COX1_STRCA
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 03-AUG-2022, entry version 117.
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 OrthoDB; 728231at2759; -.
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 CDD; cd01663; Cyt_c_Oxidase_I; 1.
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 InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR033944; Cyt_c_oxase_su1_dom.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 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
