CYB_TETNG
ID CYB_TETNG Reviewed; 380 AA.
AC Q4JQH5; Q9T3U3; Q9TEC9; Q9XMK8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17076253; DOI=10.1080/10425170600700378;
RA Yue G.H., Lo L.C., Zhu Z.Y., Lin G., Feng F.;
RT "The complete nucleotide sequence of the mitochondrial genome of Tetraodon
RT nigroviridis.";
RL DNA Seq. 17:115-121(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-134, AND VARIANT ILE-42.
RA Fischer C., Bouneau L., Roest Crollius H., Quetier F., Weissenbach J.,
RA Bernot A.;
RT "Evolutionary relationships and discrimination between T. nigroviridis and
RT T. fluviatilis at the molecular level.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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 3 respiratory subunits
CC (MT-CYB, CYC1 and UQCRFS1), 2 core proteins (UQCRC1 and UQCRC2) and
CC probably 6 low-molecular weight proteins.
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; DQ019313; AAY26163.1; -; Genomic_DNA.
DR EMBL; AJ248546; CAB51151.1; -; Genomic_DNA.
DR EMBL; AJ248547; CAB51152.1; -; Genomic_DNA.
DR EMBL; AJ248548; CAB51153.1; -; Genomic_DNA.
DR EMBL; AJ248549; CAB51154.1; -; Genomic_DNA.
DR EMBL; AJ248550; CAB51155.1; -; Genomic_DNA.
DR EMBL; AJ248556; CAB51156.1; -; Genomic_DNA.
DR EMBL; AJ248558; CAB51157.1; -; Genomic_DNA.
DR EMBL; AJ248559; CAB51158.1; -; Genomic_DNA.
DR EMBL; AJ248560; CAB51159.1; -; Genomic_DNA.
DR EMBL; AJ248561; CAB51160.1; -; Genomic_DNA.
DR EMBL; AJ248562; CAB51161.1; -; Genomic_DNA.
DR EMBL; AJ248563; CAB51162.1; -; Genomic_DNA.
DR EMBL; AJ248564; CAB51163.1; -; Genomic_DNA.
DR EMBL; AJ248565; CAB51164.1; -; Genomic_DNA.
DR EMBL; AJ248566; CAB51165.1; -; Genomic_DNA.
DR EMBL; AJ248567; CAB51166.1; -; Genomic_DNA.
DR EMBL; AJ248568; CAB51167.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4JQH5; -.
DR SMR; Q4JQH5; -.
DR STRING; 99883.ENSTNIP00000007009; -.
DR Ensembl; ENSTNIT00000007164; ENSTNIP00000007009; ENSTNIG00000004374.
DR GeneTree; ENSGT00390000017948; -.
DR HOGENOM; CLU_031114_3_0_1; -.
DR InParanoid; Q4JQH5; -.
DR OMA; RFFAFHF; -.
DR TreeFam; TF353088; -.
DR Proteomes; UP000007303; Mitochondrion.
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; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..380
FT /note="Cytochrome b"
FT /id="PRO_0000061655"
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 321..342
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00157"
FT TRANSMEM 349..369
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 42
FT /note="V -> I"
FT /evidence="ECO:0000269|Ref.2"
SQ SEQUENCE 380 AA; 42548 MW; 61FE71A2A08FF57A CRC64;
MASLRKTHPL MKIANDMVVD LPTPSNISAW WNFGSLLGLC LVAQILTGLF LAMHYTSDIA
TAFSSVAHIC RDVNYGWLIR NLHANGASFF FICLYLHIGR GLYYGSYLQK ETWNIGVVLL
LLVMATAFVG YVLPWGQMSF WGATVITNLL SAVPYVGNTL VQWVWGGFSV DHATLTRFFA
FHFLLPFIVA AAVIVHLIFL HETGSNNPLG LNSDTDKIPF HPYFSYKDLI GFTVLLTTLT
MLALFSPNYL GDPDNFTPAN PLVTPAHIKP EWYFLFAYAI LRSIPNKLGG VLALLASILR
LMEVPLLHTS KKRKPYFSDP LTNFLFWTLI GRMWPSSPES EACLVEHPYV IIGQAASILY
FSLFLVLMPA AGWLENKTLQ
