Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytochrome b

Gene

MT-CYB

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.

Cofactori

hemeNote: Binds 2 heme groups non-covalently.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi83 – 831Iron 1 (heme b562 axial ligand)PROSITE-ProRule annotation1 Publication
Metal bindingi97 – 971Iron 2 (heme b566 axial ligand)
Metal bindingi182 – 1821Iron 1 (heme b562 axial ligand)
Metal bindingi196 – 1961Iron 2 (heme b566 axial ligand)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_281214. Respiratory electron transport.

Protein family/group databases

TCDBi3.D.3.2.1. the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b
Alternative name(s):
Complex III subunit 3
Complex III subunit III
Cytochrome b-c1 complex subunit 3
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Gene namesi
Name:MT-CYB
Synonyms:COB, CYTB, MTCYB
Encoded oniMitochondrion
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Mitochondrion

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei33 – 5321HelicalSequence AnalysisAdd
BLAST
Transmembranei76 – 9823HelicalSequence AnalysisAdd
BLAST
Transmembranei115 – 13521HelicalSequence AnalysisAdd
BLAST
Transmembranei140 – 15819HelicalSequence AnalysisAdd
BLAST
Transmembranei178 – 19821HelicalSequence AnalysisAdd
BLAST
Transmembranei229 – 24921HelicalSequence AnalysisAdd
BLAST
Transmembranei288 – 30821HelicalSequence AnalysisAdd
BLAST
Transmembranei323 – 34321HelicalSequence AnalysisAdd
BLAST
Transmembranei346 – 36621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 379379Cytochrome bPRO_0000060686Add
BLAST

Proteomic databases

PRIDEiP00157.

Expressioni

Gene expression databases

ExpressionAtlasiP00157. baseline.

Interactioni

Subunit structurei

The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1).

Protein-protein interaction databases

DIPiDIP-350N.
IntActiP00157. 2 interactions.
STRINGi9913.ENSBTAP00000053148.

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Helixi9 – 1810Combined sources
Beta strandi22 – 243Combined sources
Helixi29 – 313Combined sources
Helixi33 – 5220Combined sources
Turni59 – 613Combined sources
Helixi62 – 7211Combined sources
Beta strandi73 – 753Combined sources
Helixi76 – 10328Combined sources
Helixi106 – 1083Combined sources
Helixi110 – 13223Combined sources
Helixi137 – 14711Combined sources
Helixi148 – 1525Combined sources
Turni154 – 1563Combined sources
Helixi157 – 1659Combined sources
Beta strandi167 – 1704Combined sources
Helixi172 – 20332Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2193Combined sources
Helixi220 – 24526Combined sources
Turni247 – 2504Combined sources
Helixi253 – 2564Combined sources
Turni261 – 2633Combined sources
Helixi272 – 2743Combined sources
Helixi275 – 2828Combined sources
Beta strandi284 – 2863Combined sources
Helixi287 – 29913Combined sources
Helixi300 – 3078Combined sources
Beta strandi311 – 3155Combined sources
Helixi319 – 33921Combined sources
Helixi347 – 36317Combined sources
Helixi365 – 37612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE3X-ray3.00C1-379[»]
1BGYX-ray3.00C/O1-379[»]
1L0LX-ray2.35C1-379[»]
1L0NX-ray2.60C1-379[»]
1NTKX-ray2.60C1-379[»]
1NTMX-ray2.40C1-379[»]
1NTZX-ray2.60C1-379[»]
1NU1X-ray3.20C1-379[»]
1PP9X-ray2.10C/P1-379[»]
1PPJX-ray2.10C/P1-379[»]
1QCRX-ray2.70C2-379[»]
1SQBX-ray2.69C1-379[»]
1SQPX-ray2.70C1-379[»]
1SQQX-ray3.00C1-379[»]
1SQVX-ray2.85C1-379[»]
1SQXX-ray2.60C1-379[»]
2A06X-ray2.10C/P1-379[»]
2FYUX-ray2.26C1-379[»]
2YBBelectron microscopy19.00C/c1-379[»]
4D6TX-ray3.57C/P1-379[»]
4D6UX-ray4.09C/P1-379[»]
ProteinModelPortaliP00157.
SMRiP00157. Positions 1-379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00157.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome b family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1290.
GeneTreeiENSGT00390000017948.
HOGENOMiHOG000255206.
HOVERGENiHBG017694.
InParanoidiP00157.
KOiK00412.
OMAiPEHIVPE.
OrthoDBiEOG7BGHKX.
TreeFamiTF353088.

Family and domain databases

Gene3Di1.20.810.10. 1 hit.
InterProiIPR005798. Cyt_b/b6_C.
IPR005797. Cyt_b/b6_N.
IPR027387. Cytb/b6-like.
IPR030689. Cytochrome_b.
IPR016174. Di-haem_cyt_TM.
[Graphical view]
PfamiPF00032. Cytochrom_B_C. 1 hit.
PF13631. Cytochrom_B_N_2. 1 hit.
[Graphical view]
PIRSFiPIRSF038885. COB. 1 hit.
SUPFAMiSSF81342. SSF81342. 1 hit.
SSF81648. SSF81648. 1 hit.
PROSITEiPS51003. CYTB_CTER. 1 hit.
PS51002. CYTB_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00157-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNIRKSHPL MKIVNNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF
60 70 80 90 100
LAMHYTSDTT TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLYMHVGR
110 120 130 140 150
GLYYGSYTFL ETWNIGVILL LTVMATAFMG YVLPWGQMSF WGATVITNLL
160 170 180 190 200
SAIPYIGTNL VEWIWGGFSV DKATLTRFFA FHFILPFIIM AIAMVHLLFL
210 220 230 240 250
HETGSNNPTG ISSDVDKIPF HPYYTIKDIL GALLLILALM LLVLFAPDLL
260 270 280 290 300
GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALAFSILI
310 320 330 340 350
LALIPLLHTS KQRSMMFRPL SQCLFWALVA DLLTLTWIGG QPVEHPYITI
360 370
GQLASVLYFL LILVLMPTAG TIENKLLKW
Length:379
Mass (Da):42,591
Last modified:July 21, 1986 - v1
Checksum:i90160B99E031E016
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901F → V in strain: 65, 66 and D.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00654 Genomic DNA. Translation: CAA24007.1.
AF490528 Genomic DNA. Translation: AAM08329.1.
AF490529 Genomic DNA. Translation: AAM08342.1.
AF493541 Genomic DNA. Translation: AAM12801.1.
AF493542 Genomic DNA. Translation: AAM12814.1.
PIRiA00152. CBBO.
RefSeqiYP_209217.1. NC_006853.1.

Genome annotation databases

EnsembliENSBTAT00000060567; ENSBTAP00000053148; ENSBTAG00000043550.
GeneIDi3283889.
KEGGibta:3283889.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00654 Genomic DNA. Translation: CAA24007.1.
AF490528 Genomic DNA. Translation: AAM08329.1.
AF490529 Genomic DNA. Translation: AAM08342.1.
AF493541 Genomic DNA. Translation: AAM12801.1.
AF493542 Genomic DNA. Translation: AAM12814.1.
PIRiA00152. CBBO.
RefSeqiYP_209217.1. NC_006853.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE3X-ray3.00C1-379[»]
1BGYX-ray3.00C/O1-379[»]
1L0LX-ray2.35C1-379[»]
1L0NX-ray2.60C1-379[»]
1NTKX-ray2.60C1-379[»]
1NTMX-ray2.40C1-379[»]
1NTZX-ray2.60C1-379[»]
1NU1X-ray3.20C1-379[»]
1PP9X-ray2.10C/P1-379[»]
1PPJX-ray2.10C/P1-379[»]
1QCRX-ray2.70C2-379[»]
1SQBX-ray2.69C1-379[»]
1SQPX-ray2.70C1-379[»]
1SQQX-ray3.00C1-379[»]
1SQVX-ray2.85C1-379[»]
1SQXX-ray2.60C1-379[»]
2A06X-ray2.10C/P1-379[»]
2FYUX-ray2.26C1-379[»]
2YBBelectron microscopy19.00C/c1-379[»]
4D6TX-ray3.57C/P1-379[»]
4D6UX-ray4.09C/P1-379[»]
ProteinModelPortaliP00157.
SMRiP00157. Positions 1-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-350N.
IntActiP00157. 2 interactions.
STRINGi9913.ENSBTAP00000053148.

Protein family/group databases

TCDBi3.D.3.2.1. the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.

Proteomic databases

PRIDEiP00157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000060567; ENSBTAP00000053148; ENSBTAG00000043550.
GeneIDi3283889.
KEGGibta:3283889.

Organism-specific databases

CTDi4519.

Phylogenomic databases

eggNOGiCOG1290.
GeneTreeiENSGT00390000017948.
HOGENOMiHOG000255206.
HOVERGENiHBG017694.
InParanoidiP00157.
KOiK00412.
OMAiPEHIVPE.
OrthoDBiEOG7BGHKX.
TreeFamiTF353088.

Enzyme and pathway databases

ReactomeiREACT_281214. Respiratory electron transport.

Miscellaneous databases

EvolutionaryTraceiP00157.
NextBioi20810196.
PROiP00157.

Gene expression databases

ExpressionAtlasiP00157. baseline.

Family and domain databases

Gene3Di1.20.810.10. 1 hit.
InterProiIPR005798. Cyt_b/b6_C.
IPR005797. Cyt_b/b6_N.
IPR027387. Cytb/b6-like.
IPR030689. Cytochrome_b.
IPR016174. Di-haem_cyt_TM.
[Graphical view]
PfamiPF00032. Cytochrom_B_C. 1 hit.
PF13631. Cytochrom_B_N_2. 1 hit.
[Graphical view]
PIRSFiPIRSF038885. COB. 1 hit.
SUPFAMiSSF81342. SSF81342. 1 hit.
SSF81648. SSF81648. 1 hit.
PROSITEiPS51003. CYTB_CTER. 1 hit.
PS51002. CYTB_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome."
    Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F., Young I.G.
    J. Mol. Biol. 156:683-717(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: HerefordImported.
    Tissue: Heart.
  2. "Evolution of the cytochrome b gene of mammals."
    Irwin D.M., Kocher T.D., Wilson A.C.
    J. Mol. Evol. 32:128-144(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Bos taurus mitochondrial protein coding regions."
    Wettstein P.J.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 65, 66, D and F.
  4. "Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria."
    Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L., Deisenhofer J.
    Science 277:60-66(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  5. "Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex."
    Iwata S., Lee J.W., Okada K., Lee J.K., Iwata M., Rasmussen B., Link T.A., Ramaswamy S., Jap B.K.
    Science 281:64-71(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  6. "The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition."
    Gao X., Wen X., Yu C., Esser L., Tsao S., Quinn B., Zhang L., Yu L., Xia D.
    Biochemistry 41:11692-11702(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
  7. "Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex."
    Esser L., Quinn B., Li Y.F., Zhang M., Elberry M., Yu L., Yu C.A., Xia D.
    J. Mol. Biol. 341:281-302(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS).
  8. "Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern."
    Huang L.S., Cobessi D., Tung E.Y., Berry E.A.
    J. Mol. Biol. 351:573-597(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  9. "Surface-modulated motion switch: capture and release of iron-sulfur protein in the cytochrome bc1 complex."
    Esser L., Gong X., Yang S., Yu L., Yu C.A., Xia D.
    Proc. Natl. Acad. Sci. U.S.A. 103:13045-13050(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS).

Entry informationi

Entry nameiCYB_BOVIN
AccessioniPrimary (citable) accession number: P00157
Secondary accession number(s): Q8SE06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.