ID   ATP9_MAIZE              Reviewed;          74 AA.
AC   P00840;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=ATP synthase subunit 9, mitochondrial;
DE   AltName: Full=Lipid-binding protein;
GN   Name=ATP9;
OS   Zea mays (Maize).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16593542; DOI=10.1073/pnas.82.4.1015;
RA   Dewey R.E., Schuster A.M., Levings C.S. III, Timothy D.H.;
RT   "Nucleotide sequence of F0-ATPase proteolipid (subunit 9) gene of maize
RT   mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:1015-1019(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. B73;
RX   PubMed=2875379; DOI=10.1007/bf00330180;
RA   Bland M.M., Levings C.S. III, Matzinger D.F.;
RT   "The tobacco mitochondrial ATPase subunit 9 gene is closely linked to an
RT   open reading frame for a ribosomal protein.";
RL   Mol. Gen. Genet. 204:8-16(1986).
RN   [3]
RP   RNA EDITING.
RX   PubMed=8662195; DOI=10.1007/bf02426960;
RA   Grosskopf D., Mulligan R.M.;
RT   "Developmental- and tissue-specificity of RNA editing in mitochondria of
RT   suspension-cultured maize cells and seedlings.";
RL   Curr. Genet. 29:556-563(1996).
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:8662195}, 28
CC       {ECO:0000269|PubMed:8662195}, 31 {ECO:0000269|PubMed:8662195}, 45
CC       {ECO:0000269|PubMed:8662195}, 61 {ECO:0000269|PubMed:8662195}, 64
CC       {ECO:0000269|PubMed:8662195}, 71 {ECO:0000269|PubMed:8662195};
CC   -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR   EMBL; M10408; AAA70271.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M18339; AAA70273.1; ALT_SEQ; Genomic_DNA.
DR   PIR; A01041; LWZMA.
DR   AlphaFoldDB; P00840; -.
DR   SMR; P00840; -.
DR   MaizeGDB; 69203; -.
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_0000112214"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..72
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