CYB_CHICK
ID CYB_CHICK Reviewed; 380 AA.
AC P18946;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 Gallus gallus (Chicken).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX PubMed=2329578; DOI=10.1016/0022-2836(90)90225-b;
RA Desjardins P., Morais R.;
RT "Sequence and gene organization of the chicken mitochondrial genome. A
RT novel gene order in higher vertebrates.";
RL J. Mol. Biol. 212:599-634(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8308906; DOI=10.1007/bf00178867;
RA Kornegay J.R., Kocher T.D., Williams L.A., Wilson A.C.;
RT "Pathways of lysozyme evolution inferred from the sequences of cytochrome b
RT in birds.";
RL J. Mol. Evol. 37:367-379(1993).
RN [3] {ECO:0007744|PDB:1BCC, ECO:0007744|PDB:2BCC, ECO:0007744|PDB:3BCC, ECO:0007744|PDB:3H1H, ECO:0007744|PDB:3H1I, ECO:0007744|PDB:3H1J}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH HEME AND UBIQUINONE,
RP TOPOLOGY, COFACTOR, AND SUBUNIT.
RX PubMed=9565029; DOI=10.1038/33612;
RA Zhang Z., Huang L., Shulmeister V.M., Chi Y.I., Kim K.K., Hung L.W.,
RA Crofts A.R., Berry E.A., Kim S.H.;
RT "Electron transfer by domain movement in cytochrome bc1.";
RL Nature 392:677-684(1998).
RN [4] {ECO:0007744|PDB:3H1L}
RP X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) IN COMPLEX WITH HEME, TOPOLOGY,
RP COFACTOR, AND SUBUNIT.
RX PubMed=20025846; DOI=10.1016/j.bbabio.2009.12.003;
RA Berry E.A., Huang L.S., Lee D.W., Daldal F., Nagai K., Minagawa N.;
RT "Ascochlorin is a novel, specific inhibitor of the mitochondrial cytochrome
RT bc1 complex.";
RL Biochim. Biophys. Acta 1797:360-370(2010).
RN [5] {ECO:0007744|PDB:3L70}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH HEME AND UBIQUINONE,
RP TOPOLOGY, COFACTOR, AND SUBUNIT.
RX PubMed=21575592; DOI=10.1016/j.bbabio.2011.04.005;
RA Berry E.A., Huang L.S.;
RT "Conformationally linked interaction in the cytochrome bc(1) complex
RT between inhibitors of the Q(o) site and the Rieske iron-sulfur protein.";
RL Biochim. Biophys. Acta 1807:1349-1363(2011).
RN [6] {ECO:0007744|PDB:3TGU}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH HEME AND UBIQUINONE,
RP TOPOLOGY, COFACTOR, AND SUBUNIT.
RX PubMed=22690928; DOI=10.1021/ja3001908;
RA Hao G.F., Wang F., Li H., Zhu X.L., Yang W.C., Huang L.S., Wu J.W.,
RA Berry E.A., Yang G.F.;
RT "Computational discovery of picomolar Q(o) site inhibitors of cytochrome
RT bc1 complex.";
RL J. Am. Chem. Soc. 134:11168-11176(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:0000250|UniProtKB:P00157}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:20025846, ECO:0000269|PubMed:21575592,
CC ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029};
CC Note=Binds 2 heme b groups non-covalently.
CC {ECO:0000269|PubMed:20025846, ECO:0000269|PubMed:21575592,
CC ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029};
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:0000269|PubMed:20025846, ECO:0000269|PubMed:21575592,
CC ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20025846, ECO:0000269|PubMed:21575592,
CC ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029}.
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:0000269|PubMed:20025846, ECO:0000269|PubMed:21575592,
CC ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029}.
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DR EMBL; X52392; CAA36636.1; -; Genomic_DNA.
DR EMBL; L08376; AAA18844.1; -; Genomic_DNA.
DR PIR; S10198; S10198.
DR RefSeq; NP_006926.1; NC_001323.1.
DR PDB; 1BCC; X-ray; 3.16 A; C=1-380.
DR PDB; 2BCC; X-ray; 3.50 A; C=1-380.
DR PDB; 3BCC; X-ray; 3.70 A; C=1-380.
DR PDB; 3CWB; X-ray; 3.51 A; C/P=1-380.
DR PDB; 3H1H; X-ray; 3.16 A; C/P=1-380.
DR PDB; 3H1I; X-ray; 3.53 A; C/P=1-380.
DR PDB; 3H1J; X-ray; 3.00 A; C/P=1-380.
DR PDB; 3H1K; X-ray; 3.48 A; C/P=1-380.
DR PDB; 3H1L; X-ray; 3.21 A; C/P=1-380.
DR PDB; 3L70; X-ray; 2.75 A; C/P=1-380.
DR PDB; 3L71; X-ray; 2.84 A; C/P=1-380.
DR PDB; 3L72; X-ray; 3.06 A; C/P=1-380.
DR PDB; 3L73; X-ray; 3.04 A; C/P=1-380.
DR PDB; 3L74; X-ray; 2.76 A; C/P=1-380.
DR PDB; 3L75; X-ray; 2.79 A; C/P=1-380.
DR PDB; 3TGU; X-ray; 2.70 A; C/P=1-380.
DR PDB; 4U3F; X-ray; 3.23 A; C/P=2-380.
DR PDBsum; 1BCC; -.
DR PDBsum; 2BCC; -.
DR PDBsum; 3BCC; -.
DR PDBsum; 3CWB; -.
DR PDBsum; 3H1H; -.
DR PDBsum; 3H1I; -.
DR PDBsum; 3H1J; -.
DR PDBsum; 3H1K; -.
DR PDBsum; 3H1L; -.
DR PDBsum; 3L70; -.
DR PDBsum; 3L71; -.
DR PDBsum; 3L72; -.
DR PDBsum; 3L73; -.
DR PDBsum; 3L74; -.
DR PDBsum; 3L75; -.
DR PDBsum; 3TGU; -.
DR PDBsum; 4U3F; -.
DR AlphaFoldDB; P18946; -.
DR SMR; P18946; -.
DR STRING; 9031.ENSGALP00000034623; -.
DR PaxDb; P18946; -.
DR Ensembl; ENSGALT00000053400; ENSGALP00000049893; ENSGALG00000032079.
DR VEuPathDB; HostDB:geneid_63549472; -.
DR eggNOG; KOG4663; Eukaryota.
DR GeneTree; ENSGT00390000017948; -.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; P18946; -.
DR OMA; RFFAFHF; -.
DR OrthoDB; 1125966at2759; -.
DR PhylomeDB; P18946; -.
DR TreeFam; TF353088; -.
DR Reactome; R-GGA-611105; Respiratory electron transport.
DR EvolutionaryTrace; P18946; -.
DR PRO; PR:P18946; -.
DR Proteomes; UP000000539; Mitochondrion.
DR Bgee; ENSGALG00000032079; Expressed in spermatocyte and 13 other tissues.
DR ExpressionAtlas; P18946; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IMP:AgBase.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:AgBase.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
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; NAS:AgBase.
DR GO; GO:0006979; P:response to oxidative stress; IEP:AgBase.
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 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transmembrane; Transmembrane helix; Transport;
KW Ubiquinone.
FT CHAIN 1..380
FT /note="Cytochrome b"
FT /id="PRO_0000060776"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:3L70"
FT TRANSMEM 78..99
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:3L70"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:3L70"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:3L70"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:3L70"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:3L70"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:3L70"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:3L70"
FT BINDING 84
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:0000255|PROSITE-ProRule:PRU00968,
FT ECO:0000269|PubMed:20025846, ECO:0000269|PubMed:21575592,
FT ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029,
FT ECO:0007744|PDB:1BCC, ECO:0007744|PDB:2BCC,
FT ECO:0007744|PDB:3BCC, ECO:0007744|PDB:3H1H,
FT ECO:0007744|PDB:3H1I, ECO:0007744|PDB:3H1J,
FT ECO:0007744|PDB:3H1K, ECO:0007744|PDB:3H1L,
FT ECO:0007744|PDB:3L70, ECO:0007744|PDB:3L71,
FT ECO:0007744|PDB:3L72, ECO:0007744|PDB:3L73,
FT ECO:0007744|PDB:3L74, ECO:0007744|PDB:3L75,
FT ECO:0007744|PDB:3TGU"
FT BINDING 98
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:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:1BCC,
FT ECO:0007744|PDB:2BCC, ECO:0007744|PDB:3BCC,
FT ECO:0007744|PDB:3CWB, ECO:0007744|PDB:3H1H,
FT ECO:0007744|PDB:3H1I, ECO:0007744|PDB:3H1J,
FT ECO:0007744|PDB:3H1K, ECO:0007744|PDB:3H1L,
FT ECO:0007744|PDB:3L70, ECO:0007744|PDB:3L71,
FT ECO:0007744|PDB:3L72, ECO:0007744|PDB:3L73,
FT ECO:0007744|PDB:3L74, ECO:0007744|PDB:3L75,
FT ECO:0007744|PDB:3TGU"
FT BINDING 183
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:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:1BCC,
FT ECO:0007744|PDB:2BCC, ECO:0007744|PDB:3H1H,
FT ECO:0007744|PDB:3H1I, ECO:0007744|PDB:3H1J,
FT ECO:0007744|PDB:3H1L, ECO:0007744|PDB:3L70,
FT ECO:0007744|PDB:3L71, ECO:0007744|PDB:3L72,
FT ECO:0007744|PDB:3L73, ECO:0007744|PDB:3L74,
FT ECO:0007744|PDB:3L75, ECO:0007744|PDB:3TGU"
FT BINDING 197
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:0000269|PubMed:20025846,
FT ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928,
FT ECO:0000269|PubMed:9565029, ECO:0007744|PDB:1BCC,
FT ECO:0007744|PDB:2BCC, ECO:0007744|PDB:3BCC,
FT ECO:0007744|PDB:3CWB, ECO:0007744|PDB:3H1H,
FT ECO:0007744|PDB:3H1I, ECO:0007744|PDB:3H1J,
FT ECO:0007744|PDB:3H1K, ECO:0007744|PDB:3H1L,
FT ECO:0007744|PDB:3L70, ECO:0007744|PDB:3L71,
FT ECO:0007744|PDB:3L72, ECO:0007744|PDB:3L73,
FT ECO:0007744|PDB:3L74, ECO:0007744|PDB:3L75,
FT ECO:0007744|PDB:3TGU"
FT BINDING 202
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000269|PubMed:21575592,
FT ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029,
FT ECO:0007744|PDB:1BCC, ECO:0007744|PDB:3CWB,
FT ECO:0007744|PDB:3H1K, ECO:0007744|PDB:3L72"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 34..53
FT /evidence="ECO:0007829|PDB:3TGU"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 77..104
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 111..133
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 138..148
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 173..204
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 221..246
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 276..284
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3L74"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 320..341
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 348..364
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 366..377
FT /evidence="ECO:0007829|PDB:3TGU"
SQ SEQUENCE 380 AA; 42592 MW; D2D4496EC294D77A CRC64;
MAPNIRKSHP LLKMINNSLI DLPAPSNISA WWNFGSLLAV CLMTQILTGL LLAMHYTADT
SLAFSSVAHT CRNVQYGWLI RNLHANGASF FFICIFLHIG RGLYYGSYLY KETWNTGVIL
LLTLMATAFV GYVLPWGQMS FWGATVITNL FSAIPYIGHT LVEWAWGGFS VDNPTLTRFF
ALHFLLPFAI AGITIIHLTF LHESGSNNPL GISSDSDKIP FHPYYSFKDI LGLTLMLTPF
LTLALFSPNL LGDPENFTPA NPLVTPPHIK PEWYFLFAYA ILRSIPNKLG GVLALAASVL
ILFLIPFLHK SKQRTMTFRP LSQTLFWLLV ANLLILTWIG SQPVEHPFII IGQMASLSYF
TILLILFPTI GTLENKMLNY
