ID E2GE66_EPIPO Unreviewed; 499 AA. AC E2GE66; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 22-APR-2020, entry version 38. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {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; Holometabola; 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] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; CC Evidence={ECO:0000256|RuleBase:RU000369}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|RuleBase:RU000369}. 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; HM346386; ADN64858.1; -; Genomic_DNA. 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:0009060; P:aerobic respiration; IEA:InterPro. 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 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|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711163, KW ECO:0000256|SAM:Phobius}; 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 Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122, 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="COX1" 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 //