ID   COX1_APTAU              Reviewed;         337 AA.
AC   O03515;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   22-FEB-2023, entry version 109.
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   Apteryx australis (Southern brown kiwi).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Apterygiformes; Apterygidae; Apteryx.
OX   NCBI_TaxID=8822;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Mantelli;
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}.
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DR   EMBL; U76057; AAB61313.1; -; Genomic_DNA.
DR   AlphaFoldDB; O03515; -.
DR   SMR; O03515; -.
DR   UniPathway; UPA00705; -.
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; 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   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_0000183285"
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;  36780 MW;  BE846B9B550F77DD CRC64;
     MTFITRWLFS TNHKDIGTLY LIFGAWAGMV GTALSLLIRA ELGQPGTLLG DDQIYNVIVT
     AHAFVMIFFM VMPVMIGGFG NWLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSTIE
     AGAGTGWTVY PPLAGNLAHA GASVDLAIFS LHLAGISSIL GAINFITTAI NMKPPALSQY
     QTPLFVWSVL ITAILLLLSL PVLAAGITML LTDRNLNTTF FDPAGGGDPV LYQHLFWFFG
     HPEVYILILP GFGMISHVVT YYAGKKEPFG YMGMVWAMLS IGFLGFIVWA HHMFTVGMDV
     DTRAYFTSAT MIIAIPTGIK VFSWLATLHG GTIKWDP
//