COX3_BRAFL
ID COX3_BRAFL Reviewed; 262 AA.
AC P69216; C6L3C4; C6L3D7; C6L3L5; C6L3Q4; C6L3Z5; C6L408; O47425;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
GN Name=COIII;
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-6; ILE-52; VAL-160 AND
RP VAL-210.
RC STRAIN=Bf-H01, Bf-H02, Bf-H03, Bf-H04, Bf-H05, Bf-H06, Bf-H07, Bf-H08,
RC Bf-H09, Bf-H10, Bf-M01, Bf-M02, Bf-M03, Bf-M04, Bf-M05, Bf-M06, Bf-M07,
RC Bf-M08, Bf-M09, and Bf-M10;
RA Takada Y., Imai T.;
RT "Branchiostoma mitochondrial DNA, complete genome.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000312|Proteomes:UP000001554};
RX PubMed=10331267; DOI=10.1093/oxfordjournals.molbev.a026122;
RA Boore J.L., Daehler L.L., Brown W.M.;
RT "Complete sequence, gene arrangement, and genetic code of mitochondrial DNA
RT of the cephalochordate Branchiostoma floridae (Amphioxus).";
RL Mol. Biol. Evol. 16:410-418(1999).
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; AB478574; BAH86333.1; -; Genomic_DNA.
DR EMBL; AB478575; BAH86346.1; -; Genomic_DNA.
DR EMBL; AB478576; BAH86359.1; -; Genomic_DNA.
DR EMBL; AB478577; BAH86372.1; -; Genomic_DNA.
DR EMBL; AB478578; BAH86385.1; -; Genomic_DNA.
DR EMBL; AB478579; BAH86398.1; -; Genomic_DNA.
DR EMBL; AB478580; BAH86411.1; -; Genomic_DNA.
DR EMBL; AB478581; BAH86424.1; -; Genomic_DNA.
DR EMBL; AB478582; BAH86437.1; -; Genomic_DNA.
DR EMBL; AB478583; BAH86450.1; -; Genomic_DNA.
DR EMBL; AB478584; BAH86463.1; -; Genomic_DNA.
DR EMBL; AB478585; BAH86476.1; -; Genomic_DNA.
DR EMBL; AB478586; BAH86489.1; -; Genomic_DNA.
DR EMBL; AB478587; BAH86502.1; -; Genomic_DNA.
DR EMBL; AB478588; BAH86515.1; -; Genomic_DNA.
DR EMBL; AB478589; BAH86528.1; -; Genomic_DNA.
DR EMBL; AB478590; BAH86541.1; -; Genomic_DNA.
DR EMBL; AB478591; BAH86554.1; -; Genomic_DNA.
DR EMBL; AB478592; BAH86567.1; -; Genomic_DNA.
DR EMBL; AB478593; BAH86580.1; -; Genomic_DNA.
DR EMBL; AF098298; AAB87994.1; -; Genomic_DNA.
DR RefSeq; NP_007761.1; NC_000834.1.
DR AlphaFoldDB; P69216; -.
DR SMR; P69216; -.
DR GeneID; 808730; -.
DR KEGG; bfo:808730; -.
DR CTD; 4514; -.
DR InParanoid; P69216; -.
DR OMA; SIYWWGS; -.
DR Proteomes; UP000001554; Mitochondrion.
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:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
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; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..262
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000183747"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 6
FT /note="P -> S (in strain: Bf-H09)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 52
FT /note="V -> I (in strain: Bf-M01 and Bf-H10)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 160
FT /note="A -> V (in strain: Bf-H07)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 210
FT /note="I -> V (in strain: Bf-H03 and Bf-H04)"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 262 AA; 29711 MW; 6D93D8338AC870D8 CRC64;
MTGYQPHPWH LVEPSPWPLV GGSAAFTLTV GLVMWFHYNS ISLMILGLVM IVATMIQWWR
DVIREATFQG CHTSYVLSGL RRGMVLFIVS EVFFFLAFFW AFFHSSLAPT VELGVTWPPV
GVHPLNAFAV PLLNTAVLLS SGVTVTWAHH ALMEGKRTEA IQSLAITVML GLYFTGLQAW
EYYEAPFTIA DSVYGSTFFV ATGFHGLHVI IGSTFLMVCL GRQVFYHYTS SHHFGFEAAA
WYWHFVDVVW LFLYVCIYWW GS
