CYB_MICMU
ID CYB_MICMU Reviewed; 379 AA.
AC Q9G0S9; Q35043; Q8HEG1; Q9G935; Q9G936; Q9G937; Q9G938; Q9G939; Q9G940;
AC Q9G941;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Cytochrome b;
DE AltName: Full=Complex III subunit 3;
DE AltName: Full=Complex III subunit III;
DE AltName: Full=Cytochrome b-c1 complex subunit 3;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex cytochrome b subunit;
GN Name=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS Microcebus murinus (Gray mouse lemur) (Lemur murinus).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Cheirogaleidae; Microcebus.
OX NCBI_TaxID=30608;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8643538; DOI=10.1073/pnas.93.10.5122;
RA Yoder A.D., Cartmill M., Ruvolo M., Smith K., Vilgalys R.;
RT "Ancient single origin for Malagasy primates.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5122-5126(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 00-016A-8EBC, Isolate Jorg 33, Isolate Jorg 37,
RC Isolate Jorg 64, Isolate RMR 24, Isolate RMR 44, Isolate YLE199, and
RC Isolate YLE74;
RX PubMed=11005834; DOI=10.1073/pnas.200121897;
RA Yoder A.D., Rasoloarison R.M., Goodman S.M., Irwin J.A., Atsalis S.,
RA Ravosa M.J., Ganzhorn J.U.;
RT "Remarkable species diversity in Malagasy mouse lemurs (primates,
RT Microcebus).";
RL Proc. Natl. Acad. Sci. U.S.A. 97:11325-11330(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate YLE357;
RA Yoder A.D., Burns M.M., Genin F.;
RT "Molecular evidence of reproductive isolation in sympatric sibling species
RT of mouse lemurs.";
RL Folia Primatol. 23:1335-1343(2002).
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:0000250|UniProtKB:P00157}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:P00157};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000250|UniProtKB:P00157};
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:0000250|UniProtKB:P00157}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00157}.
CC -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at
CC about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs
CC at about 566 nm. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
CC -!- CAUTION: The full-length protein contains only eight transmembrane
CC helices, not nine as predicted by bioinformatics tools.
CC {ECO:0000250|UniProtKB:P00157}.
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DR EMBL; U53572; AAC50529.1; -; Genomic_DNA.
DR EMBL; AF285557; AAG30702.1; -; Genomic_DNA.
DR EMBL; AF285558; AAG30703.1; -; Genomic_DNA.
DR EMBL; AF285559; AAG30704.1; -; Genomic_DNA.
DR EMBL; AF285560; AAG30705.1; -; Genomic_DNA.
DR EMBL; AF285561; AAG30706.1; -; Genomic_DNA.
DR EMBL; AF285562; AAG30707.1; -; Genomic_DNA.
DR EMBL; AF285563; AAG30708.1; -; Genomic_DNA.
DR EMBL; AF285564; AAG30709.1; -; Genomic_DNA.
DR EMBL; AF285565; AAG30710.1; -; Genomic_DNA.
DR EMBL; AF285566; AAG30711.1; -; Genomic_DNA.
DR EMBL; AY167071; AAN86562.1; -; Genomic_DNA.
DR RefSeq; YP_009192261.1; NC_028718.1.
DR AlphaFoldDB; Q9G0S9; -.
DR SMR; Q9G0S9; -.
DR Ensembl; ENSMICT00000053028; ENSMICP00000022746; ENSMICG00000037851.
DR GeneID; 26823990; -.
DR KEGG; mmur:26823990; -.
DR CTD; 4519; -.
DR GeneTree; ENSGT00390000017948; -.
DR OrthoDB; 1125966at2759; -.
DR Bgee; ENSMICG00000037851; Expressed in adult mammalian kidney and 8 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..379
FT /note="Cytochrome b"
FT /id="PRO_0000061187"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
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:0000250|UniProtKB:P00157"
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:0000250|UniProtKB:P00157"
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:0000250|UniProtKB:P00157"
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:0000250|UniProtKB:P00157"
FT BINDING 201
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT VARIANT 2
FT /note="T -> A (in strain: Isolate RMR 24)"
FT VARIANT 42
FT /note="V -> A (in strain: Isolate Jorg 37)"
FT VARIANT 78
FT /note="I -> V (in strain: Isolate Jorg 64)"
FT VARIANT 158
FT /note="T -> N (in strain: Isolate YLE357)"
FT VARIANT 183
FT /note="F -> Y (in strain: Isolate Jorg 33)"
FT VARIANT 185
FT /note="L -> M (in strain: Isolate RMR 24)"
FT VARIANT 186
FT /note="P -> T (in strain: Isolate YLE74)"
FT VARIANT 195
FT /note="V -> I (in strain: Isolate RMR 44)"
FT VARIANT 234
FT /note="F -> L (in strain: Isolate Jorg 64)"
FT VARIANT 251
FT /note="G -> D (in strain: Isolate Jorg 64)"
FT VARIANT 316
FT /note="T -> A (in strain: Isolate Jorg 37)"
FT VARIANT 324
FT /note="M -> I (in strain: Isolate 00-016A-8EBC and Isolate
FT RMR 24)"
FT VARIANT 324
FT /note="M -> T (in strain: Isolate YLE199)"
FT VARIANT 345
FT /note="H -> Y (in strain: Isolate 00-016A-8EBC, Isolate RMR
FT 24 and Isolate YLE199)"
SQ SEQUENCE 379 AA; 42819 MW; EAD063C413622F72 CRC64;
MTNIRKTHPL MKIMNNSFID LPAPSNISSW WNFGSLLGAC LVIQIITGLF LAMHYTADTT
TAFSSVTHIC RDVNQGWIIR YLHANGASMF FLCLFLHVGR GMYYGSFTLT ETWNIGIILL
FTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYMGTDL VEWIWGGFSV DKATLTRFFA
FHFILPFVIL ALVMVHLLFL HETGSNNPLG IPSESDKIPF HPYYTIKDLL GLMFLLITLM
ILVLFSPDLL GDPDNYMPAN PLSTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVMSILI
LAIIPMLQTA KQRSMTFRPL SQIMFWILTA DLLILTWIGG QPVEHPFVTI GQVASILYFS
LILIIMPTVS LFENKMLKW
