CYB_STULI
ID CYB_STULI Reviewed; 379 AA.
AC Q35873; Q9GAM4; R4RYE7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 3.
DT 03-AUG-2022, entry version 96.
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 Sturnira lilium (Lesser yellow-shouldered bat).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Stenodermatinae; Sturnira.
OX NCBI_TaxID=27660;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate TK 22631;
RA Wright A.J., Van Den Bussche R.A., Lim B.K., Engstrom M.D., Baker R.J.;
RT "Systematics of the genera Carollia and Rhinophylla based on the cytochrome
RT b gene.";
RL J. Mammal. 80:1202-1213(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23632030; DOI=10.1016/j.ympev.2013.04.016;
RA Velazco P.M., Patterson B.D.;
RT "Diversification of the Yellow-shouldered bats, Genus Sturnira (Chiroptera,
RT Phyllostomidae), in the New World tropics.";
RL Mol. Phylogenet. Evol. 68:683-698(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
RC STRAIN=Isolate LSUMZ 25478; TISSUE=Kidney, and Liver;
RA Sudman P.D., Barkley L.J., Hafner M.S.;
RT "Familial affinity of Tomopeas ravus (Chiroptera) based on protein
RT electrophoretic and cytochrome b sequence data.";
RL J. Mammal. 75:365-377(1994).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG25916.1; Type=Miscellaneous discrepancy; Note=Sequence of dubious origin with higher similarity with canine sequences.; Evidence={ECO:0000305};
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DR EMBL; AF187035; AAG25916.1; ALT_SEQ; Genomic_DNA.
DR EMBL; KC753847; AGL94629.1; -; Genomic_DNA.
DR EMBL; L19733; AAA18504.1; -; Genomic_DNA.
DR AlphaFoldDB; Q35873; -.
DR SMR; Q35873; -.
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-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_0000061620"
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 CONFLICT 55
FT /note="Y -> C (in Ref. 3; AAA18504)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="L -> S (in Ref. 3; AAA18504)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="P -> S (in Ref. 3; AAA18504)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="S -> F (in Ref. 3; AAA18504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 42561 MW; D0CC74E7FD2D8F20 CRC64;
MTNIRKTHPL LKIINNSLVD LPAPSSLSSW WNFGSLLGVC LGVQILTGLF LAMHYTSDTA
TAFNSVTHIC RDVNYGWLLR YLHANGASMF FICLYLHVGR GLYYGSYTYS ETWNIGILLL
FAVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTEL VQWIWGGFSV DKATLTRFFA
FHFLLPFIVA ALVMVHLLFL HETGSNNPTG IPSDPDMIPF HPYYTIKDIL GFLIMLTALS
ALVLFSPDLL GDPDNYIPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALVLSILI
LAIIPILHMS KQRSMMFRPL SQCLFWLLVA VLLTLTWIGG QPVEHPYIII GQTASVLYFL
ILLVLMPLTS ITENHLLKW
