ID A0A076JDS2_9MUSC Unreviewed; 511 AA. AC A0A076JDS2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 26-FEB-2020, entry version 22. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; GN Name=COI {ECO:0000313|EMBL:AII71820.1}; OS Liriomyza langei. OG Mitochondrion {ECO:0000313|EMBL:AII71820.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; Opomyzoidea; OC Agromyzidae; Phytomyzinae; Liriomyza. OX NCBI_TaxID=1484199 {ECO:0000313|EMBL:AII71820.1}; RN [1] {ECO:0000313|EMBL:AII71820.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Lang25 {ECO:0000313|EMBL:AII71878.1}, Lang36 RC {ECO:0000313|EMBL:AII71820.1}, Lang44 {ECO:0000313|EMBL:AII71884.1}, RC and Lang8 {ECO:0000313|EMBL:AII71802.1}; RA Scheffer S.J., Lewis M.L., Gaimari S.D., Reitz S.R.; RT "Molecular Survey for the Invasive Leafminer Pest Liriomyza huidobrensis RT (Diptera: Agromyzidae) in California Uncovers Only the Native Pest RT Liriomyza langei."; RL J. Econ. Entomol. 107:1959-1964(2014). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {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; EC=1.9.3.1; CC Evidence={ECO:0000256|RuleBase:RU000369, CC ECO:0000256|SAAS:SAAS01116619}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00887552}. 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; KJ778705; AII71802.1; -; Genomic_DNA. DR EMBL; KJ778714; AII71820.1; -; Genomic_DNA. DR EMBL; KJ778743; AII71878.1; -; Genomic_DNA. DR EMBL; KJ778746; AII71884.1; -; 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, ECO:0000256|SAAS:SAAS00887236}; KW Electron transport {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711094}; KW Heme {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711161}; KW Iron {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711183}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711163, KW ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711155}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711157, ECO:0000313|EMBL:AII71820.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711097}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711106}; 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}; KW Transport {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711099}. FT TRANSMEM 12..35 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 55..81 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 102..124 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 144..169 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 181..208 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 228..249 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 270..289 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 301..325 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 337..357 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 377..398 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 410..428 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 448..471 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..510 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" SQ SEQUENCE 511 AA; 56597 MW; A7B5B038BEBAE46F CRC64; MRQWLFSTNH KDIGTLYFMF GAWSGMVGTS LSILIRAELG HPGALIGDDQ IYNVIVTAHA FIMIFFMVMP IMIGGFGNWL VPLMLGAPDM AFPRMNNMSF WLLPPALTLL LMSSMVENGA GTGWTVYPPL SSIIAHGGAS VDLAIFSLHL AGISSILGAV NFITTIINMR STGITFDRMP LFVWSVLITA ILLLLSLPVL AGAITMLLTD RNFNTSFFDP AGGGDPILYQ HLFWFFGHPE VYILILPGFG MISHIISHES GKKETFGSLG MIYAMLAIGL LGFIVWAHHM FTVGLDVDTR AYFTSATMII AVPTGIKIFS WLATLHGTQL SYTPTTLWSL GFVFLFTVGG LTGVVLANSS IDVVLHDTYY VVAHFHYVLS MGAVFAIMAG FIHWYPLFTG LSLNVKLLKS QFFIMFIGVN LTFFPQHFLG LAGMPRRYSD YPDAYTAWNV ISTIGSSISL LGIILFLYII WESMMTQRQV IFPIQLNSSI EWYQNTPPAE HSYSELPMLT N //