ID C3TVH1_CAPIB Unreviewed; 261 AA.
AC C3TVH1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Cytochrome c oxidase subunit 3 {ECO:0000256|ARBA:ARBA00015944, ECO:0000256|RuleBase:RU003375};
GN Name=COXIII {ECO:0000313|EMBL:ACI24451.1};
OS Capra ibex (Ibex).
OG Mitochondrion {ECO:0000313|EMBL:ACI24451.1}.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=72542 {ECO:0000313|EMBL:ACI24451.1};
RN [1] {ECO:0000313|EMBL:ACI24451.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19294454; DOI=10.1007/s00239-009-9208-7;
RA Hassanin A., Ropiquet A., Couloux A., Cruaud C.;
RT "Evolution of the mitochondrial genome in mammals living at high altitude:
RT new insights from a study of the tribe Caprini (Bovidae, Antilopinae).";
RL J. Mol. Evol. 68:293-310(2009).
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; FJ207526; ACI24451.1; -; Genomic_DNA.
DR RefSeq; YP_007625061.1; NC_020623.1.
DR AlphaFoldDB; C3TVH1; -.
DR GeneID; 14841607; -.
DR CTD; 4514; -.
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 {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|RuleBase:RU003375, ECO:0000313|EMBL:ACI24451.1};
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 79..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..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; 29836 MW; C48E789F0FB1C00B CRC64;
MTHQTHAYHM VNPSPWPLTG ALSALLLTSG LIMWFHFNST ALLTLGLTTN MLTMYQWWRD
VIRESTFQGH HTPPVQKGLR YGMILFIISE VLFFTGFFWA FYHSSLAPTP ELGGCWPPTG
IHPLNPLEVP LLNTSVLLAS GVSITWAHHS LMEGDRSHML QALFITITLG LYFTLLQASE
YYEAPFTISD GVYGSTFFVA TGFHGLHVII GSTFLIVCFF RQLKFHFTSN HHFGFEAAAW
YWHFVDVVWL FLYVSIYWWG S
//