COX3_CHOCR
ID COX3_CHOCR Reviewed; 272 AA.
AC P48872;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 94.
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 Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OG Mitochondrion.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Apices;
RX PubMed=7616569; DOI=10.1006/jmbi.1995.0392;
RA Leblanc C., Boyen C., Richard O., Bonnard G., Grienenberger J.-M.,
RA Kloareg B.;
RT "Complete sequence of the mitochondrial DNA of the rhodophyte Chondrus
RT crispus (Gigartinales). Gene content and genome organization.";
RL J. Mol. Biol. 250:484-495(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Apices;
RX PubMed=8190631; DOI=10.1093/nar/22.8.1400;
RA Boyen C., Leblanc C., Bonnard G., Grienenberger J.M., Kloareg B.;
RT "Nucleotide sequence of the cox3 gene from Chondrus crispus: evidence that
RT UGA encodes tryptophan and evolutionary implications.";
RL Nucleic Acids Res. 22:1400-1403(1994).
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}.
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DR EMBL; Z47547; CAA87605.1; -; Genomic_DNA.
DR PIR; S43951; S43951.
DR RefSeq; NP_062484.1; NC_001677.2.
DR AlphaFoldDB; P48872; -.
DR SMR; P48872; -.
DR GeneID; 809356; -.
DR KEGG; ccp:ChcroMp05; -.
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..272
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183758"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 272 AA; 31189 MW; DC408B19950F4021 CRC64;
MTTLSQISKS VQRHPFHLVD PSPWPFVASL CAFSCAIGGV MYMHAYVNGS FILSISFFCL
LLVMFTWWRD VIRESTFEGH HTGIVQQGLR FGVILFIISE ILFFFAFFWA FFHSSLAPTI
EIGSIWPPKG INVLNPWEIP FLNTLILLLS GCTVTWCHHS LVSNLRNQSV LSLFLTIVLA
IVFTTFQAYE YSMADFRLSD GIYGSTFYMA TGFHGFHVLV GTISLAVCLI RLLQYQLTQQ
HHFGFESAAW YWHFVDVVWL FLFVSIYWWG GS
