ATP61_ARATH
ID ATP61_ARATH Reviewed; 385 AA.
AC P93298; A7KNE5; F4INF7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=ATP synthase subunit a-1;
DE AltName: Full=F-ATPase protein 6;
DE AltName: Full=P6-1;
DE Flags: Precursor;
GN Name=ATP6-1; OrderedLocusNames=AtMg00410 {ECO:0000312|Araport:ATMG00410};
GN and
GN OrderedLocusNames=At2g07741 {ECO:0000312|Araport:AT2G07741};
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], AND RNA EDITING.
RC STRAIN=cv. Columbia;
RX PubMed=9039497; DOI=10.1093/dnares/3.5.287;
RA Marienfeld J.R., Unseld M., Brandt P., Brennicke A.;
RT "Genomic recombination of the mitochondrial atp6 gene in Arabidopsis
RT thaliana at the protein processing site creates two different
RT presequences.";
RL DNA Res. 3:287-290(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 [GENOMIC DNA], AND 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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. C24, cv. Columbia, and cv. Landsberg erecta;
RX PubMed=21951689; DOI=10.1186/1741-7007-9-64;
RA Davila J.I., Arrieta-Montiel M.P., Wamboldt Y., Cao J., Hagmann J.,
RA Shedge V., Xu Y.Z., Weigel D., Mackenzie S.A.;
RT "Double-strand break repair processes drive evolution of the mitochondrial
RT genome in Arabidopsis.";
RL BMC Biol. 9:64-64(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT2G07741).
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 [6]
RP GENOME REANNOTATION (AT2G07741).
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-316, 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).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core and F(0)
CC - containing the membrane proton channel, linked together by a central
CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC catalytic domain of F(1) is coupled via a rotary mechanism of the
CC central stalk subunits to proton translocation. Key component of the
CC proton channel; it may play a direct role in the translocation of
CC protons across the membrane (By similarity). {ECO:0000250}.
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 inner membrane; Multi-pass membrane
CC protein.
CC -!- RNA EDITING: Modified_positions=159 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941, ECO:0000269|PubMed:9039497};
CC -!- MISCELLANEOUS: The atp6 gene is located on the border of one of the
CC mitochondrial DNA repeats resulting in two identical copies of the
CC mature protein with different propeptide extensions.
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 (At2g07741) 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 A chain family. {ECO:0000305}.
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DR EMBL; Y08501; CAA69778.3; ALT_SEQ; Genomic_DNA.
DR EMBL; JF729200; AEK01254.1; ALT_SEQ; Genomic_DNA.
DR EMBL; JF729201; AEK01282.1; ALT_SEQ; Genomic_DNA.
DR EMBL; JF729202; AEK01327.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC006225; AAM15167.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06126.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EF488888; ABS50600.1; -; mRNA.
DR EMBL; EF488889; ABS50601.1; -; mRNA.
DR RefSeq; NP_085503.1; NC_001284.2.
DR RefSeq; NP_178810.1; NM_126768.1.
DR AlphaFoldDB; P93298; -.
DR SMR; P93298; -.
DR IntAct; P93298; 1.
DR STRING; 3702.AT2G07741.1; -.
DR PaxDb; P93298; -.
DR GeneID; 815413; -.
DR KEGG; ath:AT2G07741; -.
DR Araport; AT2G07741; -.
DR Araport; ATMG00410; -.
DR eggNOG; KOG4665; Eukaryota.
DR HOGENOM; CLU_041018_0_3_1; -.
DR InParanoid; P93298; -.
DR OrthoDB; 1095315at2759; -.
DR PhylomeDB; P93298; -.
DR PRO; PR:P93298; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; P93298; differential.
DR Genevisible; P93298; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); 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; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 2: Evidence at transcript level;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW RNA editing; Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..133
FT /id="PRO_0000002602"
FT CHAIN 134..385
FT /note="ATP synthase subunit a-1"
FT /id="PRO_0000002603"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 385 AA; 42342 MW; F171DB0D3B0D7129 CRC64;
MRRIFLFDEN SLNSSSTIDT SSASTIDTSF ASQCTNFSSG QASGTQDTHA GIFEDCPGLN
PNDERVVELQ CEIREKCEAL TQDPEMGLIL GEALHAESDN VPFLQSIADD LTQNGVSGEA
FQEALNIVGQ AAASPLDQFE IVPLIPMHIG NFYFSFTNSS LFMLLTLSFF LLLIHFVTKK
GGGNLVPNAW QSLVELLYDF VLNLVKEQIG GLSGNVKQMF FPCILVTFLF LLFCNLQGMI
PYSFTVTSHF LITLALSFSI FIGITIVGFQ RHGLHFFSFL LPAGVPLPLA PFLVLLELIS
YCFRALSLGI RLFANMMAGH SLVKILSGFA WTMLCMNDIF YFIGALGPLF IVLALTGLEL
GVAILQAYVF TILICIYLND AINLH
