ID G3JYV8_TAMPA Unreviewed; 372 AA. AC G3JYV8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 03-JUL-2019, entry version 34. DE RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU362117}; DE Flags: Fragment; GN Name=cytb {ECO:0000313|EMBL:AEO79517.1}; OS Tamias panamintinus (Panamint chipmunk) (Neotamias panamintinus). OG Mitochondrion {ECO:0000313|EMBL:AEO79517.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; OC Sciuridae; Xerinae; Marmotini; Tamias. OX NCBI_TaxID=123790 {ECO:0000313|EMBL:AEO79517.1}; RN [1] {ECO:0000313|EMBL:AEO79517.1} RP NUCLEOTIDE SEQUENCE. RA Reid N.M., Demboski J.R., Sullivan J.; RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEO79517.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21878471; DOI=10.1093/sysbio/syr094; RA Reid N., Demboski J.R., Sullivan J.; RT "Phylogeny estimation of the radiation of western North American RT chipmunks (Tamias) in the face of introgression using reproductive RT protein genes."; RL Syst. Biol. 61:44-62(2012). CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase CC complex (complex III or cytochrome b-c1 complex) that is part of CC the mitochondrial respiratory chain. The b-c1 complex mediates CC electron transfer from ubiquinol to cytochrome c. Contributes to CC the generation of a proton gradient across the mitochondrial CC membrane that is then used for ATP synthesis. CC {ECO:0000256|RuleBase:RU362117}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|PIRSR:PIRSR038885-2, CC ECO:0000256|RuleBase:RU362117}; CC Note=Binds 2 heme groups non-covalently. CC {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU362117}. 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; JN042472; AEO79517.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro. DR CDD; cd00290; cytochrome_b_C; 1. DR CDD; cd00284; Cytochrome_b_N; 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; IPR030689; Cytochrome_b. DR InterPro; IPR016174; Di-haem_cyt_TM. DR Pfam; PF00032; Cytochrom_B_C; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR PIRSF; PIRSF038885; COB; 1. DR SUPFAM; SSF81342; SSF81342; 1. DR SUPFAM; SSF81648; SSF81648; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|RuleBase:RU362117}; KW Heme {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117}; KW Iron {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117}; KW Membrane {ECO:0000256|RuleBase:RU362117}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR038885-2, KW ECO:0000256|RuleBase:RU362117}; KW Mitochondrion {ECO:0000256|RuleBase:RU362117, KW ECO:0000313|EMBL:AEO79517.1}; KW Respiratory chain {ECO:0000256|RuleBase:RU362117}; KW Transmembrane {ECO:0000256|RuleBase:RU362117}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362117}; KW Transport {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 23 45 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 80 100 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 106 126 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 138 159 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 171 193 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 222 239 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 281 300 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 312 332 Helical. {ECO:0000256|RuleBase:RU362117}. FT TRANSMEM 338 365 Helical. {ECO:0000256|RuleBase:RU362117}. FT DOMAIN 1 202 CYTB_NTER. {ECO:0000259|PROSITE:PS51002}. FT DOMAIN 203 372 CYTB_CTER. {ECO:0000259|PROSITE:PS51003}. FT METAL 76 76 Iron 1 (heme b562 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT METAL 90 90 Iron 2 (heme b566 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT METAL 175 175 Iron 1 (heme b562 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT METAL 189 189 Iron 2 (heme b566 axial ligand). FT {ECO:0000256|PIRSR:PIRSR038885-2}. FT BINDING 194 194 Ubiquinone. {ECO:0000256|PIRSR: FT PIRSR038885-1}. FT NON_TER 1 1 {ECO:0000313|EMBL:AEO79517.1}. FT NON_TER 372 372 {ECO:0000313|EMBL:AEO79517.1}. SQ SEQUENCE 372 AA; 42237 MW; E5E876F524D7901D CRC64; HPLIKIINHS FIDLPAPSNI SAWWNFGSLL GICLIIQILT GLFLAMHYTS DTMTAFSSVT HICRDVNYGW LIRYMHANGA SMFFICLFLH VGRGLYYGSY TYFETWNIGV ILLFAVMATA FMGYVLPWGQ MSFWGATVIT NLLSAIPYIG TTLVEWIWGG FSVDKATLTR FFAFHFILPF IITALVMVHL LFLHETGSNN PSGLISDSDK IPFHPYYTIK DILGILLLIL ILMILVLFSP DLLGDPDNYT PANPLSTPPH IKPEWYFLFA YAILRSIPNK LGGVLALVLS ILILMLFPIL HMSKQRSMMF RPLSQCMFWI LVADLFTLTW IGGQPVEYPF IIIGQLASIL YFMIILLILP AISLFENKLL KW //