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P00176 (CP2B1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cytochrome P450 2B1

EC=1.14.14.1
Alternative name(s):
CYPIIB1
Cytochrome P450-B
Short name=Cytochrome P450b
Cytochrome P450-LM2
Cytochrome P450-PB1
Cytochrome P450-PB2
Gene names
Name:Cyp2b1
Synonyms:Cyp2b-1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

Catalytic activity

RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.

Cofactor

Heme group By similarity.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.

Induction

By phenobarbital.

Post-translational modification

Phosphorylation is accompanied by a decrease in enzyme activity.

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Cytochrome P450 2B1
PRO_0000051678

Sites

Metal binding4361Iron (heme axial ligand)

Amino acid modifications

Modified residue1281Phosphoserine; by PKA Ref.8

Natural variations

Natural variant3031S → G in isozyme PB2.
Natural variant321 – 3222AE → TV in isozyme PB2.
Natural variant3371L → P in isozyme PB2.
Natural variant3391T → S in isozyme PB2.
Natural variant3441S → T in isozyme PB2.

Experimental info

Sequence conflict41T → S Ref.2
Sequence conflict41T → S AA sequence Ref.5
Sequence conflict921A → P in AAA41046. Ref.2
Sequence conflict1611Q → E AA sequence Ref.5
Sequence conflict2051T → R in AAA41046. Ref.2
Sequence conflict3281I → V in AAA41046. Ref.2
Sequence conflict3571Q → H in AAA41046. Ref.2
Sequence conflict3921L → R in AAA41046. Ref.2
Sequence conflict4161A → V in AAA41046. Ref.2
Sequence conflict4341R → H in AAA41046. Ref.2
Sequence conflict4731K → M no nucleotide entry Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00176 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 74615501AD5497DD

FASTA49155,934
        10         20         30         40         50         60 
MEPTILLLLA LLVGFLLLLV RGHPKSRGNF PPGPRPLPLL GNLLQLDRGG LLNSFMQLRE 

        70         80         90        100        110        120 
KYGDVFTVHL GPRPVVMLCG TDTIKEALVG QAEDFSGRGT IAVIEPIFKE YGVIFANGER 

       130        140        150        160        170        180 
WKALRRFSLA TMRDFGMGKR SVEERIQEEA QCLVEELRKS QGAPLDPTFL FQCITANIIC 

       190        200        210        220        230        240 
SIVFGERFDY TDRQFLRLLE LFYRTFSLLS SFSSQVFEFF SGFLKYFPGA HRQISKNLQE 

       250        260        270        280        290        300 
ILDYIGHIVE KHRATLDPSA PRDFIDTYLL RMEKEKSNHH TEFHHENLMI SLLSLFFAGT 

       310        320        330        340        350        360 
ETSSTTLRYG FLLMLKYPHV AEKVQKEIDQ VIGSHRLPTL DDRSKMPYTD AVIHEIQRFS 

       370        380        390        400        410        420 
DLVPIGVPHR VTKDTMFRGY LLPKNTEVYP ILSSALHDPQ YFDHPDSFNP EHFLDANGAL 

       430        440        450        460        470        480 
KKSEAFMPFS TGKRICLGEG IARNELFLFF TTILQNFSVS SHLAPKDIDL TPKESGIGKI 

       490 
PPTYQICFSA R 

« Hide

References

[1]"Gene structure of a phenobarbital-inducible cytochrome P-450 in rat liver."
Mizukami Y., Sogawa K., Suwa Y., Muramatsu M., Fujii-Kuriyama Y.
Proc. Natl. Acad. Sci. U.S.A. 80:3958-3962(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Gene structure of a major form of phenobarbital-inducible cytochrome P-450 in rat liver."
Suwa Y., Mizukami Y., Sogawa K., Fujii-Kuriyama Y.
J. Biol. Chem. 260:7980-7984(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Primary structure of a cytochrome P-450: coding nucleotide sequence of phenobarbital-inducible cytochrome P-450 cDNA from rat liver."
Fujii-Kuriyama Y., Mizukami Y., Kawajiri K., Sogawa K., Muramatsu M.
Proc. Natl. Acad. Sci. U.S.A. 79:2793-2797(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-491 (ISOZYMES PB1 AND PB2).
[4]Fujii-Kuriyama Y., Mizukami Y., Kawajiri K., Sogawa K., Muramatsu M.
Proc. Natl. Acad. Sci. U.S.A. 79:5443-5443(1982)
Cited for: SEQUENCE REVISION TO 166; 292 AND 378 (ISOZYMES PB1 AND PB2).
[5]"Antibodies targeted against hypervariable and constant regions of cytochromes P450IIB1 and P450IIB2."
Oesch F., Waxman D.J., Morrissey J.J., Honscha W., Kissel W., Friedberg T.
Arch. Biochem. Biophys. 270:23-32(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-18; 146-165; 329-379 AND 401-423.
[6]"Amino acid compositions and partial amino acid sequences of three highly purified forms of liver microsomal cytochrome P-450 from rats treated with polychlorinated biphenyls, phenobarbital, or 3-methylcholanthrene."
Botelho L.H., Ryan D.E., Levin W.
J. Biol. Chem. 254:5635-5640(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-22.
[7]"Identification of active-site peptides from 3H-labeled 2-ethynylnaphthalene-inactivated P450 2B1 and 2B4 using amino acid sequencing and mass spectrometry."
Roberts E.S., Hopkins N.E., Zaluzec E.J., Gage D.A., Alworth W.L., Hollenberg P.F.
Biochemistry 33:3766-3771(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 273-283 AND 290-301.
[8]"Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450."
Pyerin W., Taniguchi H.
EMBO J. 8:3003-3010(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-128.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00320 expand/collapse EMBL AC list , L00313, L00314, L00315, L00316, L00317, L00318, L00319, M11251 Genomic DNA. Translation: AAA41046.1.
J00719 mRNA. Translation: AAA41024.1.
M37134 mRNA. Translation: AAC42028.1.
PIRO4RTPB. A00176.
O4RTP2. A21162.
UniGeneRn.228579.

3D structure databases

ProteinModelPortalP00176.
SMRP00176. Positions 28-491.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP00176.
ChEMBLCHEMBL3335.

PTM databases

PhosphoSiteP00176.

Proteomic databases

PaxDbP00176.
PRIDEP00176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2466. rat.

Organism-specific databases

RGD2466. Cyp2b1.

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000036992.
HOVERGENHBG015789.
PhylomeDBP00176.

Gene expression databases

GenevestigatorP00176.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008068. Cyt_P450_E_grp-I_CYP2B-like.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR01685. EP450ICYP2B.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCP2B1_RAT
AccessionPrimary (citable) accession number: P00176
Secondary accession number(s): Q64584
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families