ID   G3JYV8_TAMPA            Unreviewed;       372 AA.
AC   G3JYV8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-NOV-2024, entry version 48.
DE   RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, 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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   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 chipmunks
RT   (Tamias) in the face of introgression using reproductive protein genes.";
RL   Syst. Biol. 61:44-62(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: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004448}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family.
CC       {ECO:0000256|RuleBase:RU362117}.
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DR   EMBL; JN042472; AEO79517.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3JYV8; -.
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:TreeGrafter.
DR   CDD; cd00290; cytochrome_b_C; 1.
DR   CDD; cd00284; Cytochrome_b_N; 1.
DR   FunFam; 1.20.810.10:FF:000002; Cytochrome b; 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        23..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        138..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        171..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        222..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        281..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   TRANSMEM        338..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362117"
FT   DOMAIN          1..202
FT                   /note="Cytochrome b/b6 N-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51002"
FT   DOMAIN          203..372
FT                   /note="Cytochrome b/b6 C-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51003"
FT   BINDING         76
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         90
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         175
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         189
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         194
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:AEO79517.1"
FT   NON_TER         372
FT                   /evidence="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
//