ID   COX3_ANOQU              Reviewed;         262 AA.
AC   P33508;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   22-FEB-2023, entry version 103.
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   Anopheles quadrimaculatus (Common malaria mosquito).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Orlando;
RX   PubMed=2134168; DOI=10.1002/arch.940140104;
RA   Cockburn A.F., Mitchell S.E., Seawright J.A.;
RT   "Cloning of the mitochondrial genome of Anopheles quadrimaculatus.";
RL   Arch. Insect Biochem. Physiol. 14:31-36(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   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC       {ECO:0000305}.
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DR   EMBL; L04272; AAA93545.2; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; P33508; -.
DR   SMR; P33508; -.
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; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.120.80; Cytochrome c oxidase, subunit III, four-helix bundle; 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:SF7; CYTOCHROME C OXIDASE SUBUNIT 3; 1.
DR   PANTHER; PTHR11403; CYTOCHROME C OXIDASE SUBUNIT III; 1.
DR   Pfam; PF00510; COX3; 1.
DR   SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 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..262
FT                   /note="Cytochrome c oxidase subunit 3"
FT                   /id="PRO_0000183733"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   262 AA;  30172 MW;  EAE85C6059567823 CRC64;
     MSAHANHPFH LVDYSPWPLT GAIGAMTTVS GLVQWFHQYT MTLFILGNII TILTMYQWWR
     DISREGTFQG LHTFPVTIGL RWGMILFIVS EIFFFISFFW AFFHSSLSPT IELGMTWPPV
     GIIAFNPFQI PLLNTAILLA SGVTVTWAHH ALMESNHSQA TQGLFFTIVL GIYFSILQAY
     EYIEAPFTIA DAVYGSTFYM ATGFHGLHVL IGTTFLLICF LRHINFHFSK NHHFGFEAAA
     WYWHFVDVVW LFLYISIYWW GS
//