ID   A0A7T5BXY7_ANTFL        Unreviewed;       261 AA.
AC   A0A7T5BXY7;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   29-MAY-2024, entry version 9.
DE   RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|ARBA:ARBA00015944, ECO:0000256|RuleBase:RU003375};
GN   Name=COX3 {ECO:0000313|EMBL:QQD89998.1};
OS   Antechinus flavipes (Yellow-footed marsupial mouse) (Phascogale flavipes).
OG   Mitochondrion {ECO:0000313|EMBL:QQD89998.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Antechinus.
OX   NCBI_TaxID=38775 {ECO:0000313|EMBL:QQD89998.1};
RN   [1] {ECO:0000313|EMBL:QQD89998.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Adam Ant {ECO:0000313|EMBL:QQD89998.1};
RA   Seim I.;
RT   "The mitochondrial genome of the yellow-footed dusky antechinus, Antechinus
RT   flavipes.";
RL   Submitted (SEP-2019) 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:0000256|RuleBase:RU003375}.
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:0000256|ARBA:ARBA00029331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC         Evidence={ECO:0000256|ARBA:ARBA00029331};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC       {ECO:0000256|ARBA:ARBA00010581, ECO:0000256|RuleBase:RU003375}.
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DR   EMBL; MN447797; QQD89998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7T5BXY7; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:TreeGrafter.
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 {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003375, ECO:0000313|EMBL:QQD89998.1};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003375};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        16..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        41..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        191..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..261
FT                   /note="Heme-copper oxidase subunit III family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50253"
SQ   SEQUENCE   261 AA;  29848 MW;  587B9B7AD3F2873B CRC64;
     MTHQTHAYHM VNPSPWPLTG ALSAFLLTSG MIMWFHFHST LLLFMGVTSI LLTMFQWWRD
     VVREGTYQGH HTPVVQKGLR YGMVLFIMSE VFFFVGFFWA FYHSSLSPAL ELGGCWPPVG
     INPLNPLEVP LLNTAILLAS GVSITWAHHS LMEGNRNQMI QALATTIGLG LYFTILQAME
     YYEAPFTISD GIYGSTFFVA TGFHGLHVII GSLFLIVCLL RQLFYHFTST HHFGFEAAAW
     YWHFVDVVWL FLYVSIYWWG S
//