ID A0A068BA71_9NEOP Unreviewed; 265 AA. AC A0A068BA71; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 22-APR-2020, entry version 19. 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; OS Micrarchus sp. n. 2 LTD-2014. OG Mitochondrion {ECO:0000313|EMBL:AIC79428.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Polyneoptera; Phasmatodea; Verophasmatodea; Anareolatae; OC Diapheromeridae; Pachymorphinae; Micrarchus; unclassified Micrarchus. OX NCBI_TaxID=1448259 {ECO:0000313|EMBL:AIC79428.1}; RN [1] {ECO:0000313|EMBL:AIC79428.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MMT004 {ECO:0000313|EMBL:AIC79388.1}, MMT027 RC {ECO:0000313|EMBL:AIC79424.1}, MMT028 {ECO:0000313|EMBL:AIC79426.1}, RC MMT029 {ECO:0000313|EMBL:AIC79428.1}, MMT032 RC {ECO:0000313|EMBL:AIC79434.1}, and MMT056 RC {ECO:0000313|EMBL:AIC79478.1}; RX PubMed=24762129; DOI=10.1111/mec.12767; RA Dunning L.T., Dennis A.B., Sinclair B.J., Newcomb R.D., Buckley T.R.; RT "Divergent transcriptional responses to low temperature among populations RT of alpine and lowland species of New Zealand stick insects (Micrarchus)."; RL Mol. Ecol. 23:2712-2726(2014). 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; KJ142656; AIC79388.1; -; Genomic_DNA. DR EMBL; KJ142674; AIC79424.1; -; Genomic_DNA. DR EMBL; KJ142675; AIC79426.1; -; Genomic_DNA. DR EMBL; KJ142676; AIC79428.1; -; Genomic_DNA. DR EMBL; KJ142679; AIC79434.1; -; Genomic_DNA. DR EMBL; KJ142701; AIC79478.1; -; 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 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:AIC79428.1}; 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, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 21..42 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 54..77 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 89..108 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 128..147 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 159..178 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 198..224 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..263 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AIC79428.1" SQ SEQUENCE 265 AA; 29812 MW; F47F4A1E3930D668 CRC64; GFGMISHIIA HESGKKEVFG NLGMIFAMGA IGLLGFVVWA HHMFTVGMDV DTRAYFTSAT MIIAVPTGIK VFSWLATMYG SKLTLSPPCL WAMGFVFLFT LGGLTGIVLS NSSIDITLHD TYYVVAHFHY VLSMGAVFAI MAGFIQWFPL FTGMSMNPLW LKIQFTTMFI GVNMTFFPQH FLGLAGMPRR YSDYPDMFTA WNIISSMGAI ISMVSMMMFI MIMWESLSSM RQTIFSSHMT SSLEWNHNLP PTEHTYNELP ILIKF //