ID   COX1_CHICK              Reviewed;         515 AA.
AC   P18943;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Cytochrome c oxidase subunit 1;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide I;
GN   Name=MT-CO1; Synonyms=COI, COXI, MTCO1;
OS   Gallus gallus (Chicken).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RC   TISSUE=Liver;
RX   PubMed=2329578; DOI=10.1016/0022-2836(90)90225-b;
RA   Desjardins P., Morais R.;
RT   "Sequence and gene organization of the chicken mitochondrial genome. A
RT   novel gene order in higher vertebrates.";
RL   J. Mol. Biol. 212:599-634(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}.
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DR   EMBL; X52392; CAA36627.1; -; Genomic_DNA.
DR   PIR; S10189; S10189.
DR   RefSeq; NP_006917.1; NC_001323.1.
DR   AlphaFoldDB; P18943; -.
DR   SMR; P18943; -.
DR   STRING; 9031.ENSGALP00000046506; -.
DR   PaxDb; 9031-ENSGALP00000034614; -.
DR   Ensembl; ENSGALT00000053568; ENSGALP00000046506; ENSGALG00000032142.
DR   VEuPathDB; HostDB:geneid_63549487; -.
DR   eggNOG; KOG4769; Eukaryota.
DR   HOGENOM; CLU_011899_7_3_1; -.
DR   InParanoid; P18943; -.
DR   Reactome; R-GGA-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-GGA-611105; Respiratory electron transport.
DR   Reactome; R-GGA-9707564; Cytoprotection by HMOX1.
DR   UniPathway; UPA00705; -.
DR   PRO; PR:P18943; -.
DR   Proteomes; UP000000539; Mitochondrion.
DR   Bgee; ENSGALG00000032142; Expressed in colon and 13 other cell types or tissues.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:AgBase.
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:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR   CDD; cd01663; Cyt_c_Oxidase_I; 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   InterPro; IPR033944; Cyt_c_oxase_su1_dom.
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; Magnesium; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Respiratory chain; Sodium; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..515
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183306"
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..170
FT                   /note="Helical; Name=IV"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        171..182
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        183..212
FT                   /note="Helical; Name=V"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        213..227
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        228..261
FT                   /note="Helical; Name=VI"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        262..269
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        270..286
FT                   /note="Helical; Name=VII"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        287..298
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        299..327
FT                   /note="Helical; Name=VIII"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        328..335
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        336..357
FT                   /note="Helical; Name=IX"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        358..370
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        371..400
FT                   /note="Helical; Name=X"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        401..406
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        407..433
FT                   /note="Helical; Name=XI"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        434..446
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        447..478
FT                   /note="Helical; Name=XII"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        479..515
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         240
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         244
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   BINDING         290
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
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         368
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         369
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         376
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         378
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         441
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   CROSSLNK        240..244
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
SQ   SEQUENCE   515 AA;  57051 MW;  29EF4E3DB9B9CDA9 CRC64;
     MTFINRWLFS TNHKDIGTLY LIFGTWAGMA GTALSLLIRA ELGQPGTLLG DDQIYNVIVT
     AHAFVMIFFM VMPIMIGGFG NWLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSTVE
     AGAGTGWTVY PPLAGNLAHA GASVDLAIFH YLAGVSSILG AINFITTIIN MKPPALSQYQ
     TPLFVWSVLI TAILLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH
     PEVYILILPG FGMISHVVAY YAGKKEPFGY MGMVWAMLSI GFLGFIVWAH HMFTVRMDVD
     TRAYFTSATM IIAIPTGIKV FSWLATLHGG TIKWDPPMLW ALGFIFLFTI GGLTGIVLAN
     SSLDIALHDT YYVVAHFHYV LSMGAVFAIL AGFTHWFPLF TGFTLHPSWT KAHFGVMFTG
     VNLTFFPQHF LGLAGMPRRY SDYPDAYTLW NTLSSIGSLI SMTAVIMLMF IVWEAFSAKR
     KVLQPELTAT NIEWIHGCPP PYHTFEEPAF VQVQE
//