ID COX3_DICDI Reviewed; 435 AA. AC O21049; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 24-JAN-2024, 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=cox3; ORFNames=DDB_G0294092; OS Dictyostelium discoideum (Social amoeba). OG Mitochondrion. OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=AX3; RX PubMed=9000384; DOI=10.1007/s002940050179; RA Ogawa S., Matsuo K., Angata K., Yanagisawa K., Tanaka Y.; RT "Group-I introns in the cytochrome c oxidase genes of Dictyostelium RT discoideum: two related ORFs in one loop of a group-I intron, a cox1/2 RT hybrid gene and an unusually large cox3 gene."; RL Curr. Genet. 31:80-88(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX3; RX PubMed=10821186; DOI=10.1007/pl00008685; RA Ogawa S., Yoshino R., Angata K., Iwamoto M., Pi M., Kuroe K., Matsuo K., RA Morio T., Urushihara H., Yanagisawa K., Tanaka Y.; RT "The mitochondrial DNA of Dictyostelium discoideum: complete sequence, gene RT content and genome organization."; RL Mol. Gen. Genet. 263:514-519(2000). 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 -!- 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; D16579; BAA21120.1; -; Genomic_DNA. DR EMBL; AB000109; BAA78053.1; -; Genomic_DNA. DR PIR; T43749; T43749. DR RefSeq; NP_050071.1; NC_000895.1. DR AlphaFoldDB; O21049; -. DR SMR; O21049; -. DR STRING; 44689.O21049; -. DR GeneID; 2193893; -. DR KEGG; ddi:DidioMp04; -. DR dictyBase; DDB_G0294092; cox3. DR InParanoid; O21049; -. DR PhylomeDB; O21049; -. DR PRO; PR:O21049; -. DR Proteomes; UP000002195; Mitochondrion. 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: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; Cytochrome c oxidase, subunit III, four-helix bundle; 2. 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; 2. DR SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 2. DR PROSITE; PS50253; COX3; 1. PE 3: Inferred from homology; KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; KW Translocase; Transmembrane; Transmembrane helix. FT CHAIN 1..435 FT /note="Cytochrome c oxidase subunit 3" FT /id="PRO_0000312370" FT TRANSMEM 70..90 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 96..116 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 132..152 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 176..196 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 325..345 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 360..380 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 412..432 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 435 AA; 50234 MW; 5AC920869B67F434 CRC64; MKGFFENLFR QNVRSVINTG KKVGARAAAR EIINQEWGYP LANHEVLFLT NVYQPKHMKR HPFHIVRGTV APLAVTLPLG FFVLNYFGVI SSKLGLLIAL SSFIGGLVIW TISIIFDSLY DQQHTYEVKR GLVMGMMMFI ISEVMFFFSF FWSYFYISLS PNIAIGCVWP PYGLTVYSYM GLPLLNTVLL LLSGAILTDG YTILTEQKAV HEKNEKVLAV EEAFKNLMNL YKTKNSINTL TFVDERRDKF FGKESRQEDK IAEQKLIAIS AGVKELRDLD WDLYFFENPE NIEPNYKEPT NLSVIEYALI TIYLKKRNKV IKTRLYFTLL CAVVFLACQG YEYFFAPFSM NDGIYGSLFF LLTGFHGFHV LVGSILIGII TIRFIVGNFN LLNVGTNFQI YKNKSTGFAC TLFYWHFVDI VWIFLYIVIY WWGSR //