ID COX6_DICDI Reviewed; 93 AA. AC P26310; Q54T04; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 108. DE RecName: Full=Cytochrome c oxidase polypeptide 6, mitochondrial; DE AltName: Full=Cytochrome c oxidase polypeptide VI; GN Name=cxfA; Synonyms=cox6; ORFNames=DDB_G0282097; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-18. RC STRAIN=AX3; RX PubMed=1650252; DOI=10.1016/0167-4781(91)90180-t; RA Rizzuto R., Sandona D., Capaldi R.A., Bisson R.; RT "Characterization of a cDNA encoding subunit VI of cytochrome c oxidase RT from the slime mold Dictyostelium discoideum."; RL Biochim. Biophys. Acta 1089:386-388(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). 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:P00424}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000250|UniProtKB:P00424}. 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 seevral 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:P00424}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00424}; Single-pass membrane protein CC {ECO:0000250|UniProtKB:P00424}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase IV 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; X55672; CAA39207.1; -; mRNA. DR EMBL; AAFI02000045; EAL66374.1; -; Genomic_DNA. DR PIR; S17190; OGDO6. DR RefSeq; XP_640351.1; XM_635259.1. DR AlphaFoldDB; P26310; -. DR SMR; P26310; -. DR STRING; 44689.P26310; -. DR PaxDb; 44689-DDB0215013; -. DR EnsemblProtists; EAL66374; EAL66374; DDB_G0282097. DR GeneID; 8623406; -. DR KEGG; ddi:DDB_G0282097; -. DR dictyBase; DDB_G0282097; cxfA. DR eggNOG; ENOG502RIDF; Eukaryota. DR HOGENOM; CLU_2404152_0_0_1; -. DR InParanoid; P26310; -. DR OMA; RYPKGFK; -. DR UniPathway; UPA00705; -. DR PRO; PR:P26310; -. DR Proteomes; UP000002195; Chromosome 3. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. PE 1: Evidence at protein level; KW Direct protein sequencing; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Oxidoreductase; Reference proteome; KW Transmembrane; Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1650252" FT CHAIN 2..93 FT /note="Cytochrome c oxidase polypeptide 6, mitochondrial" FT /id="PRO_0000194086" FT TOPO_DOM 2..33 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000250|UniProtKB:P00424" FT TRANSMEM 34..53 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 54..93 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:P00424" SQ SEQUENCE 93 AA; 10666 MW; 6D73D3EA4A448A96 CRC64; MSTGNESYNL RYPKGFKGYP YNMYKLEGYG TPKGYITLIG VVATLTVSGL FFAKTRSNKR EYPTHNKEWR AKTLAYAKET NADPIYQLPK DKI //