ID A0A0Y0QKD5_ARCFO Unreviewed; 200 AA. AC A0A0Y0QKD5; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 24-JAN-2024, entry version 15. DE RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531}; DE AltName: Full=Complex III subunit 3 {ECO:0000256|ARBA:ARBA00031681}; DE AltName: Full=Complex III subunit III {ECO:0000256|ARBA:ARBA00032600}; DE AltName: Full=Cytochrome b-c1 complex subunit 3 {ECO:0000256|ARBA:ARBA00029812}; DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit {ECO:0000256|ARBA:ARBA00032818}; DE Flags: Fragment; GN Name=cytb {ECO:0000313|EMBL:AMB62298.1}; OS Arctocephalus forsteri (New Zealand fur seal) (Arctocephalus australis OS forsteri). OG Mitochondrion {ECO:0000313|EMBL:AMB62298.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Otariidae; OC Arctocephalus. OX NCBI_TaxID=29084 {ECO:0000313|EMBL:AMB62298.1}; RN [1] {ECO:0000313|EMBL:AMB62298.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26768113; DOI=10.1016/j.ympev.2015.12.012; RA Salis A.T., Easton L.J., Robertson B.C., Gemmell N., Smith I.W., RA Weisler M.I., Waters J.M., Rawlence N.J.; RT "Myth or relict: Does ancient DNA detect the enigmatic Upland seal?"; RL Mol. Phylogenet. Evol. 97:101-106(2016). 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 b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|ARBA:ARBA00001970}; 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 --------------------------------------------------------------------------- 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; KU510840; AMB62298.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0Y0QKD5; -. 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:0022904; P:respiratory electron transport chain; IEA:InterPro. DR CDD; cd00284; Cytochrome_b_N; 1. DR InterPro; IPR005797; Cyt_b/b6_N. DR InterPro; IPR027387; Cytb/b6-like_sf. DR InterPro; IPR048259; Cytochrome_b_N_euk/bac. DR InterPro; IPR016174; Di-haem_cyt_TM. DR PANTHER; PTHR19271; CYTOCHROME B; 1. DR PANTHER; PTHR19271:SF37; CYTOCHROME B; 1. DR Pfam; PF00033; Cytochrome_B; 1. DR SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 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:AMB62298.1}; 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 30..56 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 77..98 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 113..133 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 140..158 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 178..199 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..200 FT /note="Cytochrome b/b6 N-terminal region profile" FT /evidence="ECO:0000259|PROSITE:PS51002" FT NON_TER 200 FT /evidence="ECO:0000313|EMBL:AMB62298.1" SQ SEQUENCE 200 AA; 22603 MW; 65192A76E33DABA9 CRC64; MTNIRKMHPL AKIINNSLID LPAPSNISAW WNFGSLLAVC LALQILTGLF LAMHYTSDTT TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLYMHVGR GLYYGSYTLM ETWNIGIILL FMIMATAFMG YVLPWGQMSF WGATVITNLL SAVPYIGTNL VEWIWGGFSV DKATLTRFFA FHFILPFVAS ALVMVHLLFL //