ID   COX5B_THUOB             Reviewed;          20 AA.
AC   P80974;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Cytochrome c oxidase subunit 5B, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide Vb;
DE   Flags: Fragment;
OS   Thunnus obesus (Bigeye tuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX   NCBI_TaxID=8241;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Heart, and Liver;
RX   PubMed=9310366; DOI=10.1111/j.1432-1033.1997.t01-1-00099.x;
RA   Arnold S., Lee I., Kim M., Song E., Linder D., Lottspeich F., Kadenbach B.;
RT   "The subunit structure of cytochrome-c oxidase from tuna heart and liver.";
RL   Eur. J. Biochem. 248:99-103(1997).
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:P04037}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P04037}.
CC   -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC       multisubunit enzyme composed of 14 subunits. The complex is composed of
CC       a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC       the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A,
CC       COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC       are encoded in the nuclear genome. The complex exists as a monomer or a
CC       dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC       membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC       ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC       III, CIII), resulting in different assemblies (supercomplex
CC       SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)).
CC       {ECO:0000250|UniProtKB:P00428}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00428}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00428}; Matrix side
CC       {ECO:0000250|UniProtKB:P00428}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 5B family.
CC       {ECO:0000305}.
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DR   PIR; S77983; S77983.
DR   AlphaFoldDB; P80974; -.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane.
FT   CHAIN           1..>20
FT                   /note="Cytochrome c oxidase subunit 5B, mitochondrial"
FT                   /id="PRO_0000197032"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2158 MW;  76F1473E1F392BD7 CRC64;
     GTLKGIPTDD EQATGLERRT