ATP9_ARATH
ID ATP9_ARATH Reviewed; 85 AA.
AC P60112; A7KNE9; Q08366; Q8S875;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ATP synthase subunit 9, mitochondrial;
DE AltName: Full=Lipid-binding protein;
GN Name=ATP9; OrderedLocusNames=AtMg01080;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8776901; DOI=10.2307/3870308;
RA Sakamoto W., Kondo H., Murata M., Motoyoshi F.;
RT "Altered mitochondrial gene expression in a maternal distorted leaf mutant
RT of Arabidopsis induced by chloroplast mutator.";
RL Plant Cell 8:1377-1390(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. C24;
RX PubMed=8988169; DOI=10.1038/ng0197-57;
RA Unseld M., Marienfeld J.R., Brandt P., Brennicke A.;
RT "The mitochondrial genome of Arabidopsis thaliana contains 57 genes in
RT 366,924 nucleotides.";
RL Nat. Genet. 15:57-61(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT2G07671).
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-78, AND RNA EDITING.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta; TISSUE=Rosette leaf;
RX PubMed=17565941; DOI=10.1534/genetics.107.073585;
RA Bentolila S., Elliott L.E., Hanson M.R.;
RT "Genetic architecture of mitochondrial editing in Arabidopsis thaliana.";
RL Genetics 178:1693-1708(2008).
RN [5]
RP RNA EDITING.
RX PubMed=10611383; DOI=10.1073/pnas.96.26.15324;
RA Giege P., Brennicke A.;
RT "RNA editing in Arabidopsis mitochondria effects 441 C to U changes in
RT ORFs.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15324-15329(1999).
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=18 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 28 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 56 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 75 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941};
CC -!- MISCELLANEOUS: A stretch of 270 kb of the mitochondrial genome is
CC duplicated within the centromere of chromosome 2 resulting in the
CC duplication of the gene. The expression of this duplicated gene
CC (At2g07671) is not demonstrated. It is also probably not RNA edited and
CC therefore differs in all the positions known to be edited.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM15515.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D82062; BAA11530.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Y08501; CAA69793.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007730; AAM15515.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EF488892; ABS50604.1; -; mRNA.
DR EMBL; EF488893; ABS50605.1; -; mRNA.
DR RefSeq; NP_085561.2; NC_001284.2.
DR RefSeq; NP_178769.2; NM_126728.3.
DR AlphaFoldDB; P60112; -.
DR SMR; P60112; -.
DR IntAct; P60112; 2.
DR STRING; 3702.AT2G07671.1; -.
DR PaxDb; P60112; -.
DR PeptideAtlas; P60112; -.
DR GeneID; 815343; -.
DR KEGG; ath:AT2G07671; -.
DR Araport; ATMG01080; -.
DR eggNOG; ENOG502S4GY; Eukaryota.
DR InParanoid; P60112; -.
DR OrthoDB; 1564365at2759; -.
DR PRO; PR:P60112; -.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; P60112; baseline and differential.
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: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..85
FT /note="ATP synthase subunit 9, mitochondrial"
FT /id="PRO_0000112208"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000250"
FT SITE 68
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 85 AA; 8936 MW; D95420E7A0BDB9C7 CRC64;
MTKREYNSQP EMLEGAKLIG AGAATIALAG AAIGIGNVFS SLIHSVARNP SLAKQLFGYA
ILGFALTEAI ALFALMMAFL ILFVF
