ID J7EIJ6_9NEOP Unreviewed; 339 AA. AC J7EIJ6; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 23-MAY-2018, entry version 23. 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=CO1 {ECO:0000313|EMBL:ADP01204.1}; OS Spodoptera pectinicornis. OG Mitochondrion {ECO:0000313|EMBL:ADP01204.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; OC Noctuoidea; Noctuidae; Amphipyrinae; Spodoptera. OX NCBI_TaxID=134412 {ECO:0000313|EMBL:ADP01204.1}; RN [1] {ECO:0000313|EMBL:ADP01204.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22939903; DOI=10.1016/j.ympev.2012.08.006; RA Kergoat G.J., Prowell D.P., Le Ru B.P., Mitchell A., Dumas P., RA Clamens A.L., Condamine F.L., Silvain J.F.; RT "Disentangling dispersal, vicariance and adaptive radiation patterns: RT A case study using armyworms in the pest genus Spodoptera RT (Lepidoptera: Noctuidae)."; RL Mol. Phylogenet. Evol. 65:855-870(2012). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {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; HQ177401; ADP01204.1; -; 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:0070469; C:respiratory chain; 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:0009060; P:aerobic respiration; IEA:InterPro. 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 Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:ADP01204.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 339 Cytochrome c oxidase subunit 1. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003791722. FT TRANSMEM 58 84 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 96 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 156 172 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 184 204 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 216 238 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 250 270 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 290 309 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 321 338 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 339 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:ADP01204.1}. FT NON_TER 339 339 {ECO:0000313|EMBL:ADP01204.1}. SQ SEQUENCE 339 AA; 37293 MW; 4503868C17DE1742 CRC64; GSPDMAFPRL NNMSFWLLPP SLTLLISSSI VENGAGTGWT VYPPLSSNIA HGGSSVDLAI FSLHLAGISS ILGAINFITT IINMRLNNLS FDQMPLFVWA VGITAFLLLL SLPVLAGAIT MLLTDRNLNT SFFDPAGGGD PILYQHLFWF LDTPKFMFXF LPGFGMISHI ISQESGKKET FGCLGMIYAM LAIGLLGFIV WAHHMFTVGM DIDTRAYFTS ATMIIAVPTG IKIFSWLATF HGTQINYSPS ILWSLGFVFL FTVGGLTGVI LSNSSIDITL HDTYYVVAHF HYVLSMGAVF AILGGFIHWY PLFTGLSLNP YMLKIQFFIM FIGVNLTFF //