ID A0A0A0QK12_9SAUR Unreviewed; 232 AA. AC A0A0A0QK12; DT 04-FEB-2015, integrated into UniProtKB/TrEMBL. DT 04-FEB-2015, sequence version 1. DT 12-AUG-2020, entry version 13. DE RecName: Full=Complex III subunit 3 {ECO:0000256|ARBA:ARBA00015233}; DE AltName: Full=Complex III subunit III {ECO:0000256|ARBA:ARBA00016192}; DE AltName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531}; DE AltName: Full=Cytochrome b-c1 complex subunit 3 {ECO:0000256|ARBA:ARBA00016333}; DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit {ECO:0000256|ARBA:ARBA00015182}; DE Flags: Fragment; GN Name=cytb {ECO:0000313|EMBL:AIL53579.1}; OS Thermophis baileyi. OG Mitochondrion {ECO:0000313|EMBL:AIL53579.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Dipsadidae; Thermophis. OX NCBI_TaxID=527827 {ECO:0000313|EMBL:AIL53579.1}; RN [1] {ECO:0000313|EMBL:AIL53579.1} RP NUCLEOTIDE SEQUENCE. RA Hofmann S., Kraus S., Dorge T., Nothnagel M., Fritzsche P., Miehe G.; RT "Effects of Pleistocene climatic fluctuations on the phylogeography, RT demography and population structure of a high-elevation snake species, RT Thermophis baileyi, on the Tibetan Plateau."; RL J. Biogeogr. 41:2162-2172(2014). 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 -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- SUBUNIT: The cytochrome bc1 complex contains 3 respiratory subunits CC (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and CC probably 6 low-molecular weight proteins. CC {ECO:0000256|ARBA:ARBA00011660}. 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 --------------------------------------------------------------------------- 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; KF595099; AIL53563.1; -; Genomic_DNA. DR EMBL; KF595105; AIL53569.1; -; Genomic_DNA. DR EMBL; KF595106; AIL53570.1; -; Genomic_DNA. DR EMBL; KF595107; AIL53571.1; -; Genomic_DNA. DR EMBL; KF595108; AIL53572.1; -; Genomic_DNA. DR EMBL; KF595109; AIL53573.1; -; Genomic_DNA. DR EMBL; KF595115; AIL53579.1; -; Genomic_DNA. DR EMBL; KF595119; AIL53583.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro. DR CDD; cd00284; Cytochrome_b_N; 1. DR Gene3D; 1.20.810.10; -; 1. DR InterPro; IPR005798; Cyt_b/b6_C. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like_sf. DR InterPro; IPR016174; Di-haem_cyt_TM. DR Pfam; PF00033; Cytochrome_B; 1. DR SUPFAM; SSF81342; SSF81342; 1. DR PROSITE; PS51003; CYTB_CTER; 1. DR PROSITE; PS51002; CYTB_NTER; 1. PE 4: Predicted; KW Electron transport {ECO:0000256|ARBA:ARBA00022982}; KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000313|EMBL:AIL53579.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}; KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075}. FT TRANSMEM 16..41 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 68..86 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 98..118 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 124..143 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 164..185 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 215..231 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..195 FT /note="CYTB_NTER" FT /evidence="ECO:0000259|PROSITE:PS51002" FT DOMAIN 196..232 FT /note="CYTB_CTER" FT /evidence="ECO:0000259|PROSITE:PS51003" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AIL53579.1" FT NON_TER 232 FT /evidence="ECO:0000313|EMBL:AIL53579.1" SQ SEQUENCE 232 AA; 26198 MW; 7E9E135D569CA174 CRC64; LLLFNLLPVG SNISTWWCFG SMLLTCSMLQ IMTGFFLAIH YTANIDLAFS SIVHITRDVP YGWTMQNLHA IGASMFFICI YTHTARGLYY GSYLNKEVWM TGTALLITLM ATAFFGYVLP WGQMSFWAAT VITNLLTAVP YLGHTLTTWL WGGFSINDPT LTRFFALHFI LPFAIISLAS IHIMFLHNEG SSNPLGTNSD IDKIPFHPYH SHKDILMLTT MITLLFITLT FT //