ID   I3WE50_SORCI            Unreviewed;       371 AA.
AC   I3WE50;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU362117};
DE   Flags: Fragment;
GN   Name=CYTB {ECO:0000313|EMBL:AFL03142.1};
OS   Sorex cinereus (Masked shrew).
OG   Mitochondrion {ECO:0000313|EMBL:AFL03142.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Sorex.
OX   NCBI_TaxID=36803 {ECO:0000313|EMBL:AFL03142.1};
RN   [1] {ECO:0000313|EMBL:AFL03142.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mitochondrial cytochrome b gene partial cds
RC   {ECO:0000313|EMBL:AFL03142.1};
RX   PubMed=22652055; DOI=10.1016/j.ympev.2012.05.021;
RA   Hope A.G., Speer K.A., Demboski J.R., Talbot S.L., Cook J.A.;
RT   "A climate for speciation: Rapid spatial diversification within the Sorex
RT   cinereus complex of shrews.";
RL   Mol. Phylogenet. Evol. 64:671-684(2012).
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; JQ085948; AFL03142.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3WE50; -.
DR   SMR; I3WE50; -.
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:0022904; P:respiratory electron transport chain; IEA:InterPro.
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        24..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        71..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        134..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        172..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        223..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        282..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        313..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        340..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   DOMAIN          1..203
FT                   /note="Cytochrome b/b6 N-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51002"
FT   DOMAIN          204..371
FT                   /note="Cytochrome b/b6 C-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51003"
FT   BINDING         77
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         91
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         176
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         190
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         195
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFL03142.1"
FT   NON_TER         371
FT                   /evidence="ECO:0000313|EMBL:AFL03142.1"
SQ   SEQUENCE   371 AA;  41560 MW;  1F4FE0EC66842BD6 CRC64;
     THPLMKIINS SFIDFPAPSN ISSWWNFGSL LGVCLIVQIL TGLFLAMHYT SDTMTAFSSV
     THICRDVNYG WLIRYLHANG ASMFFICLFL HVGRGLYYGS YMFLETWNIG VLLLFAVMAT
     AFMGYVLPWG QMSFWGATVI TNLLSAIPYI GSDLVEWIWG GFSVDKATLT RFFAFHFILP
     FIIAALAGVH LLFLHETGSN NPSGLCSDAD KIPFHPYYTI KDILGVLLLI LTLTSLVLFS
     PDLLGDPDNY TPANPLNTPP HIKPEWYFLF AYAILRSIPN KLGGVLALVL SILVLAAVPF
     LHTSKQRSMM FRPFSQCLFW ILVADLLTLT WIGGQPVEHP FIIIGQLASI LYFLLILVLM
     PITSLFENNL L
//