COX3_WHEAT
ID COX3_WHEAT Reviewed; 265 AA.
AC P15953;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
GN Name=COX3;
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].
RC STRAIN=cv. Capitole;
RX PubMed=2155710; DOI=10.1007/bf00313247;
RA Gualberto J.M., Domon C., Weil J.H., Grienenberger J.-M.;
RT "Structure and transcription of the gene coding for subunit 3 of cytochrome
RT oxidase in wheat mitochondria.";
RL Curr. Genet. 17:41-47(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Capitole; TISSUE=Etiolated plantlet;
RX PubMed=1588598; DOI=10.1007/bf00162974;
RA Karlovsky P., Fartmann B.;
RT "Genetic code and phylogenetic origin of oomycetous mitochondria.";
RL J. Mol. Evol. 34:254-258(1992).
RN [3]
RP RNA EDITING.
RX PubMed=1695731; DOI=10.1093/nar/18.13.3771;
RA Gualberto J.M., Weil J.H., Grienenberger J.M.;
RT "Editing of the wheat coxIII transcript: evidence for twelve C to U and one
RT U to C conversions and for sequence similarities around editing sites.";
RL Nucleic Acids Res. 18:3771-3776(1990).
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:P00420}.
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:P00420};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00420};
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:P00420}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00420}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00420}.
CC -!- RNA EDITING: Modified_positions=82 {ECO:0000269|PubMed:1695731}, 86
CC {ECO:0000269|PubMed:1695731}, 97 {ECO:0000269|PubMed:1695731}, 104
CC {ECO:0000269|PubMed:1695731}, 105 {ECO:0000269|PubMed:1695731}, 138
CC {ECO:0000269|PubMed:1695731}, 141 {ECO:0000269|PubMed:1695731}, 171
CC {ECO:0000269|PubMed:1695731}, 176 {ECO:0000269|PubMed:1695731}, 189
CC {ECO:0000269|PubMed:1695731}, 252 {ECO:0000269|PubMed:1695731}, 255
CC {ECO:0000269|PubMed:1695731};
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; X52539; CAA36775.1; -; mRNA.
DR EMBL; X15944; CAA34071.1; ALT_SEQ; Genomic_DNA.
DR PIR; S10331; OTWT3M.
DR RefSeq; YP_398397.1; NC_007579.1.
DR AlphaFoldDB; P15953; -.
DR SMR; P15953; -.
DR STRING; 4565.EPlTAEP00000010091; -.
DR eggNOG; KOG4664; Eukaryota.
DR ExpressionAtlas; P15953; baseline.
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:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR CDD; cd01665; Cyt_c_Oxidase_III; 1.
DR Gene3D; 1.20.120.80; -; 1.
DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3.
DR InterPro; IPR033945; Cyt_c_oxase_su3_dom.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR PANTHER; PTHR11403; PTHR11403; 1.
DR Pfam; PF00510; COX3; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR PROSITE; PS50253; COX3; 1.
PE 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; RNA editing;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..265
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183871"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 265 AA; 29796 MW; A7918C9FBFC22608 CRC64;
MIESQRHSYH LVDPSPWPIS GSLGALATTV GGVMYMHSFQ GGATLLSLGL IFILYTMFVW
WRDVLRESTL EGHHTKAVQL GLRYGFILFI VSEVMFFFAF FWAFFHSSLA PTVEIGGIWP
PKGIGVLDPW EIPLLNTLIL LSSGAAVTWA HHAILAGKEK RAVYALVATV LLALVFTGFQ
GMEYYQAPFT ISDSIYGSTF FLATGFHGFH VIIGTLFLIV CGIRQYLGQM TKKHHVGFEA
AAWYWHFVDV VWLFLFVSIY WWGGI
