ID COX1_POMNI Reviewed; 161 AA. AC P29652; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 02-SEP-2026, entry version 116. 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 Pomoxis nigromaculatus (Black crappie) (Cantharus nigromaculatus). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Centrarchiformes; Centrarchoidei; Centrarchidae; Pomoxis. OX NCBI_TaxID=8182; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1663569; DOI=10.1093/oxfordjournals.molbev.a040685; RA Normark B.B., McCune A.R., Harrison R.G.; RT "Phylogenetic relationships of neopterygian fishes, inferred from RT mitochondrial DNA sequences."; RL Mol. Biol. Evol. 8:819-834(1991). 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] + 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: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 COXFA4, 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; M64914; AAB01478.1; -; Genomic_DNA. DR AlphaFoldDB; P29652; -. DR SMR; P29652; -. DR UniPathway; UPA00705; -. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB. DR GO; GO:0004129; F:cytochrome-c oxidase activity; ISS:UniProtKB. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:TreeGrafter. DR FunFam; 1.20.210.10:FF:000009; Cytochrome c oxidase subunit 1; 1. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Copper; Electron transport; Heme; Iron; Magnesium; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain; Sodium; KW Translocase; Transmembrane; Transmembrane helix; Transport. FT CHAIN <1..>161 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000183401" FT TRANSMEM <1..31 FT /note="Helical; Name=VI" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 32..39 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 40..56 FT /note="Helical; Name=VII" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 57..68 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 69..97 FT /note="Helical; Name=VIII" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 98..105 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 106..127 FT /note="Helical; Name=IX" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TOPO_DOM 128..140 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:P00396" FT TRANSMEM 141..>161 FT /note="Helical; Name=X" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 10 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 14 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 60 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 61 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 138 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with MT-CO2" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 139 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with MT-CO2" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 146 FT /ligand="heme a3" FT /ligand_id="ChEBI:CHEBI:83282" FT /ligand_note="high-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 148 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 CROSSLNK 10..14 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250|UniProtKB:P00396" FT NON_TER 1 FT NON_TER 161 SQ SEQUENCE 161 AA; 17991 MW; ADB0E64C3EF92EF2 CRC64; YQHLFWFFGH PEVYILILPG FGMISHIVAY YSGKKEPFGY MGMVWAMMAI GLLGFIVWAH HMFTVGMDVD TRAYFTSATM IIAIPTGVKV FSWLATLHGA SIKWETPLLW ALGFIFLFTV GGLTGIVLAN SSLDIVLHDT YYVVAHFHYV LSMGAVFAIV A //