COX5B_MOUSE
ID COX5B_MOUSE Reviewed; 128 AA.
AC P19536;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cytochrome c oxidase subunit 5B, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide Vb;
DE Flags: Precursor;
GN Name=Cox5b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow tumor;
RX PubMed=2169317; DOI=10.1016/0167-4781(90)90128-o;
RA Basu A., Avadhani N.G.;
RT "Nucleotide sequence of cDNA for nuclear encoded subunit Vb of mouse
RT cytochrome-c oxidase.";
RL Biochim. Biophys. Acta 1087:98-100(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1651332; DOI=10.1016/s0021-9258(18)98637-0;
RA Basu A., Avadhani N.G.;
RT "Structural organization of nuclear gene for subunit Vb of mouse
RT mitochondrial cytochrome c oxidase.";
RL J. Biol. Chem. 266:15450-15456(1991).
RN [3]
RP PROTEIN SEQUENCE OF 57-67 AND 74-85, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67; LYS-85 AND LYS-120, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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 EMBL; X53157; CAA37313.1; -; mRNA.
DR EMBL; M77040; AAA37515.1; -; Genomic_DNA.
DR PIR; A39425; A39425.
DR PDB; 7O37; EM; 3.20 A; f=30-128.
DR PDB; 7O3C; EM; 3.30 A; f=30-128.
DR PDB; 7O3E; EM; 3.60 A; f=30-128.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR AlphaFoldDB; P19536; -.
DR SMR; P19536; -.
DR CORUM; P19536; -.
DR IntAct; P19536; 2.
DR STRING; 10090.ENSMUSP00000038961; -.
DR iPTMnet; P19536; -.
DR PhosphoSitePlus; P19536; -.
DR SwissPalm; P19536; -.
DR SWISS-2DPAGE; P19536; -.
DR UCD-2DPAGE; P19536; -.
DR EPD; P19536; -.
DR jPOST; P19536; -.
DR MaxQB; P19536; -.
DR PaxDb; P19536; -.
DR PeptideAtlas; P19536; -.
DR PRIDE; P19536; -.
DR MGI; MGI:88475; Cox5b.
DR eggNOG; KOG3352; Eukaryota.
DR InParanoid; P19536; -.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR UniPathway; UPA00705; -.
DR ChiTaRS; Cox5b; mouse.
DR PRO; PR:P19536; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P19536; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR CDD; cd00924; Cyt_c_Oxidase_Vb; 1.
DR Gene3D; 2.60.11.10; -; 1.
DR InterPro; IPR002124; Cyt_c_oxidase_su5b.
DR InterPro; IPR036972; Cyt_c_oxidase_su5b_sf.
DR PANTHER; PTHR10122; PTHR10122; 1.
DR Pfam; PF01215; COX5B; 1.
DR PROSITE; PS00848; COX5B_1; 1.
DR PROSITE; PS51359; COX5B_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00428"
FT CHAIN 31..128
FT /note="Cytochrome c oxidase subunit 5B, mitochondrial"
FT /id="PRO_0000006110"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT MOD_RES 67
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 120
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:7O37"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7O37"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:7O37"
SQ SEQUENCE 128 AA; 13813 MW; 84AA890F1A074383 CRC64;
MASRLLRGVG ALAAQALRRT ARGAAVTRSM ASGGGVPTDE EQATGLEREI MIAAQKGLDP
YNMLPPKAAS GTKEDPNLVP SISNKRIVGC ICEEDNCTVI WFWLHKGESQ RCPNCGTHYK
LVPHQMAH
