AOX1C_ORYSJ
ID AOX1C_ORYSJ Reviewed; 345 AA.
AC Q8W855;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ubiquinol oxidase 1c, mitochondrial {ECO:0000305};
DE EC=1.10.3.11 {ECO:0000250|UniProtKB:Q39219};
DE AltName: Full=Alternative oxidase 1c {ECO:0000303|PubMed:22994594};
DE Short=OsAOX1C {ECO:0000303|PubMed:22994594};
DE Flags: Precursor;
GN Name=AOX1C {ECO:0000303|PubMed:22994594};
GN OrderedLocusNames=Os02g0700400 {ECO:0000312|EMBL:BAF09753.1},
GN LOC_Os02g47200;
GN ORFNames=OJ1111_E07.10 {ECO:0000312|EMBL:BAD07517.1},
GN P0459B01.39 {ECO:0000312|EMBL:BAD07888.1};
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 TISSUE SPECIFICITY.
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 [7]
RP LACK OF 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 leaves and panicles.
CC {ECO:0000269|PubMed:12036102}.
CC -!- INDUCTION: Is not induced either by drought, cold and salt stresses, or
CC heat shock. {ECO:0000269|PubMed:22994594}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
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DR EMBL; AB074004; BAB71944.1; -; Genomic_DNA.
DR EMBL; AB074005; BAB71945.1; -; mRNA.
DR EMBL; AP003994; BAD07517.1; -; Genomic_DNA.
DR EMBL; AP004778; BAD07888.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09753.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80461.1; -; Genomic_DNA.
DR RefSeq; XP_015623809.1; XM_015768323.1.
DR AlphaFoldDB; Q8W855; -.
DR SMR; Q8W855; -.
DR STRING; 4530.OS02T0700400-01; -.
DR PaxDb; Q8W855; -.
DR PRIDE; Q8W855; -.
DR EnsemblPlants; Os02t0700400-01; Os02t0700400-01; Os02g0700400.
DR GeneID; 4330432; -.
DR Gramene; Os02t0700400-01; Os02t0700400-01; Os02g0700400.
DR KEGG; osa:4330432; -.
DR eggNOG; ENOG502QSB5; Eukaryota.
DR HOGENOM; CLU_041974_0_1_1; -.
DR InParanoid; Q8W855; -.
DR OMA; PNWFERA; -.
DR OrthoDB; 943747at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
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..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..345
FT /note="Ubiquinol oxidase 1c, mitochondrial"
FT /id="PRO_0000440572"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 60..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 216
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 315
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 315
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 318
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT DISULFID 118
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:Q41224"
SQ SEQUENCE 345 AA; 37886 MW; 9C12A0071D846744 CRC64;
MGSRAAGSVL LRHLCPRVSS STSAAAHAHA QRPPLAGAGG GGVALWARLL STSAAAAKEE
TAASKENTGS TAAAKAEATK AAKEGPASAT ASPVASSYWG IEASKLASKD GVEWKWSCFR
PWETYSPDTT IDLKKHHEPK VLLDKVAYWT VKALRVPTDI FFQRRYGCRA MMLETVAAVP
GMVGGMLLHL RSLRRFEHSG GWIRALLEEA ENERMHLMTF MEVAKPRWYE RALVLAVQGV
FFNAYFLGYL LSPKLAHRVV GYLEEEAIHS YTEYLKDIEA GKIENVPAPP IAIDYWRLPA
GATLKDVVVV VRADEAHHRD VNHFASDVHF QGMDLKDIPA PLDYH
