AOX3_ARATH
ID AOX3_ARATH Reviewed; 318 AA.
AC Q8LEE7; Q8VY45; Q9C612; Q9LQM4;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ubiquinol oxidase 3, mitochondrial;
DE EC=1.10.3.11;
DE AltName: Full=Alternative oxidase 3;
DE Flags: Precursor;
GN Name=AOX3; Synonyms=AOX1D; OrderedLocusNames=At1g32350;
GN ORFNames=F27G20_12, F5D14.11;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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=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]
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]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16859634; DOI=10.1016/j.bbabio.2006.03.009;
RA Clifton R., Millar A.H., Whelan J.;
RT "Alternative oxidases in Arabidopsis: a comparative analysis of
RT differential expression in the gene family provides new insights into
RT function of non-phosphorylating bypasses.";
RL Biochim. Biophys. Acta 1757:730-741(2006).
RN [6]
RP INDUCTION BY ANTIMYCIN A.
RX PubMed=19825614; DOI=10.1093/mp/ssn089;
RA Strodtkoetter I., Padmasree K., Dinakar C., Speth B., Niazi P.S.,
RA Wojtera J., Voss I., Do P.T., Nunes-Nesi A., Fernie A.R., Linke V.,
RA Raghavendra A.S., Scheibe R.;
RT "Induction of the AOX1D isoform of alternative oxidase in A. thaliana T-DNA
RT insertion lines lacking isoform AOX1A is insufficient to optimize
RT photosynthesis when treated with antimycin A.";
RL Mol. Plant 2:284-297(2009).
RN [7]
RP INDUCTION BY COLD AND ETHYLENE.
RX PubMed=21814799; DOI=10.1007/s00425-011-1488-7;
RA Wang H., Huang J., Liang X., Bi Y.;
RT "Involvement of hydrogen peroxide, calcium, and ethylene in the induction
RT of the alternative pathway in chilling-stressed Arabidopsis callus.";
RL Planta 235:53-67(2012).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP LEU-42.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: Catalyzes the cyanide-resistant oxidation of ubiquinol and
CC the reduction of molecular oxygen to water, but does not translocate
CC protons and consequently is not linked to oxidative phosphorylation.
CC May increase respiration when the cytochrome respiratory pathway is
CC restricted, or in response to low temperatures (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O;
CC Xref=Rhea:RHEA:30255, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976; EC=1.10.3.11;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q39219};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250|UniProtKB:Q39219};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:25732537}; Multi-pass membrane protein
CC {ECO:0000305}. Note=Mitochondrial, possibly in the inner surface of the
CC inner mitochondrial membrane.
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings, leaves, flowers and
CC sepals. Highest expression in the senescent leaves.
CC {ECO:0000269|PubMed:16859634}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early rosette development and
CC during flowering. {ECO:0000269|PubMed:16859634}.
CC -!- INDUCTION: Up-regulated by antimycin A. No effect of ethylene or cold
CC treatment. {ECO:0000269|PubMed:19825614, ECO:0000269|PubMed:21814799}.
CC -!- MISCELLANEOUS: Unable to fully compensate for the loss of AOX1A when
CC electron flow via the cytochrome pathway is restricted.
CC {ECO:0000305|PubMed:19825614}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG60173.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007767; AAF81331.1; -; Genomic_DNA.
DR EMBL; AC084110; AAG60173.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31467.1; -; Genomic_DNA.
DR EMBL; AY072541; AAL60049.1; -; mRNA.
DR EMBL; AY085459; AAM62685.1; -; mRNA.
DR PIR; C86448; C86448.
DR RefSeq; NP_564395.1; NM_102968.3.
DR AlphaFoldDB; Q8LEE7; -.
DR SMR; Q8LEE7; -.
DR BioGRID; 25361; 5.
DR IntAct; Q8LEE7; 4.
DR STRING; 3702.AT1G32350.1; -.
DR iPTMnet; Q8LEE7; -.
DR PaxDb; Q8LEE7; -.
DR PRIDE; Q8LEE7; -.
DR ProteomicsDB; 244471; -.
DR EnsemblPlants; AT1G32350.1; AT1G32350.1; AT1G32350.
DR GeneID; 840127; -.
DR Gramene; AT1G32350.1; AT1G32350.1; AT1G32350.
DR KEGG; ath:AT1G32350; -.
DR Araport; AT1G32350; -.
DR TAIR; locus:2028311; AT1G32350.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR HOGENOM; CLU_041974_0_1_1; -.
DR InParanoid; Q8LEE7; -.
DR OMA; PKWHERA; -.
DR OrthoDB; 943747at2759; -.
DR PhylomeDB; Q8LEE7; -.
DR PRO; PR:Q8LEE7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LEE7; baseline and differential.
DR Genevisible; Q8LEE7; 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:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009916; F:alternative oxidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106292; F:superoxide-generating NADPH oxidase activity; IDA:TAIR.
DR GO; GO:0102721; F:ubiquinol:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0010230; P:alternative respiration; IBA:GO_Central.
DR CDD; cd01053; AOX; 1.
DR Gene3D; 1.20.1260.140; -; 1.
DR InterPro; IPR002680; AOX.
DR InterPro; IPR038659; AOX_sf.
DR PANTHER; PTHR31803; PTHR31803; 1.
DR Pfam; PF01786; AOX; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Electron transport; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Reference proteome; Respiratory chain; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 43..318
FT /note="Ubiquinol oxidase 3, mitochondrial"
FT /id="PRO_0000045422"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 288
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 288
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 291
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 91
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q41224"
FT CONFLICT 150
FT /note="Missing (in Ref. 3; AAL60049)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="G -> W (in Ref. 4; AAM62685)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="I -> M (in Ref. 3; AAL60049)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="L -> F (in Ref. 3; AAL60049)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="D -> E (in Ref. 3; AAL60049)"
FT /evidence="ECO:0000305"
FT CONFLICT 290..291
FT /note="HH -> PP (in Ref. 3; AAL60049)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36202 MW; F45F0526F86DD5A0 CRC64;
MSYRSIYRTL RPVLSSSVQS SGLGIGGFRG HLISHLPNVR LLSSDTSSPV SGNNQPENPI
RTADGKVIST YWGIPPTKIT KPDGSAWKWN CFQPWDSYKP DVSIDVTKHH KPSNFTDKFA
YWTVQTLKIP VQLFFQRKHM CHAMLLETVA AVPGMVGGML LHLKSLRRFE HSGGWIKALL
EEAENERMHL MTFIELSQPK WYERAIVFTV QGVFFNAYFL AYVISPKLAH RITGYLEEEA
VNSYTEFLKD IDAGKFENSP APAIAIDYWR LPKDATLRDV VYVIRADEAH HRDINHYASD
IQFKGHELKE APAPIGYH
