COX3_ARATH
ID COX3_ARATH Reviewed; 265 AA.
AC P92514; A7KNG3; F4IMA5; Q8S8B5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
GN Name=COX3; OrderedLocusNames=AtMg00730 {ECO:0000312|Araport:ATMG00730};
GN and
GN OrderedLocusNames=At2g07687 {ECO:0000312|Araport:AT2G07687};
OS Arabidopsis thaliana (Mouse-ear cress).
OG Mitochondrion.
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. C24;
RX PubMed=8988169; DOI=10.1038/ng0197-57;
RA Unseld M., Marienfeld J.R., Brandt P., Brennicke A.;
RT "The mitochondrial genome of Arabidopsis thaliana contains 57 genes in
RT 366,924 nucleotides.";
RL Nat. Genet. 15:57-61(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. C24, cv. Columbia, and cv. Landsberg erecta;
RX PubMed=21951689; DOI=10.1186/1741-7007-9-64;
RA Davila J.I., Arrieta-Montiel M.P., Wamboldt Y., Cao J., Hagmann J.,
RA Shedge V., Xu Y.Z., Weigel D., Mackenzie S.A.;
RT "Double-strand break repair processes drive evolution of the mitochondrial
RT genome in Arabidopsis.";
RL BMC Biol. 9:64-64(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT2G07687).
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION (AT2G07687).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-258, AND RNA EDITING.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta; TISSUE=Rosette leaf;
RX PubMed=17565941; DOI=10.1534/genetics.107.073585;
RA Bentolila S., Elliott L.E., Hanson M.R.;
RT "Genetic architecture of mitochondrial editing in Arabidopsis thaliana.";
RL Genetics 178:1693-1708(2008).
RN [6]
RP RNA EDITING.
RX PubMed=10611383; DOI=10.1073/pnas.96.26.15324;
RA Giege P., Brennicke A.;
RT "RNA editing in Arabidopsis mitochondria effects 441 C to U changes in
RT ORFs.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15324-15329(1999).
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:P00420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00420};
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of a catalytic core of 3 subunits and
CC several supernumerary subunits. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00420}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00420}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00420}.
CC -!- RNA EDITING: Modified_positions=38 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 82 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 86 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 104 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 105 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 138 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941}, 141 {ECO:0000269|PubMed:10611383,
CC ECO:0000269|PubMed:17565941};
CC -!- MISCELLANEOUS: A stretch of 270 kb of the mitochondrial genome is
CC duplicated within the centromere of chromosome 2 resulting in the
CC duplication of the gene. The expression of this duplicated gene
CC (At2g07687) is not demonstrated. It is also probably not RNA edited and
CC therefore differs in all the positions known to be edited.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {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; Y08501; CAA69818.3; ALT_SEQ; Genomic_DNA.
DR EMBL; JF729200; AEK01262.1; ALT_SEQ; Genomic_DNA.
DR EMBL; JF729201; AEK01298.1; ALT_SEQ; Genomic_DNA.
DR EMBL; JF729202; AEK01326.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007143; AAM15412.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06078.1; ALT_SEQ; Genomic_DNA.
DR EMBL; EF488906; ABS50618.1; -; mRNA.
DR EMBL; EF488907; ABS50619.1; -; mRNA.
DR RefSeq; NP_085532.2; NC_001284.2.
DR RefSeq; NP_178782.1; NM_126741.2.
DR AlphaFoldDB; P92514; -.
DR SMR; P92514; -.
DR STRING; 3702.AT2G07687.1; -.
DR PaxDb; P92514; -.
DR PeptideAtlas; P92514; -.
DR PRIDE; P92514; -.
DR GeneID; 815364; -.
DR KEGG; ath:AT2G07687; -.
DR Araport; AT2G07687; -.
DR Araport; ATMG00730; -.
DR eggNOG; KOG4664; Eukaryota.
DR HOGENOM; CLU_044071_0_0_1; -.
DR InParanoid; P92514; -.
DR OrthoDB; 1304563at2759; -.
DR PhylomeDB; P92514; -.
DR BioCyc; ARA:AT2G07687-MON; -.
DR BioCyc; ARA:ATMG00730-MON; -.
DR BioCyc; MetaCyc:ATMG00730-MON; -.
DR PRO; PR:P92514; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Proteomes; UP000006548; Mitochondrion (cv. C24).
DR ExpressionAtlas; P92514; baseline and differential.
DR Genevisible; P92514; 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; IBA:GO_Central.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR Gene3D; 1.20.120.80; -; 1.
DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR PANTHER; PTHR11403; PTHR11403; 1.
DR Pfam; PF00510; COX3; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR PROSITE; PS50253; COX3; 1.
PE 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW RNA editing; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..265
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183737"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 265 AA; 29961 MW; 753978DE1CAA13F1 CRC64;
MIESQRHSYH LVDPSPWPIS GSLGALATTV GGVMYMHSFQ GGARLLSLGL IFILYTMFVW
WRDVLRESTL EGHHTKVVQL GLRYGFILFI VSEVMFFFAF FWAFFHSSLA PAVEIGGIWP
PKGIEVLDPW EIPFLNTLIL LSSGAAVTWA HHAILAGKEK RAVYALVATV LLALVFTGFQ
GMEYYQAPFT ISDSIYGSTF FLATGFHGFH VIIGTLFLII CGIRQYLGHL TKEHHVGFEA
AAWYWHFVDV VWLFLFVSIY WWGGI
