ID   G3JYV8_TAMPA            Unreviewed;       372 AA.
AC   G3JYV8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   03-JUL-2019, entry version 34.
DE   RecName: Full=Cytochrome b {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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha;
OC   Sciuridae; 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
RT   chipmunks (Tamias) in the face of introgression using reproductive
RT   protein genes.";
RL   Syst. Biol. 61:44-62(2012).
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase
CC       complex (complex III or cytochrome b-c1 complex) that is part of
CC       the mitochondrial respiratory chain. The b-c1 complex mediates
CC       electron transfer from ubiquinol to cytochrome c. Contributes to
CC       the generation of a proton gradient across the mitochondrial
CC       membrane that is then used for ATP synthesis.
CC       {ECO:0000256|RuleBase:RU362117}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038885-2,
CC         ECO:0000256|RuleBase:RU362117};
CC       Note=Binds 2 heme groups non-covalently.
CC       {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|RuleBase:RU362117}.
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   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:InterPro.
DR   CDD; cd00290; cytochrome_b_C; 1.
DR   CDD; cd00284; Cytochrome_b_N; 1.
DR   Gene3D; 1.20.810.10; -; 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; IPR016174; Di-haem_cyt_TM.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   PIRSF; PIRSF038885; COB; 1.
DR   SUPFAM; SSF81342; SSF81342; 1.
DR   SUPFAM; SSF81648; SSF81648; 1.
DR   PROSITE; PS51003; CYTB_CTER; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|RuleBase:RU362117};
KW   Heme {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117};
KW   Iron {ECO:0000256|PIRSR:PIRSR038885-2, ECO:0000256|RuleBase:RU362117};
KW   Membrane {ECO:0000256|RuleBase:RU362117};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038885-2,
KW   ECO:0000256|RuleBase:RU362117};
KW   Mitochondrion {ECO:0000256|RuleBase:RU362117,
KW   ECO:0000313|EMBL:AEO79517.1};
KW   Respiratory chain {ECO:0000256|RuleBase:RU362117};
KW   Transmembrane {ECO:0000256|RuleBase:RU362117};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362117};
KW   Transport {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM     23     45       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM     80    100       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    106    126       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    138    159       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    171    193       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    222    239       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    281    300       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    312    332       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   TRANSMEM    338    365       Helical. {ECO:0000256|RuleBase:RU362117}.
FT   DOMAIN        1    202       CYTB_NTER. {ECO:0000259|PROSITE:PS51002}.
FT   DOMAIN      203    372       CYTB_CTER. {ECO:0000259|PROSITE:PS51003}.
FT   METAL        76     76       Iron 1 (heme b562 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038885-2}.
FT   METAL        90     90       Iron 2 (heme b566 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038885-2}.
FT   METAL       175    175       Iron 1 (heme b562 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038885-2}.
FT   METAL       189    189       Iron 2 (heme b566 axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR038885-2}.
FT   BINDING     194    194       Ubiquinone. {ECO:0000256|PIRSR:
FT                                PIRSR038885-1}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:AEO79517.1}.
FT   NON_TER     372    372       {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
//