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P00157 (CYB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MT-CYB
Synonyms:COB, CYTB, MTCYB
Encoded onMitochondrion
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Cofactor

Binds 2 heme groups non-covalently.

Subunit structure

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).

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein By similarity.

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.

Sequence similarities

Belongs to the cytochrome b family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Cytochrome b
PRO_0000060686

Regions

Transmembrane33 – 5321Helical; Potential
Transmembrane76 – 9823Helical; Potential
Transmembrane115 – 13521Helical; Potential
Transmembrane140 – 15819Helical; Potential
Transmembrane178 – 19821Helical; Potential
Transmembrane229 – 24921Helical; Potential
Transmembrane288 – 30821Helical; Potential
Transmembrane323 – 34321Helical; Potential
Transmembrane346 – 36621Helical; Potential

Sites

Metal binding831Iron 1 (heme b562 axial ligand) Ref.4
Metal binding971Iron 2 (heme b566 axial ligand)
Metal binding1821Iron 1 (heme b562 axial ligand)
Metal binding1961Iron 2 (heme b566 axial ligand)

Natural variations

Natural variant901F → V in strain: 65, 66 and D.

Secondary structure

1 ....................................................... 379
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00157 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 90160B99E031E016

FASTA37942,591
        10         20         30         40         50         60 
MTNIRKSHPL MKIVNNAFID LPAPSNISSW WNFGSLLGIC LILQILTGLF LAMHYTSDTT 

        70         80         90        100        110        120 
TAFSSVTHIC RDVNYGWIIR YMHANGASMF FICLYMHVGR GLYYGSYTFL ETWNIGVILL 

       130        140        150        160        170        180 
LTVMATAFMG YVLPWGQMSF WGATVITNLL SAIPYIGTNL VEWIWGGFSV DKATLTRFFA 

       190        200        210        220        230        240 
FHFILPFIIM AIAMVHLLFL HETGSNNPTG ISSDVDKIPF HPYYTIKDIL GALLLILALM 

       250        260        270        280        290        300 
LLVLFAPDLL GDPDNYTPAN PLNTPPHIKP EWYFLFAYAI LRSIPNKLGG VLALAFSILI 

       310        320        330        340        350        360 
LALIPLLHTS KQRSMMFRPL SQCLFWALVA DLLTLTWIGG QPVEHPYITI GQLASVLYFL 

       370 
LILVLMPTAG TIENKLLKW

« Hide

References

[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].
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00703522.
PIRCBBO. A00152.
RefSeqYP_209217.1. NC_006853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP00157.
SMRP00157. Positions 1-379.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-350N.
IntActP00157. 2 interactions.

Protein family/group databases

TCDB3.D.3.2.1. proton-translocating quinol:cytochrome c reductase (QCR) superfamily.

Proteomic databases

PRIDEP00157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000060567; ENSBTAP00000053148; ENSBTAG00000043550.
GeneID3283889.
KEGGbta:3283889.

Organism-specific databases

CTD4519.

Phylogenomic databases

eggNOGCOG1290.
HOGENOMHOG000255206.
HOVERGENHBG017694.
InParanoidP00157.
KOK00412.
OrthoDBEOG4Q84XW.
ProtClustDBMTH00100.

Family and domain databases

InterProIPR016175. Cyt_b/b6.
IPR005798. Cyt_b/b6_C.
IPR005797. Cyt_b/b6_N.
IPR016174. Di-haem_cyt_TM.
[Graphical view]
PANTHERPTHR19271. PTHR19271. 1 hit.
PfamPF00032. Cytochrom_B_C. 1 hit.
PF13631. Cytochrom_B_N_2. 1 hit.
[Graphical view]
SUPFAMSSF81648. Cytochrome_b/b6_C. 1 hit.
SSF81342. Transmembr_di-haem_cytochrome. 1 hit.
PROSITEPS51003. CYTB_CTER. 1 hit.
PS51002. CYTB_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00157.
NextBio20810196.

Entry information

Entry nameCYB_BOVIN
AccessionPrimary (citable) accession number: P00157
Secondary accession number(s): Q8SE06
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 1, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents