Cytochrome P450 1A2 - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot P00186 (CP1A2_MOUSE)

Last modified May 5, 2009. Version 95. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Cytochrome P450 1A2
    EC=1.14.14.1
Alternative name(s):
    CYPIA2
    P450-P2/P450-P3

Gene names

Name:	Cyp1a2
Synonyms:	Cyp1a-2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular respiration Inferred from mutant phenotype. Source: MGI dibenzo-p-dioxin metabolic process Inferred from mutant phenotype. Source: MGI drug metabolic process Inferred from mutant phenotype. Source: MGI hydrogen peroxide biosynthetic process Inferred from mutant phenotype. Source: MGI lung development Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin metabolic process Inferred from mutant phenotype. Source: MGI post-embryonic development Inferred from mutant phenotype. Source: MGI regulation of gene expression Inferred from mutant phenotype. Source: MGI toxin metabolic process Inferred from mutant phenotype. Source: MGI
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay. Source: MGI
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
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 513

513

Cytochrome P450 1A2

PRO_0000051654

Sites

Metal binding

456

Iron (heme axial ligand)

Amino acid modifications

Modified residue

288

N6-acetyllysine Ref.10

Natural variations

Natural variant

384

I → M in P2.

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Sequences

Sequence

Length

Mass (Da)

Tools

P00186-1 [UniParc].

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

513

58,184

        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

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References

	« Hide 'large scale' referencesShow '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: 6547952] [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: 6324134] [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: 3988744] [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: 6548461] [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: 3755821] [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: 15489334] [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: 3718958] [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: 2425809] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 277-315.
[10]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." 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. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	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.
IPI	IPI00128287.
PIR	O4MSM3. B92495.
RefSeq	NP_034123.1.
UniGene	Mm.15537
3D structure databases
HSSP	HSSP built from PDB template 1DT6 based on UniProtKB P00179.
SMR	P00186. Positions 33-512.
ModBase	Search...
PTM databases
PhosphoSite	P00186.
Proteomic databases
PRIDE	P00186.
Genome annotation databases
Ensembl	ENSMUSG00000032310. Mus musculus. [Contig view]
GeneID	13077.
KEGG	mmu:13077.
Organism-specific databases
MGI	MGI:88589. Cyp1a2.
Phylogenomic databases
HOGENOM	P00186.
HOVERGEN	P00186.
OMA	P00186. KQWKDPF.
Enzyme and pathway databases
BRENDA	1.14.14.1. 244.
Gene expression databases
ArrayExpress	P00186.
Bgee	P00186.
GermOnline	ENSMUSG00000032310. Mus musculus.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. IPR008066. Cyt_P450_E_grp-I_CYP1. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit. PTHR19383:SF63. Cyt_P450_E_grp-I_CYP1. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR01683. EP450ICYP1A. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	283024.
SOURCE	Search...

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Entry information

Entry name

CP1A2_MOUSE

Accession

Primary (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:	May 5, 2009
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents