ID   AT5G2_PONAB             Reviewed;         141 AA.
AC   Q5RAP9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=ATP synthase F(0) complex subunit C2, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase lipid-binding protein;
DE   AltName: Full=ATP synthase membrane subunit c locus 2 {ECO:0000250|UniProtKB:Q06055};
DE   AltName: Full=ATP synthase proteolipid P2;
DE   AltName: Full=ATPase protein 9;
DE   AltName: Full=ATPase subunit c;
DE   Flags: Precursor;
GN   Name=ATP5MC2 {ECO:0000250|UniProtKB:Q06055}; Synonyms=ATP5G2;
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=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 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. A homomeric c-ring of probably 10 subunits is part of the
CC       complex rotary element.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c. Interacts with DNAJC30; interaction is direct.
CC       {ECO:0000250|UniProtKB:Q06055}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Trimethylated by ATPSCKMT at Lys-109. Methylation is required for
CC       proper incorporation of the C subunit into the ATP synthase complex and
CC       mitochondrial respiration. {ECO:0000250|UniProtKB:Q06055}.
CC   -!- DISEASE: Note=This protein is the major protein stored in the storage
CC       bodies of animals or humans affected with ceroid lipofuscinosis (Batten
CC       disease).
CC   -!- MISCELLANEOUS: There are three genes which encode the mitochondrial ATP
CC       synthase proteolipid and they specify precursors with different import
CC       sequences but identical mature proteins. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR   EMBL; CR858965; CAH91161.1; -; mRNA.
DR   RefSeq; NP_001125678.1; NM_001132206.2.
DR   AlphaFoldDB; Q5RAP9; -.
DR   SMR; Q5RAP9; -.
DR   STRING; 9601.ENSPPYP00000005231; -.
DR   GeneID; 100172599; -.
DR   KEGG; pon:100172599; -.
DR   CTD; 517; -.
DR   eggNOG; KOG3025; Eukaryota.
DR   InParanoid; Q5RAP9; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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; 1.20.20.10; -; 1.
DR   HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR   InterPro; IPR000454; ATP_synth_F0_csu.
DR   InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR   InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR   InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR   InterPro; IPR035921; F/V-ATP_Csub_sf.
DR   PANTHER; PTHR10031; PTHR10031; 1.
DR   Pfam; PF00137; ATP-synt_C; 1.
DR   PRINTS; PR00124; ATPASEC.
DR   SUPFAM; SSF81333; SSF81333; 1.
DR   PROSITE; PS00605; ATPASE_C; 1.
PE   2: Evidence at transcript level;
KW   CF(0); Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
KW   Methylation; Mitochondrion; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..66
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           67..141
FT                   /note="ATP synthase F(0) complex subunit C2, mitochondrial"
FT                   /id="PRO_0000002564"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            124
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         109
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q06055"
SQ   SEQUENCE   141 AA;  14807 MW;  2E1F99866050E2E1 CRC64;
     MFSCFKFIST PSLVKSTSQL LSRPLSAVVL KRPEILTDES LSSLAVSRPL TSLVSSRNFQ
     TSAISRDIDT AAKFIGAGAA TVGVAGSGAG IGTVFGSLII GYARNPSLKQ QLFSYAILGF
     ALSEAMGLFC LMVAFLILFA M