ID   ATP9_BRANA              Reviewed;          74 AA.
AC   P60113; Q08366;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ATP synthase subunit 9, mitochondrial;
DE   AltName: Full=Lipid-binding protein;
GN   Name=ATP9;
OS   Brassica napus (Rape).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Isuzu-natane;
RX   PubMed=8318255; DOI=10.1266/jjg.68.47;
RA   Handa H.;
RT   "RNA editing of rapeseed mitochondrial atp9 transcripts: RNA editing
RT   changes four amino acids, but termination codon is already encoded by
RT   genomic sequence.";
RL   Jpn. J. Genet. 68:47-54(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RA   Albaum M., Abel W.O.;
RL   Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is one of the chains of the nonenzymatic
CC       membrane component (F0) of mitochondrial ATPase.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- RNA EDITING: Modified_positions=7, 17, 45, 64;
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR   EMBL; D13696; BAA02855.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; X69319; CAA49160.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P60113; -.
DR   SMR; P60113; -.
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:0005524; F:ATP binding; 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   ATP-binding; CF(0); Hydrogen ion transport; Ion transport; Lipid-binding;
KW   Membrane; Mitochondrion; Nucleotide-binding; RNA editing; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..74
FT                   /note="ATP synthase subunit 9, mitochondrial"
FT                   /id="PRO_0000112210"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   SITE            57
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   74 AA;  7477 MW;  A68C2BFAFAC27B2F CRC64;
     MLEGAKSIGA GAATIASAGA AIGIGNVFSS LIHSVARNPS LAKQSFGYAI LGFALTEAIA
     LFAPMMAFLI LFVF