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Protein

Cytochrome P450 2B1

Gene

Cyp2b1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

hemeBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi436 – 4361Iron (heme axial ligand)

GO - Molecular functioni

  1. arachidonic acid epoxygenase activity Source: GO_Central
  2. aromatase activity Source: UniProtKB-EC
  3. heme binding Source: GO_Central
  4. iron ion binding Source: InterPro
  5. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Source: GO_Central
  6. oxygen binding Source: GO_Central
  7. steroid hydroxylase activity Source: RGD

GO - Biological processi

  1. drug metabolic process Source: RGD
  2. epoxygenase P450 pathway Source: GO_Central
  3. exogenous drug catabolic process Source: GO_Central
  4. oxidation-reduction process Source: GO_Central
  5. response to calcium ion Source: RGD
  6. response to drug Source: RGD
  7. response to insulin Source: RGD
  8. response to metal ion Source: RGD
  9. response to organic cyclic compound Source: RGD
  10. response to sulfur dioxide Source: RGD
  11. xenobiotic metabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:Cyp2b1
Synonyms:Cyp2b-1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2466. Cyp2b1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. intracellular membrane-bounded organelle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 491491Cytochrome P450 2B1PRO_0000051678Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281Phosphoserine; by PKA1 Publication

Post-translational modificationi

Phosphorylation is accompanied by a decrease in enzyme activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP00176.
PRIDEiP00176.

PTM databases

PhosphoSiteiP00176.

Expressioni

Inductioni

By phenobarbital.

Gene expression databases

GenevestigatoriP00176.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliP00176.
SMRiP00176. Positions 28-491.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000036992.
HOVERGENiHBG015789.
InParanoidiP00176.
PhylomeDBiP00176.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008068. Cyt_P450_E_grp-I_CYP2B-like.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR01685. EP450ICYP2B.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPTILLLLA LLVGFLLLLV RGHPKSRGNF PPGPRPLPLL GNLLQLDRGG
60 70 80 90 100
LLNSFMQLRE KYGDVFTVHL GPRPVVMLCG TDTIKEALVG QAEDFSGRGT
110 120 130 140 150
IAVIEPIFKE YGVIFANGER WKALRRFSLA TMRDFGMGKR SVEERIQEEA
160 170 180 190 200
QCLVEELRKS QGAPLDPTFL FQCITANIIC SIVFGERFDY TDRQFLRLLE
210 220 230 240 250
LFYRTFSLLS SFSSQVFEFF SGFLKYFPGA HRQISKNLQE ILDYIGHIVE
260 270 280 290 300
KHRATLDPSA PRDFIDTYLL RMEKEKSNHH TEFHHENLMI SLLSLFFAGT
310 320 330 340 350
ETSSTTLRYG FLLMLKYPHV AEKVQKEIDQ VIGSHRLPTL DDRSKMPYTD
360 370 380 390 400
AVIHEIQRFS DLVPIGVPHR VTKDTMFRGY LLPKNTEVYP ILSSALHDPQ
410 420 430 440 450
YFDHPDSFNP EHFLDANGAL KKSEAFMPFS TGKRICLGEG IARNELFLFF
460 470 480 490
TTILQNFSVS SHLAPKDIDL TPKESGIGKI PPTYQICFSA R
Length:491
Mass (Da):55,934
Last modified:July 21, 1986 - v1
Checksum:i74615501AD5497DD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41T → S (PubMed:2989270).Curated
Sequence conflicti4 – 41T → S AA sequence (PubMed:2539047).Curated
Sequence conflicti92 – 921A → P in AAA41046 (PubMed:2989270).Curated
Sequence conflicti161 – 1611Q → E AA sequence (PubMed:2539047).Curated
Sequence conflicti205 – 2051T → R in AAA41046 (PubMed:2989270).Curated
Sequence conflicti328 – 3281I → V in AAA41046 (PubMed:2989270).Curated
Sequence conflicti357 – 3571Q → H in AAA41046 (PubMed:2989270).Curated
Sequence conflicti392 – 3921L → R in AAA41046 (PubMed:2989270).Curated
Sequence conflicti416 – 4161A → V in AAA41046 (PubMed:2989270).Curated
Sequence conflicti434 – 4341R → H in AAA41046 (PubMed:2989270).Curated
Sequence conflicti473 – 4731K → M no nucleotide entry (PubMed:6306654).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031S → G in isozyme PB2.
Natural varianti321 – 3222AE → TV in isozyme PB2.
Natural varianti337 – 3371L → P in isozyme PB2.
Natural varianti339 – 3391T → S in isozyme PB2.
Natural varianti344 – 3441S → T in isozyme PB2.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00320
, L00313, L00314, L00315, L00316, L00317, L00318, L00319, M11251 Genomic DNA. Translation: AAA41046.1.
J00719 mRNA. Translation: AAA41024.1.
M37134 mRNA. Translation: AAC42028.1.
PIRiA00176. O4RTPB.
A21162. O4RTP2.
UniGeneiRn.228579.

Genome annotation databases

UCSCiRGD:2466. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00320
, L00313, L00314, L00315, L00316, L00317, L00318, L00319, M11251 Genomic DNA. Translation: AAA41046.1.
J00719 mRNA. Translation: AAA41024.1.
M37134 mRNA. Translation: AAC42028.1.
PIRiA00176. O4RTPB.
A21162. O4RTP2.
UniGeneiRn.228579.

3D structure databases

ProteinModelPortaliP00176.
SMRiP00176. Positions 28-491.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP00176.
ChEMBLiCHEMBL3335.
DrugBankiDB08834. Tauroursodeoxycholic acid.

PTM databases

PhosphoSiteiP00176.

Proteomic databases

PaxDbiP00176.
PRIDEiP00176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2466. rat.

Organism-specific databases

RGDi2466. Cyp2b1.

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000036992.
HOVERGENiHBG015789.
InParanoidiP00176.
PhylomeDBiP00176.

Gene expression databases

GenevestigatoriP00176.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008068. Cyt_P450_E_grp-I_CYP2B-like.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR01685. EP450ICYP2B.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(1982) [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(1984) [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(1981) [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(1981)
    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(1988) [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(1978) [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(1993) [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(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-128.

Entry informationi

Entry nameiCP2B1_RAT
AccessioniPrimary (citable) accession number: P00176
Secondary accession number(s): Q64584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 4, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.