ID   COX3_SPOFR              Reviewed;         147 AA.
AC   Q35826;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Cytochrome c oxidase subunit 3;
DE            EC=7.1.1.9;
DE   AltName: Full=Cytochrome c oxidase polypeptide III;
DE   Flags: Fragment;
GN   Name=COIII;
OS   Spodoptera frugiperda (Fall armyworm).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Amphipyrinae; Spodoptera.
OX   NCBI_TaxID=7108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2459844; DOI=10.1016/0042-6822(88)90522-3;
RA   Ooi B.G., Miller L.K.;
RT   "Regulation of host RNA levels during baculovirus infection.";
RL   Virology 166:515-523(1988).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M22051; AAA68818.1; -; mRNA.
DR   AlphaFoldDB; Q35826; -.
DR   SMR; Q35826; -.
DR   Proteomes; UP000829999; Mitochondrion MT.
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; 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   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           <1..147
FT                   /note="Cytochrome c oxidase subunit 3"
FT                   /id="PRO_0000183855"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   147 AA;  17024 MW;  4AF1AFF80103769E CRC64;
     MWPPTSITPF NPFQIPLLNT IILISSGVSV TWAHHAIMEN NNSQMTQGLF ITIILGIYFT
     ILQAYEYFEA PFTIADSIYG STFFMATGFH GLHVIIGTLF LLICLIRHLN NHFSSNHHFG
     FEAAAWYWHF VDVVWLFLYI SIYWWGN
//