CYB_GARIS
ID CYB_GARIS Reviewed; 308 AA.
AC P16363; Q37059;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 110.
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;
DE Flags: Fragment;
GN Name=MT-CYB; Synonyms=COB, CYTB, MTCYB;
OS Garritornis isidorei (Papuan babbler) (Pomatostomus isidorei).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pomatostomidae;
OC Garritornis.
OX NCBI_TaxID=9175;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1676522; DOI=10.1098/rspb.1991.0017;
RA Edwards S.V., Arctander P., Wilson A.C.;
RT "Mitochondrial resolution of a deep branch in the genealogical tree for
RT perching birds.";
RL Proc. R. Soc. B 243:99-107(1991).
RN [2]
RP ERRATUM OF PUBMED:1676522.
RX PubMed=8920253; DOI=10.1098/rspb.1996.0049;
RA Edwards S.V., Arctander P.;
RL Proc. R. Soc. B 263:323-323(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-98.
RC TISSUE=Liver;
RX PubMed=1979038; DOI=10.1093/genetics/126.3.695;
RA Edwards S.V., Wilson A.C.;
RT "Phylogenetically informative length polymorphism and sequence variability
RT in mitochondrial DNA of Australian songbirds (Pomatostomus).";
RL Genetics 126:695-711(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-93.
RX PubMed=2762322; DOI=10.1073/pnas.86.16.6196;
RA Kocher T.D., Thomas W.K., Meyer A., Edwards S.V., Paeaebo S.,
RA Villablanca F.X., Wilson A.C.;
RT "Dynamics of mitochondrial DNA evolution in animals: amplification and
RT sequencing with conserved primers.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6196-6200(1989).
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; X60938; CAA43273.1; -; Genomic_DNA.
DR EMBL; X54913; CAA38685.1; -; Genomic_DNA.
DR EMBL; X54886; CAA38659.1; -; Genomic_DNA.
DR EMBL; X54887; CAA38660.1; -; Genomic_DNA.
DR EMBL; M25689; AAA32140.1; -; Genomic_DNA.
DR PIR; S22928; S22928.
DR AlphaFoldDB; P16363; -.
DR SMR; P16363; -.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 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..>308
FT /note="Cytochrome b"
FT /id="PRO_0000061426"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 45..66
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT BINDING 51
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 65
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 150
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 164
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 169
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT CONFLICT 7
FT /note="M -> I (in Ref. 3; CAA38685/CAA38659/CAA38660)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="G -> A (in Ref. 4; AAA32140)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="A -> T (in Ref. 4; AAA32140)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 308
SQ SEQUENCE 308 AA; 34013 MW; 5BF01EA2B0DDDBDC CRC64;
SGSLLGMCLI VRIITGLFLA AHYTADTSLA FNSVAHTCRN VQFGWLIRNL HANGASLFFI
CIYLHIGRGL YYGSYLNKET WNIGVILLLA LMATAFVGYV LPWGQMSFWG ATVITNLFSA
IPYIGQTLVE WAWGGFSVDN PTLTRFFALH FLLPFVIAGL TLVHLTFLHE TGSNNPLGIP
SDCDKIPFHP YYSTKDVLGF ALLLTPLIAL ALFSPNLLGD PENFTPANPL ATPPHIKPEW
YFLFAYAILR SIPNKLGGVL ALAASVLVLF LIPLLHNSKL RSMTFRPLSQ ILFWALVANL
LVLTWVGS
