ID   ATP5I_PONAB             Reviewed;          71 AA.
AC   Q5RBW2;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 87.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase e subunit family. {ECO:0000305}.
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DR   EMBL; CR857527; CAH89809.1; -; mRNA.
DR   EMBL; CR858521; CAH90748.1; -; mRNA.
DR   RefSeq; NP_001124837.1; NM_001131365.1.
DR   AlphaFoldDB; Q5RBW2; -.
DR   SMR; Q5RBW2; -.
DR   STRING; 9601.ENSPPYP00000016213; -.
DR   Ensembl; ENSPPYT00000016866; ENSPPYP00000016213; ENSPPYG00000014505.
DR   GeneID; 100171695; -.
DR   KEGG; pon:100171695; -.
DR   CTD; 521; -.
DR   eggNOG; KOG4326; Eukaryota.
DR   GeneTree; ENSGT00390000005102; -.
DR   HOGENOM; CLU_180903_0_0_1; -.
DR   InParanoid; Q5RBW2; -.
DR   OMA; GAFHQNR; -.
DR   OrthoDB; 1640426at2759; -.
DR   TreeFam; TF314719; -.
DR   Proteomes; UP000001595; Chromosome 4.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IEA:Ensembl.
DR   InterPro; IPR008386; ATP_synth_F0_esu_mt.
DR   PANTHER; PTHR12427; PTHR12427; 1.
DR   Pfam; PF05680; ATP-synt_E; 1.
PE   3: Inferred from homology;
KW   Acetylation; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Reference proteome; Transport.
FT   CHAIN           1..71
FT                   /note="ATP synthase subunit e, mitochondrial"
FT                   /id="PRO_0000071687"
FT   MOD_RES         34
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06185"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29419"
SQ   SEQUENCE   71 AA;  8132 MW;  08E3E78DB16A5332 CRC64;
     MVPPVQVSPL IKLGRYSALF LGVAYGATRY NYLKPRAEEE RRIAAEEKKK QDELKRIARE
     LAEAQDDSIL K