ID   ATP5L_PONAB             Reviewed;         103 AA.
AC   Q5RFH0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=ATP synthase subunit g, mitochondrial {ECO:0000305};
DE            Short=ATPase subunit g;
DE   AltName: Full=ATP synthase membrane subunit g {ECO:0000305};
GN   Name=ATP5MG {ECO:0000250|UniProtKB:O75964}; Synonyms=ATP5L;
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;
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 g subunit family. {ECO:0000305}.
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DR   EMBL; CR857188; CAH89487.1; -; mRNA.
DR   RefSeq; NP_001124640.1; NM_001131168.2.
DR   AlphaFoldDB; Q5RFH0; -.
DR   SMR; Q5RFH0; -.
DR   STRING; 9601.ENSPPYP00000004504; -.
DR   GeneID; 100171481; -.
DR   KEGG; pon:100171481; -.
DR   CTD; 10632; -.
DR   eggNOG; KOG4103; Eukaryota.
DR   InParanoid; Q5RFH0; -.
DR   OrthoDB; 1461139at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   InterPro; IPR006808; ATP_synth_F0_gsu_mt.
DR   InterPro; IPR016702; ATP_synth_su_G_mt_met.
DR   PANTHER; PTHR12386; PTHR12386; 1.
DR   Pfam; PF04718; ATP-synt_G; 1.
DR   PIRSF; PIRSF017835; ATP-synth_g_mitoch_animal; 1.
PE   3: Inferred from homology;
KW   Acetylation; ATP synthesis; CF(0); 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:0000250|UniProtKB:O75964"
FT   CHAIN           2..103
FT                   /note="ATP synthase subunit g, mitochondrial"
FT                   /id="PRO_0000071693"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O75964"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPQ8"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O75964"
FT   MOD_RES         35
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPQ8"
FT   MOD_RES         54
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPQ8"
SQ   SEQUENCE   103 AA;  11398 MW;  03D484A78EED9002 CRC64;
     MAQFVRNLVE KTPALVNAAV TYSKPRLATF WYYAKVELVP PTPAEIPRAI QGLKKIVNSA
     QTGSFKQLTV KEAVLNGLVA TEVLMWFYVG EIIGKRGIIG YDV