ID   ATP9_WHEAT              Reviewed;          74 AA.
AC   P13547;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 3.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=ATP synthase subunit 9, mitochondrial;
DE   AltName: Full=Lipid-binding protein;
GN   Name=ATP9;
OS   Triticum aestivum (Wheat).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2529479; DOI=10.1093/nar/17.18.7531;
RA   Schulte E., Staubach S., Laser B., Kueck U.;
RT   "Wheat mitochondrial DNA: organization and sequences of the atpA and atp9
RT   genes.";
RL   Nucleic Acids Res. 17:7531-7531(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Thatcher;
RX   PubMed=2535257; DOI=10.1007/bf00015551;
RA   Bonhomme S., Bird S., Bonen L.;
RT   "Comparison of the wheat mitochondrial atp9 gene sequence with
RT   mitochondrial and chloroplast homologues from other plants.";
RL   Plant Mol. Biol. 13:395-397(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1702206; DOI=10.1093/nar/18.23.7164;
RA   Nowak C., Kueck U.;
RT   "RNA editing of the mitochondrial atp9 transcript from wheat.";
RL   Nucleic Acids Res. 18:7164-7164(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 67-74.
RX   PubMed=1726783; DOI=10.2307/3869346;
RA   Begu D., Graves P.V., Domec C., Arselin G., Litvak S., Araya A.;
RT   "RNA editing of wheat mitochondrial ATP synthase subunit 9: direct protein
RT   and cDNA sequencing.";
RL   Plant Cell 2:1283-1290(1990).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-32.
RX   PubMed=2196374; DOI=10.1016/0022-2836(90)90138-c;
RA   Graves P.V., Begu D., Velours J., Neau E., Belloc F., Litvak S., Araya A.;
RT   "Direct protein sequencing of wheat mitochondrial ATP synthase subunit 9
RT   confirms RNA editing in plants.";
RL   J. Mol. Biol. 214:1-6(1990).
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, 28, 45, 64, 71, 75; Note=The stop
CC       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; X15919; CAA34061.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X15083; CAA33193.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X54621; CAA38441.1; -; mRNA.
DR   EMBL; S47364; AAB23976.1; -; mRNA.
DR   PIR; S12631; LWWTM.
DR   RefSeq; YP_398394.1; NC_007579.1.
DR   AlphaFoldDB; P13547; -.
DR   SMR; P13547; -.
DR   STRING; 4565.EPlTAEP00000010113; -.
DR   eggNOG; ENOG502S4GY; Eukaryota.
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   1: Evidence at protein level;
KW   ATP-binding; CF(0); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Lipid-binding; Membrane; Mitochondrion; Nucleotide-binding;
KW   RNA editing; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..74
FT                   /note="ATP synthase subunit 9, mitochondrial"
FT                   /id="PRO_0000112226"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
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