ID A0A514E8C8_TETUR Unreviewed; 381 AA. AC A0A514E8C8; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 17-JUN-2020, entry version 5. 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:QDI02282.1}; OS Tetranychus urticae (Two-spotted spider mite). OG Mitochondrion {ECO:0000313|EMBL:QDI02282.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari; OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae; OC Tetranychoidea; Tetranychidae; Tetranychus. OX NCBI_TaxID=32264 {ECO:0000313|EMBL:QDI02282.1}; RN [1] {ECO:0000313|EMBL:QDI02282.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=GSS {ECO:0000313|EMBL:QDI02282.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:QDI02282.1}; RX PubMed=31250237; DOI=.1007/s10493-019-00398-w; RA Inak E., Alpkent Y.N., Cobanoglu S., Dermauw W., Van Leeuwen T.; RT "Resistance incidence and presence of resistance mutations in populations RT of Tetranychus urticae from vegetable crops in Turkey."; RL Exp. Appl. Acarol. 78:343-360(2019). 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; EC=7.1.1.9; 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; MK508722; QDI02282.1; -; 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: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 InterPro; IPR023615; Cyt_c_Oxase_su1_BS. 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|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:QDI02282.1}; 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 33..54 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 75..97 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 117..142 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 154..182 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 214..233 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 245..262 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 274..295 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 307..328 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 348..370 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..369 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QDI02282.1" FT NON_TER 381 FT /evidence="ECO:0000313|EMBL:QDI02282.1" SQ SEQUENCE 381 AA; 42867 MW; DB418F644283EFF0 CRC64; GTSMSIIIRL ELMTPGSLIQ NDFIYNSMVT THAMIMIFFM VMPAMIGGFG NWLIPLMINT VDLCFPRINN MSFWLLIPSL MLMISSSMKS VLNGVGWTMY PPLTSIQYFM SSSIEMMIFS LHIAGISSIA SSINFISTIL LMKNKNYFLS NLTLFSLSIL ITTFLLLLAL PVLAGAITMI LMDRNFNTSF FDPSGGGDPI LYQHLFWFFG HPEVYILILP GFGMISHVIS YNLGKKEVFG KIGMMFAMMS IGLLGFIVWA HHMFTVGMDV DTRAYFTAAT MIIAIPTGIK IFSWFTTILN SHINFNISMY WSMGFLIMFS IGGFTGIVAS NSCLDINLHD SYYIVAHFHY VLSMGAVFAI FSGLFLWIPL NNMMYILMMM C //