COX1_ANAPL
ID COX1_ANAPL Reviewed; 102 AA.
AC P50656;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Anas platyrhynchos (Mallard) (Anas boschas).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Pekin breed; TISSUE=Liver;
RX PubMed=8230253; DOI=10.1007/bf00175506;
RA Ramirez V., Savoie P., Morais R.;
RT "Molecular characterization and evolution of a duck mitochondrial genome.";
RL J. Mol. Evol. 37:296-310(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-59.
RC STRAIN=Pekin breed; TISSUE=Liver;
RX PubMed=2390786; DOI=10.1007/bf00313080;
RA Desjardins P., Ramirez V., Morais R.;
RT "Gene organization of the Peking duck mitochondrial genome.";
RL Curr. Genet. 17:515-518(1990).
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; L22480; AAA16541.1; -; Unassigned_DNA.
DR EMBL; X55529; CAA39146.1; -; Genomic_DNA.
DR AlphaFoldDB; P50656; -.
DR SMR; P50656; -.
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 PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR PROSITE; PS50855; COX1; 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..>102
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183281"
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..>102
FT /note="Helical; Name=III"
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 CONFLICT 47..50
FT /note="TLLG -> PPGL (in Ref. 2; CAA39146)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="V -> D (in Ref. 2; CAA39146)"
FT /evidence="ECO:0000305"
FT NON_TER 102
SQ SEQUENCE 102 AA; 11414 MW; 5E1B143E869F8115 CRC64;
MTFINRWLFS TNHKDIGTLY LIFGAWAGMI GTALSLLIRA ELGQPGTLLG DDQIYNVIVT
RHAFVMIFFM VMPIMIGGFG NWLVPLMIGA PDMAFPRMNN MS
