ID   ATP5J_PONAB             Reviewed;         107 AA.
AC   Q5RBY3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=ATP synthase-coupling factor 6, mitochondrial {ECO:0000305};
DE            Short=ATPase subunit F6;
DE   AltName: Full=ATP synthase peripheral stalk subunit F6 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ATP5PF {ECO:0000250|UniProtKB:P18859}; Synonyms=ATP5J;
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 F(0)
CC       - containing the membrane proton channel, linked together by a central
CC       stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC       catalytic domain of F(1) is coupled via a rotary mechanism of the
CC       central stalk subunits to proton translocation. Part of the complex
CC       F(0) domain and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements. Also involved in the restoration of
CC       oligomycin-sensitive ATPase activity to depleted F1-F0 complexes (By
CC       similarity). {ECO:0000250}.
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 eukaryotic ATPase subunit F6 family.
CC       {ECO:0000305}.
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DR   EMBL; CR858499; CAH90727.1; -; mRNA.
DR   RefSeq; NP_001125405.1; NM_001131933.1.
DR   AlphaFoldDB; Q5RBY3; -.
DR   SMR; Q5RBY3; -.
DR   STRING; 9601.ENSPPYP00000012627; -.
DR   Ensembl; ENSPPYT00000046854; ENSPPYP00000038049; ENSPPYG00000011305.
DR   GeneID; 100172310; -.
DR   KEGG; pon:100172310; -.
DR   CTD; 522; -.
DR   eggNOG; KOG4634; Eukaryota.
DR   GeneTree; ENSGT00390000008902; -.
DR   HOGENOM; CLU_145649_1_0_1; -.
DR   InParanoid; Q5RBY3; -.
DR   OMA; PKFEVFD; -.
DR   OrthoDB; 1559269at2759; -.
DR   TreeFam; TF318998; -.
DR   Proteomes; UP000001595; Chromosome 21.
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   Gene3D; 1.10.246.110; -; 1.
DR   InterPro; IPR008387; ATP_synth_f6_mt.
DR   InterPro; IPR036204; ATP_synth_f6_sf_mt.
DR   PANTHER; PTHR12441; PTHR12441; 1.
DR   Pfam; PF05511; ATP-synt_F6; 1.
DR   PIRSF; PIRSF002455; ATP_synthase_coupling_factor_6; 1.
DR   SUPFAM; SSF111357; SSF111357; 1.
PE   3: Inferred from homology;
KW   Acetylation; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transit peptide; Transport.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           32..107
FT                   /note="ATP synthase-coupling factor 6, mitochondrial"
FT                   /id="PRO_0000002530"
FT   MOD_RES         40
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P18859"
FT   MOD_RES         45
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P18859"
FT   MOD_RES         78
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P97450"
FT   MOD_RES         93
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P97450"
FT   MOD_RES         93
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P97450"
FT   MOD_RES         98
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P18859"
FT   MOD_RES         98
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P97450"
FT   MOD_RES         104
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P18859"
SQ   SEQUENCE   107 AA;  12448 MW;  2122226CF61D7C8B CRC64;
     MILQRLFRFS VIRSAVSVYL RRNIGVTAVA FNKELDPIQK LFVDKIREYK SKRQTSGGPV
     DAGPEYQQEL EKELFKLKQM FGNADMNTFP AFKFEDPKFE VIEKPQA