COX1_DIDVI
ID COX1_DIDVI Reviewed; 513 AA.
AC P41310;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS virginiana).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX NCBI_TaxID=9267;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8056314; DOI=10.1093/genetics/137.1.243;
RA Janke A., Feldmaier-Fuchs G., Thomas K., von Haeseler A., Paabo S.;
RT "The marsupial mitochondrial genome and the evolution of placental
RT mammals.";
RL Genetics 137:243-256(1994).
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; Z29573; CAA82679.1; -; Genomic_DNA.
DR PIR; S47872; S47872.
DR RefSeq; NP_007097.1; NC_001610.1.
DR AlphaFoldDB; P41310; -.
DR SMR; P41310; -.
DR GeneID; 807779; -.
DR CTD; 4512; -.
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..513
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183322"
FT TOPO_DOM 1..11
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 12..40
FT /note="Helical; Name=I"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 41..50
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 51..86
FT /note="Helical; Name=II"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 87..94
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 95..117
FT /note="Helical; Name=III"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TOPO_DOM 118..140
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT TRANSMEM 141..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..513
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 40
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 45
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 61
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 513 AA; 57002 MW; FFDAF8036663E8C0 CRC64;
MFINRWLFST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLIGD DQIYNVIVTA
HAFIMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLASSTIEA
GAGTGWTVYP PLAGNLAHAG ASVDLAIFSL HLAGISSILG AINFITTIIN MKPPAMSQYQ
TPLFVWSVMI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH
PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGLDVD
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMLW ALGFIFLFTI GGLTGIVLAN
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFVHWFPLF TGYMLNDMWA KIHFFIMFVG
VNLTFFPQHF LGLSGMPRRY SDYPDAYTMW NVVSSIGSFI SLTAVILMVF IIWEAFASKR
EVLDVELTTT NIEWLYGCPP PYHTFEQPVF IKA
