ID   A0A3G4R2E0_OCHKO        Unreviewed;       379 AA.
AC   A0A3G4R2E0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   29-MAY-2024, entry version 17.
DE   RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117};
GN   Name=CYTB {ECO:0000313|EMBL:AYU56860.1};
OS   Ochotona koslowi (Koslov's pika).
OG   Mitochondrion {ECO:0000313|EMBL:AYU56860.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Ochotonidae; Ochotona.
OX   NCBI_TaxID=130835 {ECO:0000313|EMBL:AYU56860.1};
RN   [1] {ECO:0000313|EMBL:AYU56860.1}
RP   NUCLEOTIDE SEQUENCE.
RA   He J.Y., Ma G.Y., Xie C.H., Zhang Z.T., Su P.J.;
RT   "The complete mitochondrial DNA sequence of Ochotona koslowi.";
RL   Submitted (FEB-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   -!- 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.
CC       {ECO:0000256|RuleBase:RU362117}.
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DR   EMBL; MG888668; AYU56860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G4R2E0; -.
DR   SMR; A0A3G4R2E0; -.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:TreeGrafter.
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:TreeGrafter.
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,
KW   ECO:0000256|RuleBase:RU362117};
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|RuleBase:RU362117};
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,
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        30..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        87..107
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..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        319..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        346..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..379
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   379 AA;  42716 MW;  42268E04B8C06E10 CRC64;
     MTNIRKTHPL MKIVNHSFID LPAPSNISAW WNFGSLLGLC LGIQIITGLF LAMHYTSDTL
     TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLFLHVGR GIYYGSYTYS ETWNIGILLL
     FTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTDL VQWIWGGFSV DKATLTRFFA
     FHFILPFVIA ALVLVHLLFL HETGSNNPTG IISDADKIPF HPYYTIKDAL GFLLLISLLL
     SLVLFHPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSIAI
     LAAMPFLHTS KQRSMMFRPM SQTLFWILVA DLLTLTWIGG QPVEHPFIII GQLASFLYFL
     LILALMPICS LIENKLLKW
//