ID A0AA51RLH9_9HEMI Unreviewed; 214 AA.
AC A0AA51RLH9;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 24-JUL-2024, entry version 4.
DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|ARBA:ARBA00015946, ECO:0000256|RuleBase:RU000457};
GN Name=COII {ECO:0000313|EMBL:WMQ72144.1};
OS Okanagana arctostaphylae.
OG Mitochondrion {ECO:0000313|EMBL:WMQ72144.1}.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Cicadoidea; Cicadidae;
OC Tibicininae; Tibicinini; Okanagana.
OX NCBI_TaxID=3027814 {ECO:0000313|EMBL:WMQ72144.1};
RN [1] {ECO:0000313|EMBL:WMQ72144.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SING01075 {ECO:0000313|EMBL:WMQ72144.1};
RA Cole J.A., Chatfield-Taylor W., Smeds E.A., Gonzalez V.A., Wong C.;
RT "Phylogeny of the largest cicada radiation in North America redefines
RT Tibicinoides and Okanagana (Hemiptera: Auchenorrhyncha: Cicadidae:
RT Tibicininae).";
RL Submitted (FEB-2023) 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}.
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DR EMBL; OQ427948; WMQ72144.1; -; Genomic_DNA.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:TreeGrafter.
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:WMQ72144.1};
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 16..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..79
FT /note="Cytochrome oxidase subunit II transmembrane region
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50999"
FT DOMAIN 80..213
FT /note="Cytochrome oxidase subunit II copper A binding"
FT /evidence="ECO:0000259|PROSITE:PS50857"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:WMQ72144.1"
SQ SEQUENCE 214 AA; 24877 MW; 0F7B8F9B63BBF3B1 CRC64;
MSPMMEQLIF FHDHTLVILI VITVIVGYMM STLFLNNMID RLLLEGQLIE FIWTLLPAMT
LIFIALPSLR LLYLLDEVNN PSLTIKIIGH QWYWSYEYSD FLNVEFDSYM KSMDNLNKSE
FRLIEVDNRM ILPFNTQIRL MITSTDVLHS WATPSLGIKV DAVPGRLNQA SIMINRPGLI
YGQCSEICGS NHSFMPIVIE SINNKMFLNW LKNY
//