; -.
DR CTD; 521; -.
DR VEuPathDB; HostDB:ENSBTAG00000017496; -.
DR VGNC; VGNC:104569; ATP5ME.
DR eggNOG; KOG4326; Eukaryota.
DR GeneTree; ENSGT00390000005102; -.
DR HOGENOM; CLU_180903_0_0_1; -.
DR InParanoid; Q00361; -.
DR OMA; GAFHQNR; -.
DR OrthoDB; 1640426at2759; -.
DR TreeFam; TF314719; -.
DR Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-BTA-8949613; Cristae formation.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000017496; Expressed in tongue muscle and 106 other tissues.
DR ExpressionAtlas; Q00361; baseline.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR PANTHER; PTHR12427; PTHR12427; 1.
DR Pfam; PF05680; ATP-synt_E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; CF(0); 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 CHAIN 2..71
FT /note="ATP synthase subunit e, mitochondrial"
FT /id="PRO_0000071682"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q06185"
FT HELIX 9..42
FT /evidence="ECO:0007829|PDB:6ZIT"
SQ SEQUENCE 71 AA; 8321 MW; 18E63DB09EF1A132 CRC64;
MVPPVQVSPL IKLGRYSALF LGMAYGAKRY NYLKPRAEEE RRLAAEEKKK RDEQKRIERE
LAEAQEDTIL K