ID COX1_TINMA Reviewed; 337 AA. AC O03554; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 03-AUG-2022, entry version 103. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide I; DE Flags: Fragment; GN Name=MT-CO1; Synonyms=COI, COXI, MTCO1; OS Tinamus major (Great tinamou) (Tetrao major). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus. OX NCBI_TaxID=30468; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Lee K., Feinstein J., Cracraft J.; RT "Phylogenetic relationships of the ratite birds: resolving conflicts RT between molecular and morphological data sets."; RL (In) Mindell D.P. (eds.); RL Avian molecular evolution and systematics, pp.1-1, Academic Press, New York RL (1997). 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:P00401}. 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:P00401}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000250|UniProtKB:P00401}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000250|UniProtKB:P00396}; CC Note=Binds 2 heme A groups non-covalently per subunit. CC {ECO:0000250|UniProtKB:P00396}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000250|UniProtKB:P00396}; CC Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00396}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000250|UniProtKB:P00401}. CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a CC multisubunit enzyme composed of 14 subunits. The complex is composed of CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in CC the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A, CC COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which CC are encoded in the nuclear genome. The complex exists as a monomer or a CC dimer and forms supercomplexes (SCs) in the inner mitochondrial CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex CC III, CIII), resulting in different assemblies (supercomplex CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (By similarity). CC As a newly synthesized protein, rapidly incorporates into a multi- CC subunit assembly intermediate in the inner membrane, called MITRAC CC (mitochondrial translation regulation assembly intermediate of CC cytochrome c oxidase) complex, whose core components are COA3/MITRAC12 CC and COX14. Within the MITRAC complex, interacts with COA3 and with CC SMIM20/MITRAC7; the interaction with SMIM20 stabilizes the newly CC synthesized MT-CO1 and prevents its premature turnover. Interacts with CC TMEM177 in a COX20-dependent manner (By similarity). CC {ECO:0000250|UniProtKB:P00395, ECO:0000250|UniProtKB:P00396}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00396}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00396}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase 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; U76063; AAB61331.1; -; Genomic_DNA. DR AlphaFoldDB; O03554; -. DR SMR; O03554; -. DR UniPathway; UPA00705; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Calcium; Copper; Electron transport; Heme; Iron; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain; Sodium; KW Translocase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..>337 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000183426" FT TOPO_DOM 1..12 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 13..41 FT /note="Helical; Name=I" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 42..51 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 52..87 FT /note="Helical; Name=II" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 88..95 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 96..118 FT /note="Helical; Name=III" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 119..141 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 142..171 FT /note="Helical; Name=IV" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 172..183 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 184..213 FT /note="Helical; Name=V" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 214..228 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 229..262 FT /note="Helical; Name=VI" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 263..270 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 271..287 FT /note="Helical; Name=VII" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 288..299 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 300..328 FT /note="Helical; Name=VIII" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 329..>337 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 41 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 46 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 62 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_note="low-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 241 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 245 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 291 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 292 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00396" FT CROSSLNK 241..245 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250|UniProtKB:P00396" FT NON_TER 337 SQ SEQUENCE 337 AA; 36806 MW; 637DBE38B678F319 CRC64; MTFITRWLFS TNHKDIGTLY LIFGAWAGMV GTALSLLIRA ELGQPGTLLG DDQIYNVVVT AHAFVMIFFM VMPVMIGGFG NWLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSTVE TGVGTGWTVY PPLASNLAHA GASVDLAIFS LHLAGVSSIL GAINFITTAI NMKPPALTQY QTPLFVWSVL ITAILLLLSL PVLAAGITML LTDRNLNTTF FDPAGGGDPI LYQHLFWFFG HPEVYILILP GFGIISHVVA YYAGKKEPFG YMGMVWAMLS IGFLGFIVWA HHMFTVGMDV DTRAYFTSAT MIIAIPTGIK VFSWLATLHG GTIKWDP //