Cytochrome b5 type B precursor - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P04166 (CYB5B_RAT)

Last modified June 16, 2009. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
Cytochrome b5 type B
Alternative name(s):
Cytochrome b5 outer mitochondrial membrane isoform

Gene names

Name:	Cyb5b
Synonyms:	Cyb5m, Omb5

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Hide | Top

Protein attributes

Sequence length	146 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.
Subunit structure	Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2 By similarity.
Subcellular location	Mitochondrion outer membrane.
Sequence similarities	Belongs to the cytochrome b5 family. Contains 1 cytochrome b5 heme-binding domain.

Hide | Top

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Ligand	Heme Iron Metal-binding
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from direct assay. Source: RGD mitochondrial outer membrane Inferred from direct assay. Source: RGD
Molecular function	electron transporter, transferring electrons within CoQH2-cytochrome c reductase complex activity Traceable author statement. Source: RGD enzyme activator activity Inferred from direct assay. Source: RGD heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 11

Ref.3

PRO_0000006477

Chain

12 – 146

135

Cytochrome b5 type B

PRO_0000006478

Regions

Transmembrane

119 – 136

Potential

Domain

20 – 96

Cytochrome b5 heme-binding

Sites

Metal binding

Iron (heme axial ligand)

Metal binding

Iron (heme axial ligand)

Experimental info

Sequence conflict

N → D AA sequence Ref.3

Secondary structure

146

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P04166-1 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 1CA90DD3C81C412E
Show »

FASTA

146

16,265

        10         20         30         40         50         60 
MATPEASGSG RNGQGSDPAV TYYRLEEVAK RNTAEETWMV IHGRVYDITR FLSEHPGGEE 

        70         80         90        100        110        120 
VLLEQAGADA TESFEDVGHS PDAREMLKQY YIGDVHPNDL KPKDGDKDPS KNNSCQSSWA 

       130        140 
YWIVPIVGAI LIGFLYRHFW ADSKSS

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Charged amino acids at the carboxy-terminal portions determine intracellular locations of two isoforms of cytochrome b5." Kuroda R., Ikenoue T., Honsho M., Tujimoto S., Miroma J., Ito A. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart.
[3]	"Two homologous cytochromes b5 in a single cell." Lederer F., Ghrir R., Guiard B., Cortial S., Ito A. Eur. J. Biochem. 132:95-102(1983) [PubMed: 6840088] [Abstract] Cited for: PROTEIN SEQUENCE OF 12-103.
[4]	"13C NMR spectroscopic and X-ray crystallographic study of the role played by mitochondrial cytochrome b5 heme propionates in the electrostatic binding to cytochrome c." Rodriguez-Maranon M.J., Qiu F., Stark R.E., White S.P., Zhang X., Foundling S.I., Rodriguez V., Schilling C.L. III, Bunce R.A., Rivera M. Biochemistry 35:16378-16390(1996) [PubMed: 8973214] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[5]	"The reduction potential of cytochrome b5 is modulated by its exposed heme edge." Rivera M., Seetharaman R., Girdhar D., Wirtz M., Zhang X., Wang X., White S. Biochemistry 37:1485-1494(1998) [PubMed: 9484218] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[6]	"Modulation of redox potential in electron transfer proteins: effects of complex formation on the active site microenvironment of cytochrome b5." Wirtz M., Oganesyan V., Zhang X., Studer J., Rivera M. Faraday Discuss. 116:221-234(2000) [PubMed: 11197480] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 17-102.
[7]	"Probing the differences between rat liver outer mitochondrial membrane cytochrome b5 and microsomal cytochromes b5." Altuve A., Silchenko S., Lee K.-H., Kuczera K., Terzyan S., Zhang X., Benson D.R., Rivera M. Biochemistry 40:9469-9483(2001) [PubMed: 11583146] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-103.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

Y12517 mRNA. Translation: CAA73117.1.
BC072535 mRNA. Translation: AAH72535.1.

IPI

IPI00193233.

RefSeq

NP_085075.1.

UniGene

Rn.10249

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AWP	X-ray	2.00	A/B	13-103	[»]
1B5M	X-ray	2.70	A	19-102	[»]
1EUE	X-ray	1.80	A/B	17-102	[»]
1ICC	X-ray	2.00	A/B/C/D	17-103	[»]
1LJ0	X-ray	2.00	A/B/C/D	12-103	[»]
2I89	X-ray	2.10	A/B/C/D	12-103	[»]

ModBase

Search...

Proteomic databases

PRIDE

P04166.

Genome annotation databases

Ensembl

ENSRNOG00000011142. Rattus norvegicus. [Contig view]

GeneID

80773.

KEGG

rno:80773.

Organism-specific databases

RGD

621551. Cyb5b.

Phylogenomic databases

HOVERGEN

P04166.

Gene expression databases

ArrayExpress

P04166.

GermOnline

ENSRNOG00000011142. Rattus norvegicus.

Family and domain databases

InterPro

IPR001199. Cyt_B5.
IPR018506. Cyt_B5_heme-BS.
[Graphical view]

Gene3D

G3DSA:3.10.120.10. Cyt_B5. 1 hit.

Pfam

PF00173. Cyt-b5. 1 hit.
[Graphical view]

PRINTS

PR00363. CYTOCHROMEB5.

ProDom

PD000612. Cyt_B5. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

614866.

Hide | Top

Entry information

Entry name

CYB5B_RAT

Accession

Primary (citable) accession number: P04166
Secondary accession number(s): Q9QWG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	January 11, 2001
Last modified:	June 16, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families