AOX1C_ARATH
ID AOX1C_ARATH Reviewed; 329 AA.
AC O22048;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ubiquinol oxidase 1c, mitochondrial;
DE EC=1.10.3.11;
DE AltName: Full=Alternative oxidase 1c;
DE Flags: Precursor;
GN Name=AOX1C; OrderedLocusNames=At3g27620; ORFNames=MGF10.3;
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 [GENOMIC DNA], INDUCTION BY ANTIMYCIN A, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX PubMed=9349280; DOI=10.1023/a:1005818507743;
RA Saisho D., Nambara E., Naito S., Tsutsumi N., Hirai A., Nakazono M.;
RT "Characterization of the gene family for alternative oxidase from
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 35:585-596(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [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 IRON-BINDING SITES.
RX PubMed=10225419; DOI=10.1016/s0014-5793(99)00376-2;
RA Andersson M.E., Nordlund P.;
RT "A revised model of the active site of alternative oxidase.";
RL FEBS Lett. 449:17-22(1999).
RN [6]
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia GL1;
RX PubMed=11434463; DOI=10.1266/ggs.76.89;
RA Saisho D., Nakazono M., Lee K.-H., Tsutsumi N., Akita S., Hirai A.;
RT "The gene for alternative oxidase-2 (AOX2) from Arabidopsis thaliana
RT consists of five exons unlike other AOX genes and is transcribed at an
RT early stage during germination.";
RL Genes Genet. Syst. 76:89-97(2001).
RN [7]
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).
RN [8]
RP INDUCTION BY ABIOTIC STRESSES.
RX PubMed=16027974; DOI=10.1007/s11103-005-5514-7;
RA Clifton R., Lister R., Parker K.L., Sappl P.G., Elhafez D., Millar A.H.,
RA Day D.A., Whelan J.;
RT "Stress-induced co-expression of alternative respiratory chain components
RT in Arabidopsis thaliana.";
RL Plant Mol. Biol. 58:193-212(2005).
RN [9]
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 [10]
RP TISSUE SPECIFICITY.
RX PubMed=16258072; DOI=10.1093/pcp/pci221;
RA Elhafez D., Murcha M.W., Clifton R., Soole K.L., Day D.A., Whelan J.;
RT "Characterization of mitochondrial alternative NAD(P)H dehydrogenases in
RT Arabidopsis: intraorganelle location and expression.";
RL Plant Cell Physiol. 47:43-54(2006).
RN [11]
RP INDUCTION BY COLD.
RX PubMed=17507388; DOI=10.1093/pcp/pcm061;
RA Matos A.R., Hourton-Cabassa C., Cicek D., Reze N., Arrabaca J.D.,
RA Zachowski A., Moreau F.;
RT "Alternative oxidase involvement in cold stress response of Arabidopsis
RT thaliana fad2 and FAD3+ cell suspensions altered in membrane lipid
RT composition.";
RL Plant Cell Physiol. 48:856-865(2007).
RN [12]
RP INDUCTION BY HIGH LIGHT.
RX PubMed=19567377; DOI=10.1093/pcp/pcp090;
RA Yoshida K., Noguchi K.;
RT "Differential gene expression profiles of the mitochondrial respiratory
RT components in illuminated Arabidopsis leaves.";
RL Plant Cell Physiol. 50:1449-1462(2009).
RN [13]
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).
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:14671022}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:14671022}. Note=Mitochondrial, possibly in the
CC inner surface of the inner mitochondrial membrane.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, cotyledons and
CC flowers. High expression in stamens. {ECO:0000269|PubMed:16258072,
CC ECO:0000269|PubMed:16859634, ECO:0000269|PubMed:9349280}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously. Not detected during
CC germination. {ECO:0000269|PubMed:11434463,
CC ECO:0000269|PubMed:16859634}.
CC -!- INDUCTION: No effect of antimycin A. Up-regulated by ethylene, high
CC light, glucose, cysteine, mannitol, salicylic acid and cold treatments.
CC {ECO:0000269|PubMed:16027974, ECO:0000269|PubMed:17507388,
CC ECO:0000269|PubMed:19567377, ECO:0000269|PubMed:21814799,
CC ECO:0000269|PubMed:9349280}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; AB003175; BAA22635.1; -; Genomic_DNA.
DR EMBL; AB018114; BAB02686.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77345.1; -; Genomic_DNA.
DR EMBL; BT004153; AAO42174.1; -; mRNA.
DR EMBL; BT005467; AAO63887.1; -; mRNA.
DR RefSeq; NP_189399.1; NM_113678.3.
DR AlphaFoldDB; O22048; -.
DR SMR; O22048; -.
DR STRING; 3702.AT3G27620.1; -.
DR PaxDb; O22048; -.
DR PRIDE; O22048; -.
DR ProteomicsDB; 244414; -.
DR EnsemblPlants; AT3G27620.1; AT3G27620.1; AT3G27620.
DR GeneID; 822384; -.
DR Gramene; AT3G27620.1; AT3G27620.1; AT3G27620.
DR KEGG; ath:AT3G27620; -.
DR Araport; AT3G27620; -.
DR TAIR; locus:2089124; AT3G27620.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR HOGENOM; CLU_041974_0_1_1; -.
DR InParanoid; O22048; -.
DR OMA; YTEYLRD; -.
DR OrthoDB; 943747at2759; -.
DR PhylomeDB; O22048; -.
DR PRO; PR:O22048; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O22048; baseline and differential.
DR Genevisible; O22048; 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; ISS:TAIR.
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..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..329
FT /note="Ubiquinol oxidase 1c, mitochondrial"
FT /id="PRO_0000001733"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 158
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 248
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 102
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q41224"
SQ SEQUENCE 329 AA; 37817 MW; A587B709DA246307 CRC64;
MITTLLRRSL LDASKQATSI NGILFHQLAP AKYFRVPAVG GLRDFSKMTF EKKKTSEEEE
GSGDGVKVND QGNKGEQLIV SYWGVKPMKI TKEDGTEWKW SCFRPWETYK ADLTIDLKKH
HVPSTLPDKI AYWMVKSLRW PTDLFFQRRY GCRAIMLETV AAVPGMVGGM LMHFKSLRRF
EQSGGWIKAL LEEAENERMH LMTFMEVAKP KWYERALVIS VQGVFFNAYL IGYIISPKFA
HRMVGYLEEE AIHSYTEFLK ELDNGNIENV PAPAIAVDYW RLEADATLRD VVMVVRADEA
HHRDVNHYAS DIHYQGHELK EAPAPIGYH
