ATP7_ARATH
ID ATP7_ARATH Reviewed; 240 AA.
AC Q9SJ12; Q8LBN3;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Probable ATP synthase 24 kDa subunit, mitochondrial;
DE Flags: Precursor;
GN OrderedLocusNames=At2g21870; ORFNames=F7D8.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:AAD20405.1};
RN [1] {ECO:0000312|EMBL:AAD20405.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [2] {ECO:0000305}
RP GENOME REANNOTATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 33-47, 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 [6]
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 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. Part of the complex
CC F(0) domain (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SJ12-1; Sequence=Displayed;
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DR EMBL; AC007019; AAD20405.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07232.1; -; Genomic_DNA.
DR EMBL; AY046020; AAK76694.1; -; mRNA.
DR EMBL; AY079312; AAL85043.1; -; mRNA.
DR EMBL; AY087107; AAM64665.1; -; mRNA.
DR PIR; B84606; B84606.
DR RefSeq; NP_179778.1; NM_127756.4. [Q9SJ12-1]
DR AlphaFoldDB; Q9SJ12; -.
DR SMR; Q9SJ12; -.
DR BioGRID; 2076; 9.
DR IntAct; Q9SJ12; 1.
DR MINT; Q9SJ12; -.
DR STRING; 3702.AT2G21870.1; -.
DR MetOSite; Q9SJ12; -.
DR PaxDb; Q9SJ12; -.
DR PRIDE; Q9SJ12; -.
DR ProteomicsDB; 241041; -. [Q9SJ12-1]
DR EnsemblPlants; AT2G21870.1; AT2G21870.1; AT2G21870. [Q9SJ12-1]
DR GeneID; 816723; -.
DR Gramene; AT2G21870.1; AT2G21870.1; AT2G21870. [Q9SJ12-1]
DR KEGG; ath:AT2G21870; -.
DR Araport; AT2G21870; -.
DR TAIR; locus:2052464; AT2G21870.
DR eggNOG; ENOG502QRUU; Eukaryota.
DR HOGENOM; CLU_101182_0_0_1; -.
DR InParanoid; Q9SJ12; -.
DR OMA; VRFFAKE; -.
DR OrthoDB; 1125663at2759; -.
DR PhylomeDB; Q9SJ12; -.
DR PRO; PR:Q9SJ12; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJ12; baseline and differential.
DR Genevisible; Q9SJ12; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR InterPro; IPR031432; MGP1.
DR PANTHER; PTHR36013; PTHR36013; 1.
DR Pfam; PF15704; Mt_ATP_synt; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:11743114"
FT CHAIN 33..240
FT /note="Probable ATP synthase 24 kDa subunit, mitochondrial"
FT /id="PRO_0000002533"
FT REGION 210..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 15
FT /note="Q -> K (in Ref. 4; AAM64665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 27597 MW; 4A24650B9F0330E7 CRC64;
MAYASRFLSR SKQLQGGLVI LQQQHAIPVR AFAKEAARPT FKGDEMLKGV FFDIKNKFQA
AVDILRKEKI TLDPEDPAAV KQYANVMKTI RQKADMFSES QRIKHDIDTE TQDIPDARAY
LLKLQEIRTR RGLTDELGAE AMMFEALEKV EKDIKKPLLR SDKKGMDLLV AEFEKGNKKL
GIRKEDLPKY EENLELSMAK AQLDELKSDA VEAMESQKKK EEFQDEEMPD VKSLDIRNFI
