ID A0A6G9IHN6_HUMAN Unreviewed; 380 AA. AC A0A6G9IHN6; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 02-OCT-2024, entry version 15. DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117}; GN Name=CYTB {ECO:0000313|EMBL:QIQ23581.1}; OS Homo sapiens (Human). OG Mitochondrion {ECO:0000313|EMBL:QIQ23581.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:QIQ23581.1}; RN [1] {ECO:0000313|EMBL:QIQ23581.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood Serum {ECO:0000313|EMBL:QIQ23581.1}; RX PubMed=32150286; RA Li M., DeRosa K.L., Mann H., Spathis R., Roome A., Castellanos D., RA Gowen K., de Smet T.S., Echard J., Casey K., Shamoon-Pour M., Garruto R.M., RA Lum K.; RT "Recent kuru-induced female gene flow disrupted the coevolution of genes RT and languages in the Papua New Guinea highlands."; RL Am. J. Phys. Anthropol. 0:0-0(2020). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex CC (complex III or cytochrome b-c1 complex) that is part of the CC mitochondrial respiratory chain. The b-c1 complex mediates electron CC transfer from ubiquinol to cytochrome c. Contributes to the generation CC of a proton gradient across the mitochondrial membrane that is then CC used for ATP synthesis. {ECO:0000256|ARBA:ARBA00002566, CC ECO:0000256|RuleBase:RU362117}. CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|RuleBase:RU362117}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|RuleBase:RU362117}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR038885-2}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|PIRSR:PIRSR038885-2}; CC -!- SUBUNIT: The cytochrome bc1 complex contains 11 subunits: 3 respiratory CC subunits (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and CC UQCRC2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, CC UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of CC UQCRFS1). This cytochrome bc1 complex then forms a dimer. CC {ECO:0000256|ARBA:ARBA00011088}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004448}. CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000256|PROSITE- CC ProRule:PRU00967, ECO:0000256|RuleBase:RU362117}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MN398693; QIQ23568.1; -; Genomic_DNA. DR EMBL; MN398694; QIQ23581.1; -; Genomic_DNA. DR EMBL; MN398695; QIQ23594.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6G9IHN6; -. DR PeptideAtlas; A0A6G9IHN6; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR CDD; cd00290; cytochrome_b_C; 1. DR CDD; cd00284; Cytochrome_b_N; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR036150; Cyt_b/b6_C_sf. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like_sf. DR InterPro; IPR030689; Cytochrome_b. DR InterPro; IPR048260; Cytochrome_b_C_euk/bac. DR InterPro; IPR048259; Cytochrome_b_N_euk/bac. DR InterPro; IPR016174; Di-haem_cyt_TM. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF16; CYTOCHROME B; 1. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF038885; COB; 1. DR SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|PROSITE- KW ProRule:PRU00967}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038885-2}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038885-2}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE- KW ProRule:PRU00967}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR038885-2}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU362117}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU362117}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE- KW ProRule:PRU00967}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE- KW ProRule:PRU00967}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PROSITE- KW ProRule:PRU00967}; Ubiquinone {ECO:0000256|ARBA:ARBA00023075}. FT TRANSMEM 30..56 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 77..98 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 113..133 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 140..158 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 178..200 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 229..246 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 288..308 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 320..339 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 345..372 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT DOMAIN 1..209 FT /note="Cytochrome b/b6 N-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 210..380 FT /note="Cytochrome b/b6 C-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51003" FT BINDING 83 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b562" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 97 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b566" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 182 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b562" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 196 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b566" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-2" FT BINDING 201 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /evidence="ECO:0000256|PIRSR:PIRSR038885-1" SQ SEQUENCE 380 AA; 42700 MW; 9DCF0FAF875C1FC8 CRC64; MTPMRKINPL MKLINHSFID LPTPSNISAW WNFGSLLGAC LILQITTGLF LAMHYSPDAS TAFSSIAHIT RDVNYGWIIR YLHANGASMF FICLFLHIGR GLYYGSFLYS ETWNIGIILL LATMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VQWIWGGYSV DSPTLTRFFT FHFILPFIIT ALAALHLLFL HETGSNNPLG ITSHSDKITF HPYYTIKDAL GLLLFLLSLM TLALFSPDLL GDPDNYTLAN PLNTPPHIKP EWYFLFAYTI LRSVPNKLGG VLALLLSILI LAMIPILHMS KQQSMMFRPL SQSLYWLLAA DLLILTWIGG QPVSYPFTII GQVASVLYFT TILILMPTIS LIENKMLKWA //