COX5B_RAT
ID COX5B_RAT Reviewed; 129 AA.
AC P12075;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cytochrome c oxidase subunit 5B, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide Vb;
DE AltName: Full=Cytochrome c oxidase subunit VIA*;
DE Flags: Precursor;
GN Name=Cox5b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8206867; DOI=10.1093/oxfordjournals.jbchem.a124317;
RA Hoshinaga H., Amuro N., Goto Y., Okazaki T.;
RT "Molecular cloning and characterization of the rat cytochrome c oxidase
RT subunit Vb gene.";
RL J. Biochem. 115:194-201(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-129.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=2549512; DOI=10.1093/nar/17.15.6388;
RA Goto Y., Amuro N., Okazaki T.;
RT "Nucleotide sequence of cDNA for rat liver and brain cytochrome c oxidase
RT subunit VIa (Vb).";
RL Nucleic Acids Res. 17:6388-6388(1989).
RN [4]
RP PROTEIN SEQUENCE OF 32-41.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7601105; DOI=10.1111/j.1432-1033.1995.tb20556.x;
RA Schaegger H., Noack H., Halangk W., Brandt U., von Jagow G.;
RT "Cytochrome-c oxidase in developing rat heart. Enzymic properties and
RT amino-terminal sequences suggest identity of the fetal heart and the adult
RT liver isoform.";
RL Eur. J. Biochem. 230:235-241(1995).
RN [5]
RP PROTEIN SEQUENCE OF 50-57; 69-87 AND 113-121, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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; D10952; BAA01744.1; -; mRNA.
DR EMBL; D10951; BAA01743.1; -; Genomic_DNA.
DR EMBL; BC083179; AAH83179.1; -; mRNA.
DR EMBL; X14208; CAA32425.1; -; mRNA.
DR PIR; JC2254; JC2254.
DR RefSeq; NP_446038.1; NM_053586.1.
DR AlphaFoldDB; P12075; -.
DR SMR; P12075; -.
DR BioGRID; 250174; 4.
DR CORUM; P12075; -.
DR IntAct; P12075; 1.
DR MINT; P12075; -.
DR STRING; 10116.ENSRNOP00000022487; -.
DR CarbonylDB; P12075; -.
DR iPTMnet; P12075; -.
DR PhosphoSitePlus; P12075; -.
DR SwissPalm; P12075; -.
DR UCD-2DPAGE; P12075; -.
DR jPOST; P12075; -.
DR PaxDb; P12075; -.
DR PRIDE; P12075; -.
DR GeneID; 94194; -.
DR KEGG; rno:94194; -.
DR UCSC; RGD:620608; rat.
DR CTD; 1329; -.
DR RGD; 620608; Cox5b.
DR VEuPathDB; HostDB:ENSRNOG00000016660; -.
DR eggNOG; KOG3352; Eukaryota.
DR HOGENOM; CLU_127178_0_0_1; -.
DR InParanoid; P12075; -.
DR OMA; DSHDTIY; -.
DR OrthoDB; 1528134at2759; -.
DR PhylomeDB; P12075; -.
DR TreeFam; TF105063; -.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR UniPathway; UPA00705; -.
DR PRO; PR:P12075; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000016660; Expressed in heart and 20 other tissues.
DR Genevisible; P12075; RN.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; TAS:RGD.
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 GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
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 Acetylation; Direct protein sequencing; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Zinc.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7601105"
FT CHAIN 32..129
FT /note="Cytochrome c oxidase subunit 5B, mitochondrial"
FT /id="PRO_0000006111"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00692"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19536"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19536"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P19536"
FT VARIANT 109
FT /note="E -> Q"
SQ SEQUENCE 129 AA; 13915 MW; 5C5DD1F9C20D59A5 CRC64;
MASRLLRGVG ALAAQALRAH GPRGVAATRS MASGGGVPTD EEQATGLERE IMIAAQRGLD
PYNMLPPKAA SGTKEDPNLV PSVSNKRIVG CICEEDNCTV IWFWLHQGES QRCPNCGTHY
KLVPYQMVH
