ID COX3_WHEAT Reviewed; 265 AA. AC P15953; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 2. DT 24-JAN-2024, entry version 122. 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; OS Triticum aestivum (Wheat). OG Mitochondrion. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum. OX NCBI_TaxID=4565; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Capitole; RX PubMed=2155710; DOI=10.1007/bf00313247; RA Gualberto J.M., Domon C., Weil J.H., Grienenberger J.-M.; RT "Structure and transcription of the gene coding for subunit 3 of cytochrome RT oxidase in wheat mitochondria."; RL Curr. Genet. 17:41-47(1990). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Capitole; TISSUE=Etiolated plantlet; RX PubMed=1588598; DOI=10.1007/bf00162974; RA Karlovsky P., Fartmann B.; RT "Genetic code and phylogenetic origin of oomycetous mitochondria."; RL J. Mol. Evol. 34:254-258(1992). RN [3] RP RNA EDITING. RX PubMed=1695731; DOI=10.1093/nar/18.13.3771; RA Gualberto J.M., Weil J.H., Grienenberger J.M.; RT "Editing of the wheat coxIII transcript: evidence for twelve C to U and one RT U to C conversions and for sequence similarities around editing sites."; RL Nucleic Acids Res. 18:3771-3776(1990). 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=82 {ECO:0000269|PubMed:1695731}, 86 CC {ECO:0000269|PubMed:1695731}, 97 {ECO:0000269|PubMed:1695731}, 104 CC {ECO:0000269|PubMed:1695731}, 105 {ECO:0000269|PubMed:1695731}, 138 CC {ECO:0000269|PubMed:1695731}, 141 {ECO:0000269|PubMed:1695731}, 171 CC {ECO:0000269|PubMed:1695731}, 176 {ECO:0000269|PubMed:1695731}, 189 CC {ECO:0000269|PubMed:1695731}, 252 {ECO:0000269|PubMed:1695731}, 255 CC {ECO:0000269|PubMed:1695731}; 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; X52539; CAA36775.1; -; mRNA. DR EMBL; X15944; CAA34071.1; ALT_SEQ; Genomic_DNA. DR PIR; S10331; OTWT3M. DR RefSeq; YP_398397.1; NC_007579.1. DR AlphaFoldDB; P15953; -. DR SMR; P15953; -. DR PaxDb; 4565-EPlTAEP00000010091; -. DR eggNOG; KOG4664; Eukaryota. DR ExpressionAtlas; P15953; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro. DR CDD; cd01665; Cyt_c_Oxidase_III; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.80; Cytochrome c oxidase, subunit III, four-helix bundle; 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:SF7; CYTOCHROME C OXIDASE SUBUNIT 3; 1. DR PANTHER; PTHR11403; CYTOCHROME C OXIDASE SUBUNIT III; 1. DR Pfam; PF00510; COX3; 1. DR SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 1. DR PROSITE; PS50253; COX3; 1. PE 2: Evidence at transcript level; KW Membrane; Mitochondrion; Mitochondrion inner membrane; RNA editing; KW Translocase; Transmembrane; Transmembrane helix. FT CHAIN 1..265 FT /note="Cytochrome c oxidase subunit 3" FT /id="PRO_0000183871" 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; 29796 MW; A7918C9FBFC22608 CRC64; MIESQRHSYH LVDPSPWPIS GSLGALATTV GGVMYMHSFQ GGATLLSLGL IFILYTMFVW WRDVLRESTL EGHHTKAVQL GLRYGFILFI VSEVMFFFAF FWAFFHSSLA PTVEIGGIWP PKGIGVLDPW EIPLLNTLIL LSSGAAVTWA HHAILAGKEK RAVYALVATV LLALVFTGFQ GMEYYQAPFT ISDSIYGSTF FLATGFHGFH VIIGTLFLIV CGIRQYLGQM TKKHHVGFEA AAWYWHFVDV VWLFLFVSIY WWGGI //