ID   ATPK_PONAB              Reviewed;          94 AA.
AC   Q5R6T5;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=ATP synthase subunit f, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase membrane subunit f {ECO:0000305};
GN   Name=ATP5MF {ECO:0000250|UniProtKB:P56134}; Synonyms=ATP5J2;
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=Brain cortex;
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. Minor subunit located with subunit a in the membrane (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 {ECO:0000250}. Mitochondrion inner
CC       membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase F chain family. {ECO:0000305}.
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DR   EMBL; CR860399; CAH92525.1; -; mRNA.
DR   RefSeq; NP_001126480.1; NM_001133008.2.
DR   AlphaFoldDB; Q5R6T5; -.
DR   STRING; 9601.ENSPPYP00000019473; -.
DR   GeneID; 100173467; -.
DR   KEGG; pon:100173467; -.
DR   CTD; 9551; -.
DR   eggNOG; KOG4092; Eukaryota.
DR   InParanoid; Q5R6T5; -.
DR   OrthoDB; 1479342at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019344; F1F0-ATPsyn_F_prd.
DR   PANTHER; PTHR13080; PTHR13080; 1.
DR   Pfam; PF10206; WRW; 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; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P56134"
FT   CHAIN           2..94
FT                   /note="ATP synthase subunit f, mitochondrial"
FT                   /id="PRO_0000194827"
FT   TRANSMEM        63..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P56134"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:D3ZAF6"
FT   MOD_RES         22
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P56135"
SQ   SEQUENCE   94 AA;  10971 MW;  94E0C84363DFF89C CRC64;
     MASVGERPAP VPVKDKKLLE VKLGELPSWI LMRDFSPSGI FGAFQRGYYR YYNKYINVKK
     GSISGITMVL ACYVLFSYSF SYKHLKHERL RKYH