Cytochrome P450 1A2 - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P04799 (CP1A2_RAT)

Last modified October 13, 2009. Version 97. 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-D
    P-450d
    P-448

Gene names

Name:	Cyp1a2
Synonyms:	Cyp1a-2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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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
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to drug Inferred from expression pattern. Source: RGD response to estradiol stimulus Inferred from expression pattern. Source: RGD response to lipopolysaccharide Inferred from expression pattern. Source: RGD response to organic cyclic substance Inferred from expression pattern. Source: RGD response to stress Inferred from expression pattern. Source: RGD xenobiotic metabolic process Ref.2 Traceable author statement. Source: RGD
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from direct assay. Source: RGD
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_0000051656

Sites

Metal binding

456

Iron (heme axial ligand)

Amino acid modifications

Modified residue

288

N6-acetyllysine By similarity

Experimental info

Sequence conflict

V → M AA sequence Ref.6

Sequence conflict

137

R → H in AAA41053. Ref.2

Sequence conflict

185

F → L Ref.3

Sequence conflict

262

F → S in AAA41028. Ref.1

Sequence conflict

403

C → R in AAA41053. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P04799-1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: B1F06FDE9B7B6FA7
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FASTA

513

58,259

        10         20         30         40         50         60 
MAFSQYISLA PELLLATAIF CLVFWVLRGT RTQVPKGLKS PPGPWGLPFI GHMLTLGKNP 

        70         80         90        100        110        120 
HLSLTKLSQQ YGDVLQIRIG STPVVVLSGL NTIKQALVKQ GDDFKGRPDL YSFTLITNGK 

       130        140        150        160        170        180 
SMTFNPDSGP VWAARRRLAQ DALKSFSIAS DPTSVSSCYL EEHVSKEANH LISKFQKLMA 

       190        200        210        220        230        240 
EVGHFEPVNQ VVESVANVIG AMCFGKNFPR KSEEMLNLVK SSKDFVENVT SGNAVDFFPV 

       250        260        270        280        290        300 
LRYLPNPALK RFKNFNDNFV LFLQKTVQEH YQDFNKNSIQ DITGALFKHS ENYKDNGGLI 

       310        320        330        340        350        360 
PQEKIVNIVN DIFGAGFETV TTAIFWSILL LVTEPKVQRK IHEELDTVIG RDRQPRLSDR 

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

       430        440        450        460        470        480 
DPFVFRPERF LTNDNTAIDK TLSEKVMLFG LGKRRCIGEI PAKWEVFLFL AILLHQLEFT 

       490        500        510 
VPPGVKVDLT PSYGLTMKPR TCEHVQAWPR FSK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Coding nucleotide sequence of 3-methylcholanthrene-inducible cytochrome P-450d cDNA from rat liver." Kawajiri K., Gotoh O., Sogawa K., Tagashira Y., Muramatsu M., Fujii-Kuriyama Y. Proc. Natl. Acad. Sci. U.S.A. 81:1649-1653(1984) [PubMed: 6584898] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete nucleotide sequence of a methylcholanthrene-inducible cytochrome P-450 (P-450d) gene in the rat." Sogawa K., Gotoh O., Kawajiri K., Harada T., Fujii-Kuriyama Y. J. Biol. Chem. 260:5026-5032(1985) [PubMed: 2985574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Stable expression of rat cytochrome P450IA2 cDNA and hydroxylation of 17 beta-estradiol and 2-aminofluorene in V79 Chinese hamster cells." Wolfel C., Platt K.L., Dogra S., Glatt H., Wachter F., Doehmer J. Mol. Carcinog. 4:489-498(1991) [PubMed: 1793487] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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]. Tissue: Liver.
[5]	"The primary structure of cytochrome P-450d purified from rat liver microsomes: prediction of helical regions and domain analysis." Haniu M., Ryan D.E., Levin W., Shively J.E. Arch. Biochem. Biophys. 244:323-337(1986) [PubMed: 3947063] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Liver.
[6]	"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.
[7]	"Amino-terminal and carboxy-terminal sequence of hepatic microsomal cytochrome P-450d, a unique hemoprotein from rats treated with isosafrole." Botelho L.H., Ryan D.E., Yuan P.M., Kutny R., Shively J.E., Levin W. Biochemistry 21:1152-1155(1982) [PubMed: 7074072] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20.
[8]	"Modification of cytochrome P450 1A2 enzymes by the mechanism-based inactivator 2-ethynylnaphthalene and the photoaffinity label 4-azidobiphenyl." Yun C.H., Hammons G.J., Jones G., Martin M.V., Hopkins N.E., Alworth W.L., Guengerich F.P. Biochemistry 31:10556-10563(1992) [PubMed: 1420171] [Abstract] Cited for: PROTEIN SEQUENCE OF 67-78.
[9]	"Characterization of complementary DNA clones coding for two forms of 3-methylcholanthrene-inducible rat liver cytochrome P-450." Yabusaki Y., Murakami H., Nakamura K., Nomura N., Shimizu M., Oeda K., Ohkawa H. J. Biochem. 96:793-804(1984) [PubMed: 6548743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 147-513.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	K02422 mRNA. Translation: AAA41028.1. K03241 Genomic DNA. Translation: AAA41053.1. BC127476 mRNA. Translation: AAI27477.1. X01031 mRNA. Translation: CAA25516.1.
IPI	IPI00198947.
PIR	A61400.
RefSeq	NP_036673.3.
UniGene	Rn.5563
3D structure databases
HSSP	HSSP built from PDB template 1DT6 based on UniProtKB P00179.
SMR	P04799. Positions 33-512.
ModBase	Search...
Proteomic databases
PRIDE	P04799.
Genome annotation databases
GeneID	24297.
KEGG	rno:24297.
UCSC	NM_012541. rat.
Organism-specific databases
CTD	24297.
RGD	2459. Cyp1a2.
Phylogenomic databases
HOVERGEN	P04799.
Enzyme and pathway databases
BRENDA	1.14.14.1. 248.
Gene expression databases
Genevestigator	P04799.
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	602906.

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Entry information

Entry name

CP1A2_RAT

Accession

Primary (citable) accession number: P04799
Secondary accession number(s): A1L120, Q64588

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	May 1, 2007
Last modified:	October 13, 2009
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure 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