[1]	NUCLEOTIDE SEQUENCE [MRNA]. Kuroda R., Ikenoue T., Honsho M., Tujimoto S., Miroma J., Ito A.; "Charged amino acids at the carboxy-terminal portions determine intracellular locations of two isoforms of cytochrome b5."; Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Heart; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PROTEIN SEQUENCE OF 12-103. PubMed=6840088 [NCBI, ExPASy, EBI, Israel, Japan] Lederer F., Ghrir R., Guiard B., Cortial S., Ito A.; "Two homologous cytochromes b5 in a single cell."; Eur. J. Biochem. 132:95-102(1983).
[4]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). DOI=10.1021/bi961895o; PubMed=8973214 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "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."; Biochemistry 35:16378-16390(1996).
[5]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1021/bi972390g; PubMed=9484218 [NCBI, ExPASy, EBI, Israel, Japan] Rivera M., Seetharaman R., Girdhar D., Wirtz M., Zhang X., Wang X., White S.; "The reduction potential of cytochrome b5 is modulated by its exposed heme edge."; Biochemistry 37:1485-1494(1998).
[6]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 17-102. PubMed=11197480 [NCBI, ExPASy, EBI, Israel, Japan] Wirtz M., Oganesyan V., Zhang X., Studer J., Rivera M.; "Modulation of redox potential in electron transfer proteins: effects of complex formation on the active site microenvironment of cytochrome b5."; Faraday Discuss. 116:221-234(2000).
[7]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-103. DOI=10.1021/bi010636i; PubMed=11583146 [NCBI, ExPASy, EBI, Israel, Japan] Altuve A., Silchenko S., Lee K.-H., Kuczera K., Terzyan S., Zhang X., Benson D.R., Rivera M.; "Probing the differences between rat liver outer mitochondrial membrane cytochrome b5 and microsomal cytochromes b5."; Biochemistry 40:9469-9483(2001).

Comments

FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.
SUBUNIT: Component of a complex composed of cytochrome b5, NADH-cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity).
SUBCELLULAR LOCATION: Mitochondrion outer membrane.
SIMILARITY: Belongs to the cytochrome b5 family.
SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y12517; CAA73117.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC072535; AAH72535.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_085075.1; -.

UniGene

Rn.10249

3D structure databases

PDB

1AWP; X-ray; 2.00 A; A/B=13-103.	[ExPASy / RCSB / EBI]
1B5M; X-ray; 2.70 A; A=19-102.	[ExPASy / RCSB / EBI]
1EUE; X-ray; 1.80 A; A/B=17-102.	[ExPASy / RCSB / EBI]
1ICC; X-ray; 2.00 A; A/B/C/D=17-103.	[ExPASy / RCSB / EBI]
1LJ0; X-ray; 2.00 A; A/B/C/D=12-103.	[ExPASy / RCSB / EBI]
2I89; X-ray; 2.10 A; A/B/C/D=12-103.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AWP; -.
1B5M; -.
1EUE; -.
1ICC; -.
1LJ0; -.
2I89; -.

ModBase

P04166.

Organism-specific databases

RGD

621551; Cyb5b.

Gene expression databases

ArrayExpress

P04166; -.

GermOnline

ENSRNOG00000011142; Rattus norvegicus.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005741;	Cellular component: mitochondrial outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001199; Cyt_B5.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.120.10; Cyt_B5; 1.

Pfam

PF00173; Cyt-b5; 1.
Pfam graphical view of domain structure.

PRINTS

PR00363; CYTOCHROMEB5.

ProDom

PD000612; Cyt_B5; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00191; CYTOCHROME_B5_1; 1.
PS50255; CYTOCHROME_B5_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000011142; Rattus norvegicus. [Contig view]

GeneID

80773; -.

KEGG

rno:80773; -.

Phylogenomic databases

HOVERGEN

P04166; -.

Other

LinkHub

P04166; -.

NextBio

614866; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion outer membrane; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 11`	`11`		`PRO_0000006477`
`CHAIN`	`12 146`	`135`	`Cytochrome b5 type B.`	`PRO_0000006478`
`TRANSMEM`	`119 136`	`18`	`Potential.`
`DOMAIN`	`20 96`	`77`	`Cytochrome b5 heme-binding.`
`METAL`	`55 55`		`Iron (heme axial ligand).`
`METAL`	`79 79`		`Iron (heme axial ligand).`
`CONFLICT`	`12 12`		`N -> D (in Ref. 3; AA sequence).`
`HELIX`	`25 28`	`4`
`STRAND`	`36 41`	`6`
`STRAND`	`44 47`	`4`
`TURN`	`49 54`	`6`
`HELIX`	`60 64`	`5`
`TURN`	`65 67`	`3`
`HELIX`	`71 76`	`6`
`HELIX`	`81 87`	`7`
`TURN`	`88 90`	`3`
`STRAND`	`91 95`	`5`
`HELIX`	`97 99`	`3`

Sequence information

Length: 146 AA [This is the length of the unprocessed precursor]

Molecular weight: 16265 Da [This is the MW of the unprocessed precursor]

CRC64: 1CA90DD3C81C412E [This is a checksum on the sequence]

        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

P04166 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools