ID A0AA96UTN1_9CUCU Unreviewed; 227 AA. AC A0AA96UTN1; DT 27-MAR-2024, integrated into UniProtKB/TrEMBL. DT 27-MAR-2024, sequence version 1. DT 29-MAY-2024, entry version 2. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|ARBA:ARBA00015946, ECO:0000256|RuleBase:RU000457}; DE Flags: Fragment; GN Name=COX2 {ECO:0000313|EMBL:WNX91356.1}; OS Mandalotina sp. OG Mitochondrion {ECO:0000313|EMBL:WNX91356.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia; OC Curculionidae; Cyclominae; Mandalotina. OX NCBI_TaxID=2970825 {ECO:0000313|EMBL:WNX91356.1}; RN [1] {ECO:0000313|EMBL:WNX91356.1} RP NUCLEOTIDE SEQUENCE. RA Hsiao Y., Oberprieler R.G., Zwick A., Zhou Y.-L., Slipinski A.; RT "Instead of 300-million-year-old twosome-museomics unveil systematics, RT speciation and a Miocene origin of Australian cycad-pollinating weevils RT (Coleoptera: Curculionoidea), mirroring the diversification of Australian RT cycads."; RL Submitted (JUL-2022) 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:RU000457}. 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:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000457}; CC Note=Binds a copper A center. {ECO:0000256|RuleBase:RU000457}; 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU000457}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000457}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000256|ARBA:ARBA00007866, ECO:0000256|RuleBase:RU000457}. 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; OP134428; WNX91356.1; -; Genomic_DNA. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR CDD; cd13912; CcO_II_C; 1. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1. DR InterPro; IPR045187; CcO_II. DR InterPro; IPR002429; CcO_II-like_C. DR InterPro; IPR034210; CcO_II_C. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom. DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf. DR PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1. DR PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR PRINTS; PR01166; CYCOXIDASEII. DR SUPFAM; SSF49503; Cupredoxins; 1. DR SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 1. DR PROSITE; PS00078; COX2; 1. DR PROSITE; PS50857; COX2_CUA; 1. DR PROSITE; PS50999; COX2_TM; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000457}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU000457}; Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000457}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU000457}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, ECO:0000313|EMBL:WNX91356.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU000457}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000457}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000457}. FT TRANSMEM 28..51 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 63..87 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..91 FT /note="Cytochrome oxidase subunit II transmembrane region FT profile" FT /evidence="ECO:0000259|PROSITE:PS50999" FT DOMAIN 92..225 FT /note="Cytochrome oxidase subunit II copper A binding" FT /evidence="ECO:0000259|PROSITE:PS50857" FT NON_TER 227 FT /evidence="ECO:0000313|EMBL:WNX91356.1" SQ SEQUENCE 227 AA; 26333 MW; 5EA39607CFEB433F CRC64; MATWKTILLQ DSASPLMEQL MFFHDHTMMI LIIITILVTQ VLIGILYNTF LNRFLLEGQT IEIIWTILPA LTLIVIALPS LRLLYILDEI NNPMISIKAI GHQWYWSYEY SDYKNLEFNS YMIPTNELKL FNFRLLDVDT RMTIPFMTQI RLIVTSTDVI HSWTIPSLGI KIDGTPGRLN QMGFSINRTG LFYGQCSEIC GANHSFMPIV IESIHPVFFL HWILTQN //