COX1_SEPOF
ID COX1_SEPOF Reviewed; 223 AA.
AC Q8WEW3; Q9ZYY9;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 84.
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=COI;
OS Sepia officinalis (Common cuttlefish).
OG Mitochondrion.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Sepiida; Sepiina; Sepiidae; Sepia.
OX NCBI_TaxID=6610;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Giribet G., Wheeler W.C.;
RT "On bivalve phylogeny: a high-level phylogeny of the mollusk class Bivalvia
RT based on a combined analysis of morphology and DNA sequence data.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-221.
RA Carlini D.B., Graves J.E.;
RT "Phylogenetic analysis of cytochrome c oxidase I sequences to determine
RT higher-level relationships within the coleoid cephalopods.";
RL Bull. Mar. Sci. 64:57-76(1999).
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:P00401};
CC Note=Binds 2 heme A groups non-covalently per subunit.
CC {ECO:0000250|UniProtKB:P00401};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00401};
CC Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401};
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 a catalytic core of 3 subunits and
CC several supernumerary subunits. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00401}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00401}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; AF120630; AAL55480.1; -; Genomic_DNA.
DR EMBL; AF000062; AAC95107.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WEW3; -.
DR SMR; Q8WEW3; -.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
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; -; 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 PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR PROSITE; PS50855; COX1; 1.
PE 3: Inferred from homology;
KW Calcium; Copper; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN <1..>223
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183416"
FT TOPO_DOM <1..4
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..46
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..69
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..88
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..130
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..153
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..173
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..196
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..223
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 47
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:P00401"
FT CONFLICT 25
FT /note="T -> S (in Ref. 2; AAC95107)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="S -> T (in Ref. 2; AAC95107)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="V -> I (in Ref. 2; AAC95107)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="A -> S (in Ref. 2; AAC95107)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="I -> L (in Ref. 2; AAC95107)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="M -> L (in Ref. 2; AAC95107)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="V -> A (in Ref. 2; AAC95107)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 223
SQ SEQUENCE 223 AA; 24364 MW; 2C48081196B6CDF4 CRC64;
IGTLYFIFGI WSGLLGTSLS LMIRTELGKP GSLLNDDQLY NVVVTAHGFV MIFFLVMPIM
IGGFGNWLVP LMLGAPDMAF PRMNNMSFWL LPPSLTLLLA SSAVESGAGT GWTVYPPLSS
NISHAGPSVD LAIFSLHLAG VSSILGAINF ITTIMNMRWE GLQMERLPLF VWSVFITAIL
LLLSLPVLAG AITMLLTDRN FNTTFFDPSG GGDPILYQHL FWF
