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P00178 (CP2B4_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome P450 2B4

EC=1.14.14.1
Alternative name(s):
CYPIIB4
Cytochrome P450 isozyme 2
Short name=Cytochrome P450 LM2
Cytochrome P450 type B0
Cytochrome P450 type B1
Gene names
Name:CYP2B4
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

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. In the epoxidation of arachidonic acid it has a unique preference for the 5,6-olefin.

Catalytic activity

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

Cofactor

Heme group.

Subcellular location

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

Induction

By phenobarbital.

Polymorphism

Types B0 and B1 are probably allelic variants.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Cytochrome P450 2B4
PRO_0000051681

Sites

Metal binding4361Iron (heme axial ligand)

Amino acid modifications

Modified residue1281Phosphoserine; by PKA By similarity

Natural variations

Natural variant391V → I in B1.
Natural variant1741I → V in B1.
Natural variant2901L → I in B1.
Natural variant3141M → L in B1.
Natural variant4201L → M in B1.

Experimental info

Mutagenesis4361C → S: Conversion into an NADPH oxidase with negligible monooxygenase activity. Ref.6
Sequence conflict911Q → E AA sequence Ref.3
Sequence conflict95 – 962FS → SF AA sequence Ref.3
Sequence conflict99 – 1002Missing AA sequence Ref.3
Sequence conflict135 – 1362FG → GY AA sequence Ref.3
Sequence conflict1931P → K AA sequence Ref.3
Sequence conflict2211P → S AA sequence Ref.3
Sequence conflict3031T → A AA sequence Ref.3
Sequence conflict461 – 4655SPVPP → GNLSL AA sequence Ref.3

Secondary structure

.............................................................................. 491
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00178 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 0DB943C6CDCF690B

FASTA49155,713
        10         20         30         40         50         60 
MEFSLLLLLA FLAGLLLLLF RGHPKAHGRL PPGPSPLPVL GNLLQMDRKG LLRSFLRLRE 

        70         80         90        100        110        120 
KYGDVFTVYL GSRPVVVLCG TDAIREALVD QAEAFSGRGK IAVVDPIFQG YGVIFANGER 

       130        140        150        160        170        180 
WRALRRFSLA TMRDFGMGKR SVEERIQEEA RCLVEELRKS KGALLDNTLL FHSITSNIIC 

       190        200        210        220        230        240 
SIVFGKRFDY KDPVFLRLLD LFFQSFSLIS SFSSQVFELF PGFLKHFPGT HRQIYRNLQE 

       250        260        270        280        290        300 
INTFIGQSVE KHRATLDPSN PRDFIDVYLL RMEKDKSDPS SEFHHQNLIL TVLSLFFAGT 

       310        320        330        340        350        360 
ETTSTTLRYG FLLMLKYPHV TERVQKEIEQ VIGSHRPPAL DDRAKMPYTD AVIHEIQRLG 

       370        380        390        400        410        420 
DLIPFGVPHT VTKDTQFRGY VIPKNTEVFP VLSSALHDPR YFETPNTFNP GHFLDANGAL 

       430        440        450        460        470        480 
KRNEGFMPFS LGKRICLGEG IARTELFLFF TTILQNFSIA SPVPPEDIDL TPRESGVGNV 

       490 
PPSYQIRFLA R 

« Hide

References

[1]"Primary structures of multiple forms of cytochrome P-450 isozyme 2 derived from rabbit pulmonary and hepatic cDNAs."
Gasser R., Negishi M., Philpot R.M.
Mol. Pharmacol. 33:22-30(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes."
Tarr G.E., Black S.D., Fujita V.S., Coon M.J.
Proc. Natl. Acad. Sci. U.S.A. 80:6552-6556(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[3]"The complete amino acid sequence of rabbit phenobarbital-induced liver microsomal cytochrome P-450."
Heinemann F.S., Ozols J.
J. Biol. Chem. 258:4195-4201(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[4]"Cytochrome P-450 isozymes 2 and 5 in rabbit lung and liver. Comparisons of structure and inducibility."
Parandoosh Z., Fujita V.S., Coon M.J., Philpot R.M.
Drug Metab. Dispos. 15:59-67(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-24.
[5]"Microheterogeneity in the major phenobarbital-inducible forms of rabbit liver microsomal cytochrome P-450 as revealed by nucleotide sequencing of cloned cDNAs."
Komori M., Imai Y., Tsunasawa S., Sato R.
Biochemistry 27:73-80(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 301-491 (B1).
[6]"Replacement of active-site cysteine-436 by serine converts cytochrome P450 2B4 into an NADPH oxidase with negligible monooxygenase activity."
Vatsis K.P., Peng H.-M., Coon M.J.
J. Inorg. Biochem. 91:542-553(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-436.
[7]"An open conformation of mammalian cytochrome P450 2B4 at 1.6-A resolution."
Scott E.E., He Y.A., Wester M.R., White M.A., Chin C.C., Halpert J.R., Johnson E.F., Stout C.D.
Proc. Natl. Acad. Sci. U.S.A. 100:13196-13201(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M20856 mRNA. Translation: AAA65840.1.
M20857 mRNA. Translation: AAA31224.1.
PIRO4RBPC. A00179.
S31277.
RefSeqNP_001164602.1. NM_001171131.1.
UniGeneOcu.1858.
Ocu.7479.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PO5X-ray1.60A25-491[»]
1SUOX-ray1.90A25-491[»]
2BDMX-ray2.30A25-491[»]
2Q6NX-ray3.20A/B/C/D/E/F/G25-491[»]
3G5NX-ray2.50A/B/C/D25-491[»]
3G93X-ray3.20A/B/C/D25-491[»]
3KW4X-ray2.67A25-491[»]
3ME6X-ray3.10A/B/C/D25-491[»]
3MVRX-ray1.76A/B25-491[»]
3R1AX-ray3.50A/B/C/D/E/F/G/H25-491[»]
3R1BX-ray3.00A/B/C/D25-491[»]
3TK3X-ray2.80A/B/C/D25-491[»]
3TMZX-ray2.25A25-491[»]
3UASX-ray2.94A25-491[»]
4H1NX-ray2.99A25-491[»]
4JLTX-ray2.14A25-491[»]
ProteinModelPortalP00178.
SMRP00178. Positions 28-491.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1743542.
DrugBankDB04794. Bifonazole.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100328948.

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000036992.
HOVERGENHBG015789.

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...

Other

EvolutionaryTraceP00178.

Entry information

Entry nameCP2B4_RABIT
AccessionPrimary (citable) accession number: P00178
Secondary accession number(s): P00177
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 127 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references