COX1_APILI
ID COX1_APILI Reviewed; 521 AA.
AC P20374; Q8LUG0; Q8LXP4; Q8LXP6; Q8LXP7;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
GN Name=COI;
OS Apis mellifera ligustica (Common honeybee) (Italian honeybee).
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7469;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Thorax;
RX PubMed=2559293; DOI=10.1093/oxfordjournals.molbev.a040553;
RA Crozier R.H., Crozier Y.C., Mackinlay A.G.;
RT "The CO-I and CO-II region of honeybee mitochondrial DNA: evidence for
RT variation in insect mitochondrial evolutionary rates.";
RL Mol. Biol. Evol. 6:399-411(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Thorax;
RX PubMed=8417993; DOI=10.1093/genetics/133.1.97;
RA Crozier R.H., Crozier Y.C.;
RT "The mitochondrial genome of the honeybee Apis mellifera: complete sequence
RT and genome organization.";
RL Genetics 133:97-117(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-507.
RC STRAIN=Isolate ligus2, Isolate ligus3, Isolate ligus4, Isolate ligus5,
RC Isolate ligus6, Isolate ligus7, Isolate ligus8, and Isolate ligus9;
RA Marino A., Mantovani B., Carpana E., Sabatini A.G., Lodesani M.;
RT "ND2 and CO1 mitochondrial genes in Apis mellifera L.: a molecular approach
RT to Mediterranean populations monitoring.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-521.
RX PubMed=1649072; DOI=10.1093/genetics/128.2.393;
RA Cornuet J.-M., Garnery L., Solignac M.;
RT "Putative origin and function of the intergenic region between COI and COII
RT of Apis mellifera L. mitochondrial DNA.";
RL Genetics 128:393-403(1991).
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; M23409; AAA18476.1; -; Genomic_DNA.
DR EMBL; L06178; AAB96799.1; -; Genomic_DNA.
DR EMBL; AY114452; AAM76437.1; -; Genomic_DNA.
DR EMBL; AY114453; AAM76438.1; -; Genomic_DNA.
DR EMBL; AY114454; AAM76439.1; -; Genomic_DNA.
DR EMBL; AY114455; AAM76440.1; -; Genomic_DNA.
DR EMBL; AY114456; AAM76441.1; -; Genomic_DNA.
DR EMBL; AY114457; AAM76442.1; -; Genomic_DNA.
DR EMBL; AY114458; AAM76443.1; -; Genomic_DNA.
DR EMBL; AY114460; AAM76445.1; -; Genomic_DNA.
DR PIR; A32431; A32431.
DR RefSeq; NP_008083.1; NC_001566.1.
DR AlphaFoldDB; P20374; -.
DR SMR; P20374; -.
DR GeneID; 807695; -.
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; IEA:InterPro.
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; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..521
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183284"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 43
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 59
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 BINDING 238
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 242
FT /ligand="O2"
FT /ligand_id="ChEBI:CHEBI:15379"
FT /evidence="ECO:0000250|UniProtKB:P00396"
FT BINDING 288
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 289
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with subunit 2"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 367
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with subunit 2"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT BINDING 374
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:P00401"
FT BINDING 376
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 CROSSLNK 238..242
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:P00401"
FT VARIANT 108
FT /note="F -> L (in strain: Isolate ligus8)"
FT VARIANT 270
FT /note="S -> G (in strain: Isolate ligus8)"
FT VARIANT 271
FT /note="M -> I (in strain: Isolate ligus2)"
FT VARIANT 437
FT /note="R -> P (in strain: Isolate ligus7)"
SQ SEQUENCE 521 AA; 59294 MW; 2149417AC981CE64 CRC64;
MMKWFMSTNH KNIGILYIIL ALWSGMLGSS MSLIIRMELS SPGSWISNDQ IYNTIVTSHA
FLMIFFMVMP FLIGGFGNWL IPLMLGSPDM AFPRMNNISF WLLPPSLFML LLSNLFYPSP
GTGWTVYPPL SAYLYHSSPS VDFAIFSLHM SGISSIMGSL NLMVTIMMMK NFSMNYDQIS
LFPWSVFITA ILLIMSLPVL AGAITMLLFD RNFNTSFFDP MGGGDPILYQ HLFWFFGHPE
VYILILPGFG LISHIVMNES GKKEIFGNLS MIYAMLGIGF LGFIVWAHHM FTVGLDVDTR
AYFTSATMII AVPTGIKVFS WLATYHGSKL KLNISILWSL GFIMLFTIGG LTGIMLSNSS
IDIILHDTYY VVGHFHYVLS MGAVFAIISS FIHWYPLITG LLLNIKWLKI QFIMMFIGVN
LTFFPQHFLG LMSMPRRYSD YPDSYYCWNS ISSMGSMISL NSMIFLIFII LESLISKRML
LFKFNQSSLE WLNFLPPLDH SHLEIPLLIK NLNLKSILIK F
