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Database: UniProt
Entry: O21399
LinkDB: O21399
Original site: O21399 
ID   COX1_STRCA              Reviewed;         516 AA.
AC   O21399; O03549;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   22-FEB-2023, entry version 119.
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   Struthio camelus (Common ostrich).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=8801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9214748; DOI=10.1093/oxfordjournals.molbev.a025815;
RA   Harlid A., Janke A., Arnason U.;
RT   "The mtDNA sequence of the ostrich and the divergence between paleognathous
RT   and neognathous birds.";
RL   Mol. Biol. Evol. 14:754-761(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Harlid A.;
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sorenson M.D., Dimcheff D.E., Ast J.C., Yuri T., Mindell D.P.;
RT   "Primers for a PCR-based approach to complete mitochondrial genome
RT   sequencing.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11370967; DOI=10.1098/rspb.2001.1587;
RA   Haddrath O., Baker A.J.;
RT   "Complete mitochondrial DNA genome sequences of extinct birds: ratite
RT   phylogenetics and the vicariance biogeography hypothesis.";
RL   Proc. R. Soc. B 268:939-945(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-337.
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; Y12025; CAA72746.1; -; Genomic_DNA.
DR   EMBL; AF069429; AAD09385.1; -; Genomic_DNA.
DR   EMBL; AF338715; AAK53347.1; -; Genomic_DNA.
DR   EMBL; U76062; AAB61328.1; -; Genomic_DNA.
DR   PIR; C90612; C90612.
DR   PIR; T12411; T12411.
DR   RefSeq; NP_115443.1; NC_002785.1.
DR   AlphaFoldDB; O21399; -.
DR   SMR; O21399; -.
DR   GeneID; 803279; -.
DR   CTD; 4512; -.
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   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   Respiratory chain; Sodium; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..516
FT                   /note="Cytochrome c oxidase subunit 1"
FT                   /id="PRO_0000183422"
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..336
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        337..358
FT                   /note="Helical; Name=IX"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        359..371
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        372..401
FT                   /note="Helical; Name=X"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        402..407
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        408..434
FT                   /note="Helical; Name=XI"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        435..447
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TRANSMEM        448..479
FT                   /note="Helical; Name=XII"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   TOPO_DOM        480..516
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   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         370
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         377
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         379
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         442
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
FT   CROSSLNK        241..245
FT                   /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:P00396"
SQ   SEQUENCE   516 AA;  56932 MW;  33FFEC4806D80856 CRC64;
     MTFITRWLFS TNHKDIGTLY LIFGAWAGMV GTALSLLIRA ELGQPGTLLG DDQIYNVIVT
     AHAFVMIFFM VMPVMIGGFG NWLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSTVE
     AGAGTGWTVY PPLAGNLAHA GASVDLAIFS LHLAGVSSIL GAINFITTAI NMKPPALSQY
     QTPLFVWSVL ITAILLLLSL PVLAAGITML LTDRNLNTTF FDPAGGGDPV LYQHLFWFFG
     HPEVYILILP GFGIISHVVT YYAGKKEPFG YMGMVWAMLS IGFLGFIVWA HHMFTVGMDV
     DTRAYFTSAT MIIAIPTGIK VFSWLATLHG GTIKWDPPIL WALGFIFLFT IGGLTGIVLA
     NSSLDIALHD TYYVVAHFHY VLSMGAVFAI LAGFTHWFPL FTGYTLHPTW AKAHFGVMFT
     GVNLTFFPQH FLGLAGMPRR YSDYPDAYTL WNTMSSIGSL ISMTAVIMLM FIIWEAFSSK
     RKVLQPELIA TNIEWIHGCP PPHHTFEEPA FVQVQE
//
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