ATPAM_ARATH
ID ATPAM_ARATH Reviewed; 507 AA.
AC P92549; Q1NZ05; Q8S890;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN Name=ATPA; Synonyms=ATP1; OrderedLocusNames=AtMg01190;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT2G07698).
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 [3]
RP PROTEIN SEQUENCE OF 1-13, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
RN [4]
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
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
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits. Subunit
CC alpha does not bear the catalytic high-affinity ATP-binding sites.
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 {ECO:0000269|PubMed:11743114,
CC ECO:0000269|PubMed:14671022}. Mitochondrion inner membrane
CC {ECO:0000305}. Note=Peripheral membrane protein. {ECO:0000305}.
CC -!- RNA EDITING: Modified_positions=393 {ECO:0000269|PubMed:10611383}, 431
CC {ECO:0000269|PubMed:10611383}, 472 {ECO:0000269|PubMed:10611383}, 495
CC {ECO:0000269|PubMed:10611383};
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 (At2g07698) 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 alpha/beta chains family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM15496.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y08501; CAA69802.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007729; AAM15496.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_085571.2; NC_001284.2.
DR AlphaFoldDB; P92549; -.
DR SMR; P92549; -.
DR BioGRID; 566531; 6.
DR IntAct; P92549; 1.
DR MINT; P92549; -.
DR STRING; 3702.ATMG01190.1; -.
DR SWISS-2DPAGE; P92549; -.
DR PaxDb; P92549; -.
DR PeptideAtlas; P92549; -.
DR PRIDE; P92549; -.
DR ProteomicsDB; 246593; -.
DR Araport; ATMG01190; -.
DR eggNOG; KOG1353; Eukaryota.
DR InParanoid; P92549; -.
DR OrthoDB; 470054at2759; -.
DR BioCyc; ARA:ATMG01190-MON; -.
DR PRO; PR:P92549; -.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; P92549; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW RNA editing; Transport.
FT CHAIN 1..507
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_0000144395"
FT BINDING 171..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 373
FT /note="Required for activity"
FT /evidence="ECO:0000250"
FT CONFLICT 172
FT /note="G -> D (in Ref. 2; AAM15496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 55045 MW; 1927B3B8E1EFF51E CRC64;
MELSPRAAEL TNLFESRIRN FYANFQVDEI GRVVSVGDGI AQVYGLNEIQ AGEMVLFANG
VKGMALNLEN ENVGIVVFGG DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DAMGVPIDGK
GALSDHEQRR VEVKAPGILE RKSVHEPMQT GLKAVDSLVP IGRGQRELLI GGRQTGKTTI
AIDTILNQKQ INSRATSESE TMYCVYVAIG QKRSTVGQLI QTLEEANALE YSILVAATAS
DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD
VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVISITD GQICLETELF
YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSLKLELAQY REVAAFAQFG SDLDAATQAL
LNRGARLTEV LKQPQYAPLP IEKQILVIYA AVNGFCDRMP LDRISQYEKA ILNSVKPELL
QALKGGLTNE RKMELDAFLK ERALALI
