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Reviewed, UniProtKB/Swiss-Prot P00171 (CYB5_BOVIN)

Last modified June 16, 2009. Version 100. Feed 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

Names and origin

Protein namesRecommended name:
    Cytochrome b5
Gene names
Name: CYB5A
Synonyms: CYB5
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length134 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side. Microsome membrane; Single-pass membrane protein; Cytoplasmic side.

Sequence similarities

Belongs to the cytochrome b5 family.

Contains 1 cytochrome b5 heme-binding domain.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   DomainTransmembrane
   LigandHeme
Iron
Metal-binding
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

microsome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionheme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5 Ref.6
Chain2 – 134133Cytochrome b5
PRO_0000166008

Regions

Transmembrane109 – 13123 Potential
Domain9 – 8577Cytochrome b5 heme-binding

Sites

Metal binding441Iron (heme axial ligand) Ref.12
Metal binding681Iron (heme axial ligand) Ref.12

Amino acid modifications

Modified residue21N-acetylalanine Ref.4 Ref.6
Modified residue191N6-acetyllysine By similarity

Experimental info

Sequence conflict2 – 54AEES → ZSZZBA AA sequence Ref.5
Sequence conflict16 – 183EIQ → QIE AA sequence Ref.7
Sequence conflict181Q → E AA sequence Ref.8
Sequence conflict621N → D AA sequence Ref.7
Sequence conflict621N → D AA sequence Ref.8
Sequence conflict981S → SES Ref.2
Sequence conflict1341N → D AA sequence Ref.5

Secondary structure

................... 134
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00171-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7B7B605158D97525

FASTA13415,329
        10         20         30         40         50         60 
MAEESSKAVK YYTLEEIQKH NNSKSTWLIL HYKVYDLTKF LEEHPGGEEV LREQAGGDAT 

        70         80         90        100        110        120 
ENFEDVGHST DARELSKTFI IGELHPDDRS KITKPSESII TTIDSNPSWW TNWLIPAISA 

       130 
LFVALIYHLY TSEN 

« Hide

References

« Hide 'large scale' references
[1]"The complete nucleotide sequence of bovine liver cytochrome b5 mRNA."
Cristiano R.J., Steggles A.W.
Nucleic Acids Res. 17:799-799(1989) [PubMed: 2915932] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The isolation and characterization of the bovine cytochrome b5 gene, and a transcribed pseudogene."
Cristiano R.J., Giordano S.J., Steggles A.W.
Genomics 17:348-354(1993) [PubMed: 8406485] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal liver.
[4]"Amino acid sequences of cytochrome b5 from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b5."
Abe K., Kimura S., Kizawa R., Anan F.K., Sugita Y.
J. Biochem. 97:1659-1668(1985) [PubMed: 4030743] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-98.
Tissue: Erythrocyte.
[5]"Cytochrome b5 from microsomal membranes of equine, bovine, and porcine livers. Isolation and properties of preparations containing the membranous segment."
Ozols J.
Biochemistry 13:426-434(1974) [PubMed: 4810060] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11 AND 131-134.
[6]"Structure of cytochrome b5 and its topology in the microsomal membrane."
Ozols J.
Biochim. Biophys. Acta 997:121-130(1989) [PubMed: 2752049] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-6 AND 15-18.
[7]"Correction of the amino acid sequence of calf liver microsomal cytochrome b5."
Ozols J., Strittmatter P.
J. Biol. Chem. 244:6617-6618(1969) [PubMed: 5391285] [Abstract]
Cited for: PROTEIN SEQUENCE OF 6-98.
[8]"Comparative study of the primary structures of cytochrome b5 from four species."
Tsugita A., Kobayashi M., Tani S., Kyo S., Rashid M.A., Yoshida Y., Kajihara T., Hagihara B.
Proc. Natl. Acad. Sci. U.S.A. 67:442-447(1970) [PubMed: 5272324] [Abstract]
Cited for: PROTEIN SEQUENCE OF 6-96.
[9]"The primary structure of the nonpolar segment of bovine cytochrome b5."
Fleming P.J., Dailey H.A., Corcoran D., Strittmatter P.
J. Biol. Chem. 253:5369-5372(1978) [PubMed: 670203] [Abstract]
Cited for: PROTEIN SEQUENCE OF 92-134.
[10]"The structure of cytochrome b-5 at 2.0-A resolution."
Mathews F.S., Argos P., Levine M.
Cold Spring Harb. Symp. Quant. Biol. 37:387-395(1971)
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OXIDIZED FORM.
[11]"The structure of ferrocytochrome b5 at 2.8-A resolution."
Argos P., Mathews F.S.
J. Biol. Chem. 250:747-751(1975) [PubMed: 1167544] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF REDUCED FORM.
[12]"Refinement and structural analysis of bovine cytochrome b5 at 1.5-A resolution."
Durley R.C.E., Mathews F.S.
Acta Crystallogr. D 52:65-76(1996) [PubMed: 15299727] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[13]"Crystal structure of recombinant trypsin-solubilized fragment of cytochrome b5 and the structural comparison with Val61His mutant."
Wu J., Gan J.-H., Xia Z.-X., Wang Y.-H., Wang W.-H., Xue L.-L., Xie Y., Huang Z.-X.
Proteins 40:249-257(2000) [PubMed: 10842340] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 8-89, MUTAGENESIS.
[14]"Structures of V45E and V45Y mutants and structure comparison of a variety of cytochrome b5 mutants."
Gan J.-H., Wu J., Wang Z.-Q., Wang Y.-H., Huang Z.-X., Xia Z.-X.
Acta Crystallogr. D 58:1298-1306(2002) [PubMed: 12136141] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 8-89, MUTAGENESIS.
[15]"X-ray crystallography, CD and kinetic studies revealed the essence of the abnormal behaviors of the cytochrome b5 Phe35->Tyr mutant."
Yao P., Wu J., Wang Y.-H., Sun B.-Y., Xia Z.-X., Huang Z.-X.
Eur. J. Biochem. 269:4287-4296(2002) [PubMed: 12199707] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 8-89, CIRCULAR DICHROISM ANALYSIS, MUTAGENESIS.
[16]"The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods."
Muskett F.W., Kelly G.P., Whitford D.
J. Mol. Biol. 258:172-189(1996) [PubMed: 8613986] [Abstract]
Cited for: STRUCTURE BY NMR.
[17]"Solution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with cytochrome c."
Wu Y., Wang Y., Qian C., Lu J., Li E., Wang W., Lu J., Xie Y., Wang J., Zhu D., Huang Z., Tang W.
Eur. J. Biochem. 268:1620-1630(2001) [PubMed: 11248680] [Abstract]
Cited for: STRUCTURE BY NMR OF 8-89, MUTAGENESIS.
[18]"Effects of charged amino-acid mutation on the solution structure of cytochrome b5 and binding between cytochrome b5 and cytochrome c."
Qian C., Yao Y., Ye K., Wang J., Tang W., Wang Y., Wang W., Lu J., Xie Y., Huang Z.
Protein Sci. 10:2451-2459(2001) [PubMed: 11714912] [Abstract]
Cited for: STRUCTURE BY NMR OF 8-89, MUTAGENESIS.
[19]"The solution structure of the oxidized bovine microsomal cytochrome b5 mutant V61H."
Cao C., Zhang Q., Xue L.-L., Ma J., Wang Y.-H., Wu H., Huang Z.-X.
Biochem. Biophys. Res. Commun. 307:600-609(2003) [PubMed: 12893266] [Abstract]
Cited for: STRUCTURE BY NMR OF 8-89, MUTAGENESIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

X13617 mRNA. Translation: CAA31949.1.
M63328, M63326, M63327 Genomic DNA. Translation: AAC14455.1. Sequence problems.
L22966 Genomic DNA. No translation available.
BC108113 mRNA. Translation: AAI08114.1.
IPIIPI00714055.
PIRCBBO5. A47215.
RefSeqNP_776458.1.
UniGeneBt.64615

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CYOX-ray1.50A6-98[»]
1EHBX-ray1.90A8-89[»]
1ES1X-ray2.10A8-89[»]
1F03NMR-A8-89[»]
1F04NMR-A8-89[»]
1HKONMR-A2-105[»]
1I5UNMR-A8-89[»]
1J0QNMR-A8-89[»]
1LQXX-ray1.80A8-89[»]
1LR6X-ray1.90A8-89[»]
1M20X-ray1.80A8-89[»]
1M2IX-ray1.80A8-89[»]
1M2MX-ray1.80A8-89[»]
1M59X-ray1.90A8-89[»]
1NX7NMR-A8-88[»]
1SH4NMR-A8-88[»]
1U9MX-ray2.00A/B/C/D/E/F8-88[»]
1U9UX-ray1.86A8-88[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000012012. Bos taurus. [Contig view]
GeneID281110.
KEGGbta:281110.

Phylogenomic databases

HOVERGENP00171.
OMAP00171. QKHNHSK.

Family and domain databases

InterProIPR001199. Cyt_B5.
IPR018506. Cyt_B5_heme-BS.
[Graphical view]
Gene3DG3DSA:3.10.120.10. Cyt_B5. 1 hit.
PfamPF00173. Cyt-b5. 1 hit.
[Graphical view]
PRINTSPR00363. CYTOCHROMEB5.
ProDomPD000612. Cyt_B5. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00191. CYTOCHROME_B5_1. 1 hit.
PS50255. CYTOCHROME_B5_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYB5_BOVIN
AccessionPrimary (citable) accession number: P00171
Secondary accession number(s): Q27947, Q28837, Q32PH5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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