ID COX3_LOCMI Reviewed; 263 AA. AC P14574; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 02-SEP-2026, entry version 115. DE RecName: Full=Cytochrome c oxidase subunit 3; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide III; GN Name=COIII; OS Locusta migratoria (Migratory locust). OG Mitochondrion. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Polyneoptera; Orthoptera; OC Caelifera; Acrididea; Acridomorpha; Acridoidea; Acrididae; Oedipodinae; OC Locusta. OX NCBI_TaxID=7004; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2852067; DOI=10.1007/bf00521271; RA Haucke H.R., Gellissen G.; RT "Different mitochondrial gene orders among insects: exchanged tRNA gene RT positions in the COII/COIII region between an orthopteran and a dipteran RT species."; RL Curr. Genet. 14:471-476(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8587138; DOI=10.1007/bf00173173; RA Flook P.K., Rowell C.H.F., Gellissen G.; RT "The sequence, organization, and evolution of the Locusta migratoria RT mitochondrial genome."; RL J. Mol. Evol. 41:928-941(1995). 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] + O2 + 8 H(+)(in) = 4 Fe(III)- CC [cytochrome c] + 2 H2O + 4 H(+)(out); 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 -!- 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; X13975; CAA32156.1; -; Genomic_DNA. DR EMBL; X80245; CAA56529.1; -; Genomic_DNA. DR PIR; T11469; T11469. DR RefSeq; NP_007295.1; NC_001712.1. DR AlphaFoldDB; P14574; -. DR SMR; P14574; -. DR GeneID; 807961; -. DR CTD; 4514; -. DR GO; GO:1902494; C:catalytic complex; IEA:UniProtKB-ARBA. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0004129; F:cytochrome-c oxidase activity; ISS:UniProtKB. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:UniProtKB-ARBA. DR CDD; cd01665; Cyt_c_Oxidase_III; 1. DR FunFam; 1.10.287.70:FF:000082; Cytochrome c oxidase subunit 3; 1. DR FunFam; 1.20.120.80:FF:000002; Cytochrome c oxidase subunit 3; 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 3: Inferred from homology; KW Membrane; Mitochondrion; Mitochondrion inner membrane; Translocase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..263 FT /note="Cytochrome c oxidase subunit 3" FT /id="PRO_0000183800" FT TRANSMEM 9..29 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 40..60 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 84..104 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 129..149 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 161..181 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 198..218 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 241..261 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 263 AA; 30353 MW; C5ED6EDB148B37BD CRC64; MLTNNNNHPF HMVDYSPWPL TGAIGAMILT SGMTKWFHTF NMNLLMIGMT VIVLTMIQWW RDVVREGTFQ GLHTKLVSKG LRWGMILFIA SEVLFFASFF WAFFNSSLAP TIELGMKWPP MGIQPFNPIQ IPLLNTAILL ASGVTITWAH HSIMECNHSQ ALQGLFFTVM LGFYFTLLQM YEYWEAPFTI ADAVYGSTFF VATGFHGLHV IIGTTFLLTC LIRHMMNQFS SNHHFGFEAA AWYWHFVDVV WLFLYLSIYW WGS //