[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3). STRAIN=C57BL/6N; PubMed=6547952 [NCBI, ExPASy, EBI, Israel, Japan] Kimura S., Gonzalez F.J., Nebert D.W.; "The murine Ah locus. Comparison of the complete cytochrome P1-450 and P3-450 cDNA nucleotide and amino acid sequences."; J. Biol. Chem. 259:10705-10713(1984).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3). STRAIN=C57BL/6N; DOI=10.1093/nar/12.6.2917; PubMed=6324134 [NCBI, ExPASy, EBI, Israel, Japan] Kimura S., Gonzalez F.J., Nebert D.W.; "Mouse cytochrome P3-450: complete cDNA and amino acid sequence."; Nucleic Acids Res. 12:2917-2928(1984).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3). PubMed=3988744 [NCBI, ExPASy, EBI, Israel, Japan] Gonzalez F.J., Kimura S., Nebert D.W.; "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."; J. Biol. Chem. 260:5040-5049(1985).
[4]	ERRATUM. Gonzalez F.J., Kimura S., Nebert D.W.; J. Biol. Chem. 260:11884-11889(1985).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3). DOI=10.1016/0378-1119(84)90057-X; PubMed=6548461 [NCBI, ExPASy, EBI, Israel, Japan] Gonzalez F.J., McKenzie P.I., Kimura S., Nebert D.W.; "Isolation and characterization of full-length mouse cDNA and genomic clones of 3-methylcholanthrene-inducible cytochrome P1-450 and P3-450."; Gene 29:281-292(1984).
[6]	NUCLEOTIDE SEQUENCE [MRNA] (P2). STRAIN=DBA/2N; TISSUE=Liver; DOI=10.1093/nar/14.16.6765; PubMed=3755821 [NCBI, ExPASy, EBI, Israel, Japan] Kimura S., Nebert D.W.; "cDNA and complete amino acid sequence of mouse P2(450): allelic variant of mouse P3(450) gene."; Nucleic Acids Res. 14:6765-6766(1986).
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (P3). TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[8]	PROTEIN SEQUENCE OF 2-26. STRAIN=DBA/2; DOI=10.1021/bi00357a015; PubMed=3718958 [NCBI, ExPASy, EBI, Israel, Japan] Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V., Friedman F.K.; "Amino-terminal sequence and structure of monoclonal antibody immunopurified cytochromes P-450."; Biochemistry 25:2397-2402(1986).
[9]	NUCLEOTIDE SEQUENCE [MRNA] OF 277-315. DOI=10.1016/0006-2952(86)90577-0; PubMed=2425809 [NCBI, ExPASy, EBI, Israel, Japan] Peterson T.C., Gonzalez F.J., Nebert D.W.; "Methylation differences in the murine P-1-450 and P-3-450 genes in wild-type and mutant hepatoma cell culture."; Biochem. Pharmacol. 35:2107-2114(1986).
[10]	ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan] Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."; Mol. Cell 23:607-618(2006).

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).
SIMILARITY: Belongs to the cytochrome P450 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X01682; CAA25837.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00479; CAA25156.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X04283; CAA27832.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
K02589; AAA37509.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M10022; AAA37508.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018298; AAH18298.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC054827; AAH54827.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

B92495; O4MSM3.

NP_034123.1; -.

3D structure databases

HSSP

P00179; 1DT6. [HSSP ENTRY / PDB]

P00186; 33-512.

PTM databases

P00186; -.

Organism-specific databases

MGI

MGI:88589; Cyp1a2.

Gene expression databases

ArrayExpress

P00186; -.

GermOnline

ENSMUSG00000032310; Mus musculus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792;	Cellular component: microsome (inferred from direct assay from MGI).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0050381;	Molecular function: unspecific monooxygenase activity (inferred from direct assay from MGI).
GO:0045333;	Biological process: cellular respiration (inferred from mutant phenotype from MGI).
GO:0018894;	Biological process: dibenzo-p-dioxin metabolic process (inferred from mutant phenotype from MGI).
GO:0017144;	Biological process: drug metabolic process (inferred from mutant phenotype from MGI).
GO:0050665;	Biological process: hydrogen peroxide biosynthetic process (inferred from mutant phenotype from MGI).
GO:0030324;	Biological process: lung development (inferred from mutant phenotype from MGI).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006778;	Biological process: porphyrin metabolic process (inferred from mutant phenotype from MGI).
GO:0009791;	Biological process: post-embryonic development (inferred from mutant phenotype from MGI).
GO:0010468;	Biological process: regulation of gene expression (inferred from mutant phenotype from MGI).
GO:0009404;	Biological process: toxin metabolic process (inferred from mutant phenotype from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
IPR008066; Cyt_P450_E_grp-I_CYP1.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19383; Cyt_P450; 1.
PTHR19383:SF63; Cyt_P450_E_grp-I_CYP1; 1.

Pfam

PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR01683; EP450ICYP1A.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

ProtoNet

P00186.

Genome annotation databases

Ensembl

ENSMUSG00000032310; Mus musculus. [Contig view]

GeneID

13077; -.

KEGG

mmu:13077; -.

Phylogenomic databases

HOGENOM

P00186; -.

HOVERGEN

P00186; -.

Other

NextBio

283024; -.

SOURCE

Cyp1a2; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Polymorphism.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 513`	`513`	`Cytochrome P450 1A2.`	`PRO_0000051654`
`METAL`	`456 456`		`Iron (heme axial ligand).`
`MOD_RES`	`288 288`		`N6-acetyllysine.`
`VARIANT`	`384 384`	`1`	`I -> M (in P2).`

Sequence information

Length: 513 AA [This is the length of the unprocessed precursor]

Molecular weight: 58184 Da [This is the MW of the unprocessed precursor]

CRC64: DC2D7D976B126E3B [This is a checksum on the sequence]

        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

P00186 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools