ID A0A3G2LCP0_9RODE Unreviewed; 178 AA. AC A0A3G2LCP0; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 14-DEC-2022, entry version 12. DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117}; DE Flags: Fragment; GN Name=cytb {ECO:0000313|EMBL:AYN70015.1}; OS Meriones tristrami (Tristram's jird). OG Mitochondrion {ECO:0000313|EMBL:AYN70015.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Gerbillinae; Meriones. OX NCBI_TaxID=723805 {ECO:0000313|EMBL:AYN70015.1}; RN [1] {ECO:0000313|EMBL:AYN70015.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Gezar Darreh22 {ECO:0000313|EMBL:AYN70013.1}, Gezar Darreh26 RC {ECO:0000313|EMBL:AYN70014.1}, Khroseh13 RC {ECO:0000313|EMBL:AYN70016.1}, and Khroseh17 RC {ECO:0000313|EMBL:AYN70015.1}; RC TISSUE=Blood {ECO:0000313|EMBL:AYN70015.1}; RA Hosseini M., Oshaghi M.A., Sedaghat M.M., Mostafavi E., Mohammadi A., RA Vatandoost H., Hashemi-Aghdam S.S.; RT "Genetic Structure of Meriones Persicus Populations from West and North RT Iran."; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. 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 -!- 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. CC {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; MH384466; AYN70013.1; -; Genomic_DNA. DR EMBL; MH384467; AYN70014.1; -; Genomic_DNA. DR EMBL; MH384468; AYN70015.1; -; Genomic_DNA. DR EMBL; MH384469; AYN70016.1; -; Genomic_DNA. DR AlphaFoldDB; A0A3G2LCP0; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR CDD; cd00290; cytochrome_b_C; 1. DR Gene3D; 1.20.810.10; -; 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; IPR016174; Di-haem_cyt_TM. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF13631; Cytochrom_B_N_2; 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, KW ECO:0000256|RuleBase:RU362117}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362117}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362117}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362117}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU362117}; 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, KW ECO:0000256|RuleBase:RU362117}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU362117}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362117}; KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}. FT TRANSMEM 17..39 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 68..85 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 127..146 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT TRANSMEM 158..177 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362117" FT DOMAIN 1..48 FT /note="CYTB_NTER" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 49..178 FT /note="CYTB_CTER" FT /evidence="ECO:0000259|PROSITE:PS51003" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AYN70015.1" FT NON_TER 178 FT /evidence="ECO:0000313|EMBL:AYN70015.1" SQ SEQUENCE 178 AA; 20325 MW; 66E914499E8B6E89 CRC64; EWIWGGFSVD KATLTRFFAF HFILPFIIAA LVLVHLLFLH ETGSNNPLGL DSNADKIPFH PYYTVKDFLG VVLLILFFML LVLFFPDMLG DPDNYTPANP LNTPPHIKPE WYFLFAYAIL RSIPNKLGGV LALILSILIL ILLPLTHTSK QRSLMFRPIS QMLYWALIAN LLILTWIG //