COX5B_PIG
ID COX5B_PIG Reviewed; 129 AA.
AC Q5S3G4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cytochrome c oxidase subunit 5B, mitochondrial;
DE AltName: Full=Cytochrome c oxidase polypeptide Vb;
DE Flags: Precursor;
GN Name=COX5B;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cui X.S., Hwang K.C., Kim N.H.;
RT "Identification of pig Cox5b.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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; AY786556; AAV53387.1; -; mRNA.
DR RefSeq; NP_001007518.1; NM_001007517.1.
DR AlphaFoldDB; Q5S3G4; -.
DR SMR; Q5S3G4; -.
DR STRING; 9823.ENSSSCP00000008748; -.
DR iPTMnet; Q5S3G4; -.
DR PaxDb; Q5S3G4; -.
DR PeptideAtlas; Q5S3G4; -.
DR PRIDE; Q5S3G4; -.
DR Ensembl; ENSSSCT00000008974; ENSSSCP00000008748; ENSSSCG00000008195.
DR Ensembl; ENSSSCT00005029569; ENSSSCP00005018005; ENSSSCG00005018745.
DR Ensembl; ENSSSCT00015102934; ENSSSCP00015042820; ENSSSCG00015076314.
DR Ensembl; ENSSSCT00025034868; ENSSSCP00025014524; ENSSSCG00025025808.
DR Ensembl; ENSSSCT00030082884; ENSSSCP00030038071; ENSSSCG00030059360.
DR Ensembl; ENSSSCT00035074454; ENSSSCP00035030218; ENSSSCG00035055797.
DR Ensembl; ENSSSCT00040103184; ENSSSCP00040046704; ENSSSCG00040074620.
DR Ensembl; ENSSSCT00045050672; ENSSSCP00045035278; ENSSSCG00045029700.
DR Ensembl; ENSSSCT00050100657; ENSSSCP00050043709; ENSSSCG00050073602.
DR Ensembl; ENSSSCT00055030709; ENSSSCP00055024447; ENSSSCG00055015594.
DR Ensembl; ENSSSCT00060059096; ENSSSCP00060025318; ENSSSCG00060043563.
DR Ensembl; ENSSSCT00065054361; ENSSSCP00065023624; ENSSSCG00065039777.
DR Ensembl; ENSSSCT00070057450; ENSSSCP00070048841; ENSSSCG00070028627.
DR GeneID; 492822; -.
DR KEGG; ssc:492822; -.
DR CTD; 1329; -.
DR eggNOG; KOG3352; Eukaryota.
DR GeneTree; ENSGT00390000011010; -.
DR HOGENOM; CLU_127178_0_0_1; -.
DR InParanoid; Q5S3G4; -.
DR OMA; DSHDTIY; -.
DR OrthoDB; 1528134at2759; -.
DR TreeFam; TF105063; -.
DR Reactome; R-SSC-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-SSC-611105; Respiratory electron transport.
DR Reactome; R-SSC-9707564; Cytoprotection by HMOX1.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000008227; Chromosome 3.
DR Proteomes; UP000314985; Chromosome 3.
DR Bgee; ENSSSCG00000008195; Expressed in semimembranosus muscle and 44 other tissues.
DR Genevisible; Q5S3G4; SS.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00428"
FT CHAIN 32..129
FT /note="Cytochrome c oxidase subunit 5B, mitochondrial"
FT /id="PRO_0000253610"
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"
SQ SEQUENCE 129 AA; 13783 MW; 56FC1514AB513FE5 CRC64;
MASRLLRGAG ALAAQTLRAR GPNGVAVVRS MASGGGVPTD EEQATGLERE VMMAARKGLD
PYNILAPKAA SGTKEDPNLV PSITNKRIVG CICEEDNSTV IWFWVHKGET QRCPSCGTHY
KLVSHQLAH
