COX3_EMEND
ID COX3_EMEND Reviewed; 269 AA.
AC P00421;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-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; Synonyms=oxiC;
OS Emericella nidulans (Aspergillus nidulans).
OG Mitochondrion.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=162425;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=pabaA1 biA1;
RX PubMed=6290989; DOI=10.1093/nar/10.15.4783;
RA Netzker R., Koechel H.G., Basak N., Kuentzel H.;
RT "Nucleotide sequence of Aspergillus nidulans mitochondrial genes coding for
RT ATPase subunit 6, cytochrome oxidase subunit 3, seven unidentified
RT proteins, four tRNAs and L-rRNA.";
RL Nucleic Acids Res. 10:4783-4794(1982).
RN [2]
RP SEQUENCE REVISION TO 11; 19; 123 AND 249.
RA Lazarus C.M., Kuentzel H.;
RL Submitted (MAR-1984) to the PIR data bank.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
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 -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA99207.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA30031.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X06960; CAA30031.1; ALT_INIT; Genomic_DNA.
DR EMBL; J01390; AAA99207.1; ALT_INIT; Genomic_DNA.
DR PIR; B93436; OTAS3.
DR AlphaFoldDB; P00421; -.
DR SMR; P00421; -.
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 3: Inferred from homology;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183771"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 88
FT /note="N -> Y (in Ref. 3; AAA99207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 30360 MW; B68F4F79E8A690D2 CRC64;
MIYQSKRNFQ NHPFHLVSPS PWPLFTSISL FILTTATVLF MHGFEGFQYL VPVAVINVMY
VMGLWFRDVI SEGTYLGNHT NAVQKGLNLG VGLFIISEVF FFLAIFWAFF HSAISPSVEL
GAQWPPLGIQ GINPFELPLL NTIILLSSGV TITYAHHSLI QGNRKGALYG TVVTILLAIV
FTFFQGVEYT VSSFTISDSV YGSCFYFGTG FHGLHVIIGT AFLAVGLWRL AAYHLTDHHH
LGYESGILYW HFVDVVWLFL YISVYYWGY
