ID COX3_THEPA Reviewed; 255 AA. AC Q36098; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 94. DE RecName: Full=Cytochrome c oxidase subunit 3; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide III; GN Name=MT-CO3; Synonyms=COIII, COXIII, MTCO3; OS Theileria parva (East coast fever infection agent). OG Mitochondrion. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida; OC Theileriidae; Theileria. OX NCBI_TaxID=5875; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Muguga; RX PubMed=8112303; DOI=10.1002/j.1460-2075.1994.tb06333.x; RA Kairo A., Fairlamb A., Gobright E., Nene V.; RT "A 7.1 kb linear DNA molecule of Theileria parva has scrambled rDNA RT sequences and open reading frames for mitochondrially-encoded proteins."; RL EMBO J. 13:898-905(1994). 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; Z23263; CAA80799.1; -; Genomic_DNA. DR PIR; S41690; S41690. DR RefSeq; YP_001994286.1; NC_011005.1. DR AlphaFoldDB; Q36098; -. DR SMR; Q36098; -. DR STRING; 5875.Q36098; -. DR GeneID; 6741537; -. DR InParanoid; Q36098; -. 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; cd00386; Heme_Cu_Oxidase_III_like; 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; 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..255 FT /note="Cytochrome c oxidase subunit 3" FT /id="PRO_0000232683" FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 42..62 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 91..111 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 128..148 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 155..175 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 196..216 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 234..254 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 255 AA; 29891 MW; A3FF61D44AA28844 CRC64; MRNSAQSYLK YINIINIFET LYLFYSTGLD TLEYIDSTYK NFIIMYVNQY LLYGTTLKYL SVGEFFMNSL TIFINSIREI MTSTTMVMYA IFGMFIFSEI LVFSTFIWGY FHLRLSNPIL LAELNVEAYL QISDVLNTGS ILVSIILHRV QESANFETDF FMEQLLLIGF IFLSLQNDEY SLILSYVNNY WMTLYFFILT GLHSLHVCAG GIFVLIQSYF YEGDGSQRDE EFNAGVYWHF VEMIWIALTM LLFLA //