Cytochrome P450 2B1 - Rattus norvegicus (Rat)

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P00176 (CP2B1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 118. History...

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

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	drug metabolic process Inferred from direct assay PubMed 9425052. Source: RGD response to calcium ion Inferred from expression pattern PubMed 10454523. Source: RGD response to drug Inferred from expression pattern PubMed 18798224. Source: RGD response to insulin stimulus Inferred from expression pattern PubMed 17015271. Source: RGD response to organic cyclic compound Inferred from expression pattern PubMed 18670162. Source: RGD response to sulfur dioxide Inferred from expression pattern PubMed 17086701. Source: RGD
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell intracellular membrane-bounded organelle Inferred from direct assay PubMed 17015271. Source: RGD
Molecular_function	aromatase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro steroid hydroxylase activity Inferred from direct assay PubMed 7979377. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 491

491

Cytochrome P450 2B1

PRO_0000051678

Sites

Metal binding

436

Iron (heme axial ligand)

Amino acid modifications

Modified residue

128

Phosphoserine; by PKA Ref.8

Natural variations

Natural variant

303

S → G in isozyme PB2.

Natural variant

321 – 322

AE → TV in isozyme PB2.

Natural variant

337

L → P in isozyme PB2.

Natural variant

339

T → S in isozyme PB2.

Natural variant

344

S → T in isozyme PB2.

Experimental info

Sequence conflict

T → S Ref.2

Sequence conflict

T → S AA sequence Ref.5

Sequence conflict

A → P in AAA41046. Ref.2

Sequence conflict

161

Q → E AA sequence Ref.5

Sequence conflict

205

T → R in AAA41046. Ref.2

Sequence conflict

328

I → V in AAA41046. Ref.2

Sequence conflict

357

Q → H in AAA41046. Ref.2

Sequence conflict

392

L → R in AAA41046. Ref.2

Sequence conflict

416

A → V in AAA41046. Ref.2

Sequence conflict

434

R → H in AAA41046. Ref.2

Sequence conflict

473

K → M no nucleotide entry Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P00176 [UniParc].

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

FASTA

491

55,934

        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 M11251 Genomic DNA. Translation: AAA41046.1. J00719 mRNA. Translation: AAA41024.1. M37134 mRNA. Translation: AAC42028.1.
IPI	IPI00949532.
PIR	O4RTPB. A00176. O4RTP2. A21162.
UniGene	Rn.228579.
3D structure databases
ProteinModelPortal	P00176.
SMR	P00176. Positions 28-491.
ModBase	Search...
PTM databases
PhosphoSite	P00176.
Proteomic databases
PaxDb	P00176.
PRIDE	P00176.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:2466. rat.
Organism-specific databases
RGD	2466. Cyp2b1.
Phylogenomic databases
eggNOG	COG2124.
HOGENOM	HOG000036992.
HOVERGEN	HBG015789.
OrthoDB	EOG40K7ZR.
Gene expression databases
ArrayExpress	P00176.
Genevestigator	P00176.
GermOnline	ENSRNOG00000033680. Rattus norvegicus.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. IPR008068. Cyt_P450_E_grp-I_CYP2B-like. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR01685. EP450ICYP2B. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P00176.
ChEMBL	CHEMBL3335.

Entry information

Entry name

CP2B1_RAT

Accession

Primary (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 3, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents