COX2_WHEAT
ID COX2_WHEAT Reviewed; 260 AA.
AC P00413;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
GN Name=COX2; Synonyms=COII, COXII;
OS Triticum aestivum (Wheat).
OG Mitochondrion.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16453565; DOI=10.1002/j.1460-2075.1984.tb02168.x;
RA Bonen L., Boer P.H., Gray M.W.;
RT "The wheat cytochrome oxidase subunit II gene has an intron insert and
RT three radical amino acid changes relative to maize.";
RL EMBO J. 3:2531-2536(1984).
RN [2]
RP RNA EDITING.
RX PubMed=2552325; DOI=10.1038/341660a0;
RA Gualberto J.M., Lamattina L., Bonnard G., Weil J.-H., Grienenberger J.-M.;
RT "RNA editing in wheat mitochondria results in the conservation of protein
RT sequences.";
RL Nature 341:660-662(1989).
RN [3]
RP RNA EDITING.
RX PubMed=2552326; DOI=10.1038/341662a0;
RA Covello P.S., Gray M.W.;
RT "RNA editing in plant mitochondria.";
RL Nature 341:662-666(1989).
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:0000250|UniProtKB:P00410}.
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:0000250|UniProtKB:P00410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC Note=Binds a dinuclear copper A center per subunit.
CC {ECO:0000250|UniProtKB:P00410};
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:0000250|UniProtKB:P00410}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00410}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00410}.
CC -!- RNA EDITING: Modified_positions=26 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 56 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 57 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 87 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 129 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 130 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 188 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 196 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 207 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 213 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 228 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326}, 235 {ECO:0000269|PubMed:2552325,
CC ECO:0000269|PubMed:2552326};
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; X01108; CAA25581.1; ALT_SEQ; Genomic_DNA.
DR PIR; A00481; OBWT2.
DR RefSeq; YP_398417.1; NC_007579.1.
DR AlphaFoldDB; P00413; -.
DR SMR; P00413; -.
DR STRING; 4565.EPlTAEP00000010097; -.
DR eggNOG; KOG4767; Eukaryota.
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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR CDD; cd13912; CcO_II_C; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 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; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR02866; CoxB; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 2: Evidence at transcript level;
KW Copper; Electron transport; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW RNA editing; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..260
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183714"
FT TOPO_DOM 1..43
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..84
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..260
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 189
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 224
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 224
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 226
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with subunit 1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 228
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 228
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 232
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 235
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
SQ SEQUENCE 260 AA; 29515 MW; 272F3C4573DA066D CRC64;
MILRSLSCRF LTIALCDAAE PWQLGFQDAA TPMMQGIIDL HHDIFFFLIL ILVFVLWMLV
RALWHFNEQT NPIPQRIVHG TTIEIIWTIF PSVILLFIAI PSFALLYSMD GVLVDPAITI
KAIGHQWYWT YEYSDYNSSD EQSLTFDSYT IPEDDPELGQ SRLLEVDNRV VVPAKTHLRM
IVTPADVLHS WAVPSLGVKC DAVPGRLNLT SILVQREGVY YGQCSEICGT NHAFMPIVVE
AVTLKDYADW VSNQLILQTN
