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P00186 (CP1A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. 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 1A2

EC=1.14.14.1
Alternative name(s):
CYPIA2
Cytochrome P450-P2
Cytochrome P450-P3
Gene names
Name:Cyp1a2
Synonyms:Cyp1a-2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Most active in catalyzing 2-hydroxylation By similarity.

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 3-methylcholanthrene (3MC).

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityPolymorphism
   LigandHeme
Iron
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processalkaloid metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular aromatic compound metabolic process

Inferred from mutant phenotype PubMed 9240455. Source: MGI

cellular respiration

Inferred from mutant phenotype PubMed 7761462. Source: MGI

cellular response to cadmium ion

Inferred from direct assay PubMed 16183037. Source: MGI

dibenzo-p-dioxin metabolic process

Inferred from mutant phenotype PubMed 16636061PubMed 9240455. Source: MGI

drug metabolic process

Inferred from mutant phenotype PubMed 8643688. Source: MGI

exogenous drug catabolic process

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide biosynthetic process

Inferred from mutant phenotype PubMed 14980704. Source: MGI

lung development

Inferred from mutant phenotype PubMed 7761462. Source: MGI

monocarboxylic acid metabolic process

Inferred from electronic annotation. Source: Ensembl

monoterpenoid metabolic process

Inferred from electronic annotation. Source: Ensembl

oxidative deethylation

Inferred from electronic annotation. Source: Ensembl

oxidative demethylation

Inferred from electronic annotation. Source: Ensembl

porphyrin-containing compound metabolic process

Inferred from mutant phenotype PubMed 11274970PubMed 9461503. Source: MGI

post-embryonic development

Inferred from mutant phenotype PubMed 7761462. Source: MGI

regulation of gene expression

Inferred from mutant phenotype PubMed 12438513. Source: MGI

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

steroid catabolic process

Inferred from electronic annotation. Source: Ensembl

toxin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

toxin metabolic process

Inferred from mutant phenotype PubMed 17166882. Source: MGI

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaromatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

caffeine oxidase activity

Inferred from electronic annotation. Source: Ensembl

demethylase activity

Inferred from electronic annotation. Source: Ensembl

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

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

Inferred from direct assay PubMed 8274012. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 513512Cytochrome P450 1A2
PRO_0000051654

Sites

Metal binding4561Iron (heme axial ligand)
Binding site2251Substrate By similarity

Natural variations

Natural variant3841I → M in P2.

Sequences

Sequence LengthMass (Da)Tools
P00186 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: DC2D7D976B126E3B

FASTA51358,184
        10         20         30         40         50         60 
MAFSQYISLA PELLLATAIF CLVFWMVRAS RTQVPKGLKN PPGPWGLPFI GHMLTVGKNP 

        70         80         90        100        110        120 
HLSLTRLSQQ YGDVLQIRIG STPVVVLSGL NTIKQALVRQ GDDFKGRPDL YSFTLITNGK 

       130        140        150        160        170        180 
SMTFNPDSGP VWAARRRLAQ DALKSFSIAS DPTSASSCYL EEHVSKEANH LVSKLQKAMA 

       190        200        210        220        230        240 
EVGHFEPVSQ VVESVANVIG AMCFGKNFPR KSEEMLNIVN NSKDFVENVT SGNAVDFFPV 

       250        260        270        280        290        300 
LRYLPNPALK RFKTFNDNFV LFLQKTVQEH YQDFNKNSIQ DITSALFKHS ENYKDNGGLI 

       310        320        330        340        350        360 
PEEKIVNIVN DIFGAGFDTV TTAITWSILL LVTWPNVQRK IHEELDTVVG RDRQPRLSDR 

       370        380        390        400        410        420 
PQLPYLEAFI LEIYRYTSFV PFTIPHSTTR DTSLNGFHIP KERCIYINQW QVNHDEKQWK 

       430        440        450        460        470        480 
DPFVFRPERF LTNNNSAIDK TQSEKVMLFG LGKRRCIGEI PAKWEVFLFL AILLQHLEFS 

       490        500        510 
VPPGVKVDLT PNYGLTMKPG TCEHVQAWPR FSK 

« Hide

References

« Hide 'large scale' references
[1]"The murine Ah locus. Comparison of the complete cytochrome P1-450 and P3-450 cDNA nucleotide and amino acid sequences."
Kimura S., Gonzalez F.J., Nebert D.W.
J. Biol. Chem. 259:10705-10713(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3).
Strain: C57BL/6N.
[2]"Mouse cytochrome P3-450: complete cDNA and amino acid sequence."
Kimura S., Gonzalez F.J., Nebert D.W.
Nucleic Acids Res. 12:2917-2928(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3).
Strain: C57BL/6N.
[3]"Comparison of the flanking regions and introns of the mouse 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible cytochrome P1-450 and P3-450 genes."
Gonzalez F.J., Kimura S., Nebert D.W.
J. Biol. Chem. 260:5040-5049(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3).
[4]Erratum
Gonzalez F.J., Kimura S., Nebert D.W.
J. Biol. Chem. 260:11884-11889(1985)
[5]"Isolation and characterization of full-length mouse cDNA and genomic clones of 3-methylcholanthrene-inducible cytochrome P1-450 and P3-450."
Gonzalez F.J., McKenzie P.I., Kimura S., Nebert D.W.
Gene 29:281-292(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3).
[6]"cDNA and complete amino acid sequence of mouse P2(450): allelic variant of mouse P3(450) gene."
Kimura S., Nebert D.W.
Nucleic Acids Res. 14:6765-6766(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (P2).
Strain: DBA/2N.
Tissue: Liver.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (P3).
Tissue: Liver.
[8]"Amino-terminal sequence and structure of monoclonal antibody immunopurified cytochromes P-450."
Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V., Friedman F.K.
Biochemistry 25:2397-2402(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26.
Strain: DBA/2.
[9]"Methylation differences in the murine P-1-450 and P-3-450 genes in wild-type and mutant hepatoma cell culture."
Peterson T.C., Gonzalez F.J., Nebert D.W.
Biochem. Pharmacol. 35:2107-2114(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 277-315.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01682 Genomic DNA. Translation: CAA25837.1.
X00479 mRNA. Translation: CAA25156.1.
X04283 mRNA. Translation: CAA27832.1.
K02589 mRNA. Translation: AAA37509.1. Sequence problems.
M10022 Genomic DNA. Translation: AAA37508.1.
BC018298 mRNA. Translation: AAH18298.1.
BC054827 mRNA. Translation: AAH54827.1.
CCDSCCDS23229.1.
PIRO4MSM3. B92495.
RefSeqNP_034123.1. NM_009993.3.
UniGeneMm.15537.

3D structure databases

ProteinModelPortalP00186.
SMRP00186. Positions 33-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP00186. 2 interactions.
MINTMINT-1870125.

Chemistry

ChEMBLCHEMBL1671611.

PTM databases

PhosphoSiteP00186.

Proteomic databases

MaxQBP00186.
PaxDbP00186.
PRIDEP00186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034860; ENSMUSP00000034860; ENSMUSG00000032310.
GeneID13077.
KEGGmmu:13077.
UCSCuc009pvm.1. mouse.

Organism-specific databases

CTD1544.
MGIMGI:88589. Cyp1a2.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00750000117317.
HOGENOMHOG000036991.
HOVERGENHBG106944.
InParanoidP00186.
KOK07409.
OMAAFILEIY.
OrthoDBEOG7RBZ85.
PhylomeDBP00186.
TreeFamTF105095.

Gene expression databases

ArrayExpressP00186.
BgeeP00186.
GenevestigatorP00186.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008066. Cyt_P450_E_grp-I_CYP1.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR01683. EP450ICYP1A.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio283024.
PROP00186.
SOURCESearch...

Entry information

Entry nameCP1A2_MOUSE
AccessionPrimary (citable) accession number: P00186
Secondary accession number(s): Q9QWJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 137 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot