AOX1A_ORYSJ
ID AOX1A_ORYSJ Reviewed; 332 AA.
AC O82807;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ubiquinol oxidase 1a, mitochondrial {ECO:0000305};
DE EC=1.10.3.11 {ECO:0000250|UniProtKB:Q39219};
DE AltName: Full=Alternative oxidase 1a {ECO:0000303|PubMed:22994594};
DE Short=OsAOX1A {ECO:0000303|PubMed:22994594};
DE Flags: Precursor;
GN Name=AOX1A {ECO:0000303|PubMed:22994594};
GN Synonyms=AOX1 {ECO:0000303|Ref.8};
GN OrderedLocusNames=Os04g0600200 {ECO:0000312|EMBL:BAF15672.1},
GN LOC_Os04g51150 {ECO:0000305};
GN ORFNames=OsJ_16032 {ECO:0000312|EMBL:EAZ31867.1},
GN OSJNBa0083N12.11 {ECO:0000312|EMBL:CAD41813.2};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=9426242; DOI=10.1016/s0378-1119(97)00502-7;
RA Ito Y., Saisho D., Nakazono M., Tsutsumi N., Hirai A.;
RT "Transcript levels of tandem-arranged alternative oxidase genes in rice are
RT increased by low temperature.";
RL Gene 203:121-129(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Hayayuki; TISSUE=Anther;
RX AGRICOLA=IND21238861;
RA Abe F., Kitashiba H., Kishitani S., Toriyama K.;
RT "Isolation of a cDNA clone encoding the alternative oxidase expressed in
RT rice anthers.";
RL Sex. Plant Reprod. 10:374-375(1997).
RN [9]
RP INDUCTION.
RX PubMed=10767423; DOI=10.1016/s0014-5793(00)01411-3;
RA Tsuji H., Nakazono M., Saisho D., Tsutsumi N., Hirai A.;
RT "Transcript levels of the nuclear-encoded respiratory genes in rice
RT decrease by oxygen deprivation: evidence for involvement of calcium in
RT expression of the alternative oxidase 1a gene.";
RL FEBS Lett. 471:201-204(2000).
RN [10]
RP TISSUE SPECIFICITY, AND INDUCTION BY COLD.
RX PubMed=12036102; DOI=10.1266/ggs.77.31;
RA Saika H., Ohtsu K., Hamanaka S., Nakazono M., Tsutsumi N., Hirai A.;
RT "AOX1c, a novel rice gene for alternative oxidase; comparison with rice
RT AOX1a and AOX1b.";
RL Genes Genet. Syst. 77:31-38(2002).
RN [11]
RP INDUCTION BY COLD.
RX PubMed=12012245; DOI=10.1007/s00425-001-0714-0;
RA Watanabe A., Hirai A.;
RT "Two uncoupling protein genes of rice (Oryza sativa L.): molecular study
RT reveals the defects in the pre-mRNA processing for the heat-generating
RT proteins of the subtropical cereal.";
RL Planta 215:90-100(2002).
RN [12]
RP INDUCTION.
RX PubMed=22994594; DOI=10.1111/pce.12013;
RA Li C.R., Liang D.D., Li J., Duan Y.B., Li H., Yang Y.C., Qin R.Y., Li L.,
RA Wei P.C., Yang J.B.;
RT "Unravelling mitochondrial retrograde regulation in the abiotic stress
RT induction of rice ALTERNATIVE OXIDASE 1 genes.";
RL Plant Cell Environ. 36:775-788(2013).
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.
CC {ECO:0000250|UniProtKB:Q39219}.
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 Evidence={ECO:0000250|UniProtKB:Q39219};
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:0000250|UniProtKB:Q41224}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaf sheaths and leaf blades.
CC {ECO:0000269|PubMed:12036102}.
CC -!- DEVELOPMENTAL STAGE: Expressed in anthers at the uninucleate microspore
CC stage and the bicellular pollen stage. {ECO:0000269|Ref.8}.
CC -!- INDUCTION: Induced by cold (PubMed:12012245, PubMed:12036102,
CC PubMed:22994594). Induced by drought and salt stresses, heat shock,
CC hydrogen peroxide and methyl viologen (PubMed:22994594). Down-regulated
CC under oxygen deprivation (PubMed:10767423).
CC {ECO:0000269|PubMed:10767423, ECO:0000269|PubMed:12012245,
CC ECO:0000269|PubMed:12036102, ECO:0000269|PubMed:22994594}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; AB004813; BAA28772.1; -; Genomic_DNA.
DR EMBL; AB004864; BAA28773.1; -; mRNA.
DR EMBL; AL606683; CAD41813.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF15672.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90831.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ31867.1; -; Genomic_DNA.
DR EMBL; AK064040; BAG88978.1; -; mRNA.
DR RefSeq; XP_015635413.1; XM_015779927.1.
DR AlphaFoldDB; O82807; -.
DR SMR; O82807; -.
DR STRING; 4530.OS04T0600200-01; -.
DR PaxDb; O82807; -.
DR PRIDE; O82807; -.
DR EnsemblPlants; Os04t0600200-01; Os04t0600200-01; Os04g0600200.
DR GeneID; 4336874; -.
DR Gramene; Os04t0600200-01; Os04t0600200-01; Os04g0600200.
DR KEGG; osa:4336874; -.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR HOGENOM; CLU_041974_0_1_1; -.
DR InParanoid; O82807; -.
DR OMA; RHHEPKT; -.
DR OrthoDB; 943747at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
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; IBA:GO_Central.
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: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 2: Evidence at transcript 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..54
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 55..332
FT /note="Ubiquinol oxidase 1a, mitochondrial"
FT /id="PRO_0000440570"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
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 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 251
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="1"
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 BINDING 305
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 105
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q41224"
SQ SEQUENCE 332 AA; 37137 MW; A1A3C511404B60AD CRC64;
MSSRMAGSAI LRHVGGVRLF TASATSPAAA AAAAARPFLA GGEAVPGVWG LRLMSTSSVA
STEAAAKAEA KKADAEKEVV VNSYWGIEQS KKLVREDGTE WKWSCFRPWE TYTADTSIDL
TKHHVPKTLL DKIAYWTVKS LRFPTDIFFQ RRYGCRAMML ETVAAVPGMV GGMLLHLRSL
RRFEQSGGWI RTLLEEAENE RMHLMTFMEV ANPKWYERAL VITVQGVFFN AYFLGYLLSP
KFAHRVVGYL EEEAIHSYTE FLKDLEAGKI DNVPAPAIAI DYWRLPANAT LKDVVTVVRA
DEAHHRDVNH FASDIHYQGM ELKQTPAPIG YH
