ID A0A0N7EV94_9DIPT Unreviewed; 183 AA. AC A0A0N7EV94; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 19-JAN-2022, entry version 22. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:ALF74250.1}; OS Orthocladiinae sp. BOLD:ABA1222. OG Mitochondrion {ECO:0000313|EMBL:ALF74250.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae; OC unclassified Orthocladiinae. OX NCBI_TaxID=1724779 {ECO:0000313|EMBL:ALF74250.1}; RN [1] {ECO:0000313|EMBL:ALF74250.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26379469; RA Telfer A.C., Young M.R., Quinn J., Perez K., Sobel C.N., Sones J.E., RA Levesque-Beaudin V., Derbyshire R., Fernandez-Triana J., Rougerie R., RA Thevanayagam A., Boskovic A., Borisenko A.V., Cadel A., Brown A., Pages A., RA Castillo A.H., Nicolai A., Glenn Mockford B.M., Bukowski B., Wilson B., RA Trojahn B., Lacroix C.A., Brimblecombe C., Hay C., Ho C., Steinke C., RA Warne C.P., Garrido Cortes C., Engelking D., Wright D., Lijtmaer D.A., RA Gascoigne D., Hernandez Martich D., Morningstar D., Neumann D., Steinke D., RA Marco DeBruin D.D., Dobias D., Sears E., Richard E., Damstra E., RA Zakharov E.V., Laberge F., Collins G.E., Blagoev G.A., Grainge G., RA Ansell G., Meredith G., Hogg I., McKeown J., Topan J., Bracey J., RA Guenther J., Sills-Gilligan J., Addesi J., Persi J., Layton K.K., RA D'Souza K., Dorji K., Grundy K., Nghidinwa K., Ronnenberg K., Lee K.M., RA Xie L., Lu L., Penev L., Gonzalez M., Rosati M.E., Kekkonen M., Kuzmina M., RA Iskandar M., Mutanen M., Fatahi M., Pentinsaari M., Bauman M., Nikolova N., RA Ivanova N.V., Jones N., Weerasuriya N., Monkhouse N., Lavinia P.D., RA Jannetta P., Hanisch P.E., McMullin R.T., Ojeda Flores R., Mouttet R., RA Vender R., Labbee R.N., Forsyth R., Lauder R., Dickson R., Kroft R., RA Miller S.E., MacDonald S., Panthi S., Pedersen S., Sobek-Swant S., Naik S., RA Lipinskaya T., Eagalle T., Decaens T., Kosuth T., Braukmann T., RA Woodcock T., Roslin T., Zammit T., Campbell V., Dinca V., Peneva V., RA Hebert P.D., deWaard J.R.; RT "Biodiversity inventories in high gear: DNA barcoding facilitates a rapid RT biotic survey of a temperate nature reserve."; RL Biodivers Data J 3:E6313-E6313(2015). RN [2] {ECO:0000313|EMBL:ALF74250.1} RP NUCLEOTIDE SEQUENCE. RG Swine Surveillance; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. 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:ARBA00024637}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00024637}; 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: 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|ARBA:ARBA00009578, 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; KT702898; ALF74250.1; -; 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:respirasome; 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: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}; 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, ECO:0000313|EMBL:ALF74250.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 18..48 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 111..136 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 148..175 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..183 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ALF74250.1" FT NON_TER 183 FT /evidence="ECO:0000313|EMBL:ALF74250.1" SQ SEQUENCE 183 AA; 19587 MW; F9FE4C1EFF251837 CRC64; LIRAELGHSG SLIGDDQIYN VIVTAHAFVM IFFMVMPILI GGFGNWLVPL MLGAPDMAFP RMNNMSFWLL PPSLTLLLSS SIVENGAGTG WTVYPPLSSG IAHAGASVDL AIFSLHLAGI SSILGAVNFI TTVINMRSEG ISYDRMPLFV WSVIITAILL LLSLPVLAGA ITMLLTDRNL NTS //