ID   E2GE66_EPIPO            Unreviewed;       499 AA.
AC   E2GE66;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369};
DE            EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949, ECO:0000256|RuleBase:RU000369};
DE   Flags: Fragment;
GN   Name=COI {ECO:0000313|EMBL:ADN64858.1};
OS   Epiphyas postvittana (Light brown apple moth).
OG   Mitochondrion {ECO:0000313|EMBL:ADN64858.1}.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tortricoidea;
OC   Tortricidae; Tortricinae; Epiphyas.
OX   NCBI_TaxID=65032 {ECO:0000313|EMBL:ADN64858.1};
RN   [1] {ECO:0000313|EMBL:ADN64858.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tooman L., Rose C.J., Carraher C., Ledezma L.A., Barr N.B.;
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADN64858.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tooman L.K., Rose C.J., Carraher C., Suckling D.M., Rioux Paquette S.,
RA   Ledezma L.A., Gilligan T.M., Epstein M., Barr N.B., Newcomb R.D.;
RT   "Patterns of Mitochondrial Haplotype Diversity in the Invasive Pest
RT   Epiphyas postvittana (Lepidoptera: Tortricidae).";
RL   J. Econ. Entomol. 104:920-932(2011).
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:0000256|RuleBase:RU000369}.
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:0000256|ARBA:ARBA00029331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000256|ARBA:ARBA00029331};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}.
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:0000256|ARBA:ARBA00011164}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448,
CC       ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}.
CC   -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC       {ECO:0000256|ARBA:ARBA00009578, ECO:0000256|RuleBase:RU000369}.
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DR   EMBL; HM346386; ADN64858.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2GE66; -.
DR   UniPathway; UPA00705; -.
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; Cytochrome c oxidase-like, subunit I domain; 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; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   Pfam; PF00115; COX1; 1.
DR   PRINTS; PR01165; CYCOXIDASEI.
DR   SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR   PROSITE; PS50855; COX1; 1.
DR   PROSITE; PS00077; COX1_CUB; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Copper {ECO:0000256|RuleBase:RU000369};
KW   Electron transport {ECO:0000256|RuleBase:RU000369};
KW   Heme {ECO:0000256|RuleBase:RU000369}; Iron {ECO:0000256|RuleBase:RU000369};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369};
KW   Metal-binding {ECO:0000256|RuleBase:RU000369};
KW   Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:ADN64858.1};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000369};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000369};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}.
FT   TRANSMEM        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        364..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        397..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        435..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..497
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADN64858.1"
SQ   SEQUENCE   499 AA;  55221 MW;  B7399333725C80AC CRC64;
     GTLYFIFGIW AGMVGTSLSL LIRAELGNPG SLIGDDQIYN TIVTAHAFIM IFFMVMPIMI
     GGFGNWLVPL MLGAPDMAFP RMNNMSFWLL PPSIMLLISS SIVENGAGTG WTVYPPLSSN
     IAHSGSSVDL AIFSLHLAGI SSILGAVNFI TTIINMRPNN MSLDQMPLFV WSVGITALLL
     LLSLPVLAGA ITMLLTDRNL NTSFFDPAGG GDPILYQHLF WFFGHPEVYI LILPGFGMIS
     HIISQESGKK ETFGCLGMIY AMMAIGLLGF VVWAHHMFTV GMDIDTRAYF TSATMIIAVP
     TGIKIFSWLA TLHGTQINYS PSMLWSLGFV FLFTVGGLTG VILANSSIDV TLHDTYYVVA
     HFHYVLSMGA VFAIMGGFIH WYPLFTGLAM NPYLLKIQFF TMFIGVNLTF FPQHFLGLAG
     MPRRYSDYPD TYTSWNIISS LGSYISLIAT MLMLIIIWEP LINKRIILFP LNMNSSIEWY
     QNLPPAEHSY SELPILSNF
//