ID   ATP9_ORYSJ              Reviewed;          74 AA.
AC   P0C519; P14863; Q7JAI7;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=ATP synthase subunit 9, mitochondrial;
DE   AltName: Full=Lipid-binding protein;
GN   Name=ATP9;
OS   Oryza sativa subsp. japonica (Rice).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12471441; DOI=10.1007/s00438-002-0767-1;
RA   Notsu Y., Masood S., Nishikawa T., Kubo N., Akiduki G., Nakazono M.,
RA   Hirai A., Kadowaki K.;
RT   "The complete sequence of the rice (Oryza sativa L.) mitochondrial genome:
RT   frequent DNA sequence acquisition and loss during the evolution of
RT   flowering plants.";
RL   Mol. Genet. Genomics 268:434-445(2002).
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- RNA EDITING: Modified_positions=7 {ECO:0000269|PubMed:12471441}, 20
CC       {ECO:0000269|PubMed:12471441}, 28 {ECO:0000269|PubMed:12471441}, 31
CC       {ECO:0000269|PubMed:12471441}, 64 {ECO:0000269|PubMed:12471441}, 71
CC       {ECO:0000269|PubMed:12471441}, 75 {ECO:0000269|PubMed:12471441};
CC       Note=The stop codon at position 75 is created by RNA editing.;
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR   EMBL; BA000029; BAC19885.1; -; Genomic_DNA.
DR   RefSeq; YP_002000580.1; NC_011033.1.
DR   AlphaFoldDB; P0C519; -.
DR   SMR; P0C519; -.
DR   STRING; 4530.OS01T0899275-00; -.
DR   PRIDE; P0C519; -.
DR   GeneID; 6450130; -.
DR   KEGG; osa:6450130; -.
DR   eggNOG; ENOG502S4GY; Eukaryota.
DR   InParanoid; P0C519; -.
DR   OrthoDB; 1564365at2759; -.
DR   Proteomes; UP000059680; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IC:Gramene.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome;
KW   RNA editing; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..74
FT                   /note="ATP synthase subunit 9, mitochondrial"
FT                   /id="PRO_0000290115"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            57
FT                   /note="Reversibly protonated during proton transport"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   74 AA;  7557 MW;  CA932F847058F5E3 CRC64;
     MLEGAKLIGA GAATIALAGA AVGIGNVFSS LIHSVARNPS LAKQLFGYAI LGFALTEAIA
     LFALMMAFLI LFVF