COX3_AEDAE
ID COX3_AEDAE Reviewed; 262 AA.
AC B0FWD1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
GN Name=mt:CoIII {ECO:0000250|UniProtKB:P00417};
GN Synonyms=COX3 {ECO:0000312|EMBL:ABY51628.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OG Mitochondrion {ECO:0000312|EMBL:ABY51628.1}.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000312|EMBL:ABY51628.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12 {ECO:0000312|EMBL:ABY51628.1};
RA Lobo N.F., Lovin D., DeBruyn B., Puiu D., Shumway M., Haas B., Nene V.,
RA Severson D.W.;
RT "The mitochondrial genome of the Yellow fever mosquito - Aedes aegypti.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255}.
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DR EMBL; EU352212; ABY51628.1; -; Genomic_DNA.
DR RefSeq; YP_001649167.1; NC_010241.1.
DR AlphaFoldDB; B0FWD1; -.
DR SMR; B0FWD1; -.
DR STRING; 7159.AAEL018669-PA; -.
DR VEuPathDB; VectorBase:AAEL018669; -.
DR eggNOG; KOG4664; Eukaryota.
DR HOGENOM; CLU_044071_0_0_1; -.
DR InParanoid; B0FWD1; -.
DR OrthoDB; 1304563at2759; -.
DR Proteomes; UP000008820; Unplaced.
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; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..262
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000372685"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
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"
SQ SEQUENCE 262 AA; 30294 MW; C5F0BD10437C8101 CRC64;
MSTHANHPFH LVDYSPWPLT GAIGAMTTVT GLVQWFHQYD NTLFLLGNII TMLTMYQWWR
DISREGTFQG LHTIPVTLGL RWGMILFIIS EVFFFISFFW AFFHSSLSPT IELGMVWPPI
GIEPFNPFQI PLLNTAILLA SGVTVTWAHH SLMENNHTQT IQSLFFTVLL GIYFSILQAY
EYIEAPFTIA DNVYGSTFFV ATGFHGLHVL IGTSFLLICL FRHMNCHFSS SHHFGFEAAA
WYWHFVDVVW LFLYISIYWW GN
