COX1_DORPE
ID COX1_DORPE Reviewed; 223 AA.
AC Q8WEW4; Q9ZYZ9;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 85.
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 Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii).
OG Mitochondrion.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Doryteuthis.
OX NCBI_TaxID=1051067;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-221.
RC STRAIN=Isolate A-A128, Isolate A-R1, Isolate B-A25, Isolate B-B233,
RC Isolate B-C13, Isolate B-R11, Isolate B-R59, Isolate C-A52, Isolate D-R2,
RC Isolate E-A55, Isolate F-C70, Isolate G-B35, Isolate G-R46, Isolate H-A123,
RC Isolate H-A80, Isolate H-S26, Isolate I-C7, Isolate J-C39, Isolate K-A92,
RC Isolate L-A63, and Isolate M-C50;
RA Herke S.W., Foltz D.W.;
RT "Phylogeography of two Loligo squid (Cephalopoda: Myopsida) in the Gulf of
RT Mexico and the northwestern Atlantic Ocean.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-221.
RC STRAIN=Isolate B-B233, Isolate B-C13, and Isolate B-R59;
RA Herke S.W., Foltz D.W.;
RT "Phylogeography of two squid (Loligo pealei and L. plei) in the Gulf of
RT Mexico and Northwestern Atlantic Ocean.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF120629; AAL55479.1; -; Genomic_DNA.
DR EMBL; AF000052; AAC95097.1; -; Genomic_DNA.
DR EMBL; AF207923; AAF20964.1; -; Genomic_DNA.
DR EMBL; AF207909; AAF20950.1; -; Genomic_DNA.
DR EMBL; AF207910; AAF20951.1; -; Genomic_DNA.
DR EMBL; AF207911; AAF20952.1; -; Genomic_DNA.
DR EMBL; AF207912; AAF20953.1; -; Genomic_DNA.
DR EMBL; AF207913; AAF20954.1; -; Genomic_DNA.
DR EMBL; AF207914; AAF20955.1; -; Genomic_DNA.
DR EMBL; AF207915; AAF20956.1; -; Genomic_DNA.
DR EMBL; AF207916; AAF20957.1; -; Genomic_DNA.
DR EMBL; AF207917; AAF20958.1; -; Genomic_DNA.
DR EMBL; AF207918; AAF20959.1; -; Genomic_DNA.
DR EMBL; AF207919; AAF20960.1; -; Genomic_DNA.
DR EMBL; AF207920; AAF20961.1; -; Genomic_DNA.
DR EMBL; AF207921; AAF20962.1; -; Genomic_DNA.
DR EMBL; AF207922; AAF20963.1; -; Genomic_DNA.
DR EMBL; AF207924; AAF20965.1; -; Genomic_DNA.
DR EMBL; AF207925; AAF20966.1; -; Genomic_DNA.
DR EMBL; AF207926; AAF20967.1; -; Genomic_DNA.
DR EMBL; AY039621; AAK73250.1; -; Genomic_DNA.
DR EMBL; AY039622; AAK73251.1; -; Genomic_DNA.
DR EMBL; AY039623; AAK73252.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WEW4; -.
DR SMR; Q8WEW4; -.
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_0000183356"
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 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 NON_TER 1
FT NON_TER 223
SQ SEQUENCE 223 AA; 24373 MW; 440EF0D5B4514979 CRC64;
IGTLYFMFGI WAGLVGTSLS LMIRTELGKP GSLLNDDQLY NVVVTAHGFI MIFFMVMPIM
IGGFGNWLVP LMLGAPDMAF PRMNNMSFWL LPPSLTLLLA SSAVESGAGT GWTVYPPLSS
NLSHAGPSVD LAIFSLHLAG ISSILGAINF ITTIMNMRWE GLLMERLSLF VWSVFITAIL
LLLSLPVLAG AITMLLTDRN FNTTFFDPSG GGDPILYQHL FWF
