ID   COX8B_ONCMY             Reviewed;          20 AA.
AC   P80335;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   29-SEP-2021, entry version 66.
DE   RecName: Full=Cytochrome c oxidase subunit 8B, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide VIII-liver/heart;
DE   AltName: Full=Cytochrome c oxidase subunit 8H;
DE   Flags: Fragment;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Heart, and Liver;
RX   PubMed=8181469; DOI=10.1111/j.1432-1033.1994.tb18831.x;
RA   Freund R., Kadenbach B.;
RT   "Identification of tissue-specific isoforms for subunits Vb and VIIa of
RT   cytochrome c oxidase isolated from rainbow trout.";
RL   Eur. J. Biochem. 221:1111-1116(1994).
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:P10175}.
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:P10175}.
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:P10175}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P10175}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P10175}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase VIII family.
CC       {ECO:0000305}.
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DR   PIR; S43635; S43635.
DR   UniPathway; UPA00705; -.
DR   GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:InterPro.
DR   InterPro; IPR003205; Cyt_c_oxidase_su8.
DR   Pfam; PF02285; COX8; 1.
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 8B, mitochondrial"
FT                   /id="PRO_0000150125"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2050 MW;  4977B9DE80E62C58 CRC64;
     LSGKPAKXHL SVGEQAIAMT