ATP6A_ARATH
ID ATP6A_ARATH Reviewed; 55 AA.
AC P0DO44; A0A178V8C6; Q9SN96;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=ATP synthase small subunit 6-A, mitochondrial {ECO:0000303|PubMed:18338219, ECO:0000303|PubMed:23096681};
DE Short=AtMtATP6 {ECO:0000303|PubMed:18338219, ECO:0000303|PubMed:23096681};
DE Short=MtATP6 {ECO:0000303|PubMed:18338219, ECO:0000303|PubMed:23096681};
DE AltName: Full=ATP synthase 6 kDa subunit, mitochondrial {ECO:0000305};
DE Flags: Precursor;
GN Name=ATP6 {ECO:0000303|PubMed:18338219, ECO:0000303|PubMed:23096681};
GN OrderedLocusNames=At3g46430 {ECO:0000312|Araport:AT3G46430};
GN ORFNames=F18L15.150 {ECO:0000312|EMBL:CAB62034.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15276431; DOI=10.1016/j.phytochem.2004.03.028;
RA Brugiere S., Kowalski S., Ferro M., Seigneurin-Berny D., Miras S.,
RA Salvi D., Ravanel S., d'Herin P., Garin J., Bourguignon J., Joyard J.,
RA Rolland N.;
RT "The hydrophobic proteome of mitochondrial membranes from Arabidopsis cell
RT suspensions.";
RL Phytochemistry 65:1693-1707(2004).
RN [6]
RP REPRESSION BY SUCROSE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15829605; DOI=10.1105/tpc.104.030254;
RA Giege P., Sweetlove L.J., Cognat V., Leaver C.J.;
RT "Coordination of nuclear and mitochondrial genome expression during
RT mitochondrial biogenesis in Arabidopsis.";
RL Plant Cell 17:1497-1512(2005).
RN [7]
RP FUNCTION, AND INDUCTION BY SALT; MANNITOL; DROUGHT AND COLD.
RC STRAIN=cv. Columbia;
RX PubMed=18338219; DOI=10.1007/s10529-008-9685-6;
RA Zhang X., Liu S., Takano T.;
RT "Overexpression of a mitochondrial ATP synthase small subunit gene
RT (AtMtATP6) confers tolerance to several abiotic stresses in Saccharomyces
RT cerevisiae and Arabidopsis thaliana.";
RL Biotechnol. Lett. 30:1289-1294(2008).
RN [8]
RP FUNCTION, AND INDUCTION BY ABIOTIC STRESSES.
RX PubMed=23096681; DOI=10.4238/2012.october.4.3;
RA Moghadam A.A., Taghavi S.M., Niazi A., Djavaheri M., Ebrahimie E.;
RT "Isolation and in silico functional analysis of MtATP6, a 6-kDa subunit of
RT mitochondrial F(1)F0-ATP synthase, in response to abiotic stress.";
RL Genet. Mol. Res. 11:3547-3567(2012).
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 (Probable). F-type ATPases consist of two
CC structural domains, F(1) - containing the extramembraneous catalytic
CC core and F(0) - containing the membrane proton channel, linked together
CC by a central stalk and a peripheral stalk (Probable). During catalysis,
CC ATP synthesis in the catalytic domain of F(1) is coupled via a rotary
CC mechanism of the central stalk subunits to proton translocation
CC (Probable). Part of the complex F(0) domain (Probable). Confers
CC tolerance to several abiotic stresses (e.g. salt, mannitol, drought,
CC oxidative and cold stresses), probably by providing additional energy
CC needed for cell homeostasis (PubMed:18338219, PubMed:23096681).
CC {ECO:0000269|PubMed:18338219, ECO:0000269|PubMed:23096681,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15276431}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Induced by several abiotic stresses such as salt, mannitol,
CC drought and cold (PubMed:18338219). Under oxidative stress caused by
CC H(2)O(2), transient induction followed by strongly reduced levels
CC (PubMed:18338219). Induced by sucrose (PubMed:15829605).
CC {ECO:0000269|PubMed:15829605, ECO:0000269|PubMed:18338219}.
CC -!- SIMILARITY: Belongs to the ATPase 6 subunit family. {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; AL133298; CAB62034.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78157.1; -; Genomic_DNA.
DR EMBL; AK117680; BAC42332.1; -; mRNA.
DR EMBL; AY064154; AAL36060.1; -; mRNA.
DR EMBL; AY081559; AAM10121.1; -; mRNA.
DR EMBL; AY097410; AAM19926.1; -; mRNA.
DR PIR; T45700; T45700.
DR SMR; P0DO44; -.
DR EnsemblPlants; AT3G46430.1; AT3G46430.1; AT3G46430.
DR EnsemblPlants; AT5G59613.1; AT5G59613.1; AT5G59613.
DR EnsemblPlants; AT5G59613.2; AT5G59613.2; AT5G59613.
DR Gramene; AT3G46430.1; AT3G46430.1; AT3G46430.
DR Gramene; AT5G59613.1; AT5G59613.1; AT5G59613.
DR Gramene; AT5G59613.2; AT5G59613.2; AT5G59613.
DR Araport; AT3G46430; -.
DR Proteomes; UP000006548; Chromosome 3.
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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IDA:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0010555; P:response to mannitol; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IDA:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IDA:UniProtKB.
PE 2: Evidence at transcript level;
KW CF(0); Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Stress response;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..11
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 12..55
FT /note="ATP synthase small subunit 6-A, mitochondrial"
FT /id="PRO_0000454200"
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 55 AA; 6585 MW; 96CEA6088EEBAA32 CRC64;
MRLFDPWPVF FKREWKRCWP FLTGFAVTGV LITKLTAGLT EEDAKNSKFV QQHRR
