ID   A0A2P1BT90_9CERV        Unreviewed;       137 AA.
AC   A0A2P1BT90;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-NOV-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:AVI57478.1};
OS   Cervus hanglu hanglu (Kashmir red deer).
OG   Mitochondrion {ECO:0000313|EMBL:AVI57478.1}.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Cervus.
OX   NCBI_TaxID=408872 {ECO:0000313|EMBL:AVI57478.1};
RN   [1] {ECO:0000313|EMBL:AVI57478.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=D183 {ECO:0000313|EMBL:AVI57478.1};
RA   Meiri M., Kosintsev P., Conroy K., Meiri S., Barnes I., Lister A.;
RT   "Subspecies dynamics in space and time: a study of the red deer complex
RT   using ancient and modern DNA and morphology.";
RL   J. Biogeogr. 0:0-0(2018).
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: Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004448}.
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DR   EMBL; MG020595; AVI57478.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P1BT90; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:TreeGrafter.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:TreeGrafter.
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:SF16; 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:AVI57478.1};
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        26..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..137
FT                   /note="Cytochrome b/b6 N-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51002"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AVI57478.1"
FT   NON_TER         137
FT                   /evidence="ECO:0000313|EMBL:AVI57478.1"
SQ   SEQUENCE   137 AA;  15666 MW;  12577FF937D7038C CRC64;
     RKTHPLMKIV NNAFIDLPAP SNISSWWNFG SLLGICLILQ ILTGLFLAMH YTSDTMTAFS
     SVTHICRDVN YGWIIRYMHA NGASMFFICL FMHVGRGLYY GSYTFLETWN IGVILLFTVM
     ATAFVGYVLP WGQMSFW
//