Cytochrome P450 1A2 - Rattus norvegicus (Rat)

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P04799 (CP1A2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cytochrome P450 1A2
EC=1.14.14.1

Alternative name(s):
CYPIA2
Cytochrome P-448
Cytochrome P-450d
Cytochrome P450-D

Gene names

Name:	Cyp1a2
Synonyms:	Cyp1a-2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	alkaloid metabolic process Inferred from electronic annotation. Source: Compara cellular respiration Inferred from electronic annotation. Source: Compara cellular response to cadmium ion Inferred from electronic annotation. Source: Compara dibenzo-p-dioxin metabolic process Inferred from electronic annotation. Source: Compara exogenous drug catabolic process Inferred from electronic annotation. Source: Compara hydrogen peroxide biosynthetic process Inferred from electronic annotation. Source: Compara lung development Inferred from electronic annotation. Source: Compara monocarboxylic acid metabolic process Inferred from electronic annotation. Source: Compara monoterpenoid metabolic process Inferred from electronic annotation. Source: Compara oxidative deethylation Inferred from electronic annotation. Source: Compara oxidative demethylation Inferred from electronic annotation. Source: Compara porphyrin-containing compound metabolic process Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara regulation of gene expression Inferred from electronic annotation. Source: Compara response to drug Inferred from expression pattern PubMed 19122336. Source: RGD response to estradiol stimulus Inferred from expression pattern PubMed 18992763. Source: RGD response to lipopolysaccharide Inferred from expression pattern PubMed 18314883. Source: RGD response to stress Inferred from expression pattern PubMed 17973897. Source: RGD steroid catabolic process Inferred from electronic annotation. Source: Compara toxin biosynthetic process Inferred from electronic annotation. Source: Compara xenobiotic metabolic process Traceable author statement Ref.2. Source: RGD
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell intracellular membrane-bounded organelle Inferred from direct assay PubMed 12162855. Source: RGD
Molecular_function	aromatase activity Inferred from electronic annotation. Source: EC caffeine oxidase activity Inferred from electronic annotation. Source: Compara demethylase activity Inferred from electronic annotation. Source: Compara electron carrier activity Inferred from electronic annotation. Source: InterPro 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 1441600. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 513

512

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

137

R → H no nucleotide entry Ref.3

Sequence conflict

185

F → L no nucleotide entry Ref.3

Sequence conflict

262

F → S in AAA41028. Ref.1

Sequence conflict

403

C → R in AAA41053. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P04799 [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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 147-513.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. NM_012541.3.
UniGene	Rn.5563.
3D structure databases
ProteinModelPortal	P04799.
SMR	P04799. Positions 33-512.
ModBase	Search...
Proteomic databases
PRIDE	P04799.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000021653; ENSRNOP00000021653; ENSRNOG00000016173.
GeneID	24297.
KEGG	rno:24297.
UCSC	RGD:2459. rat.
Organism-specific databases
CTD	1544.
RGD	2459. Cyp1a2.
Phylogenomic databases
GeneTree	ENSGT00680000099714.
HOVERGEN	HBG106944.
KO	K07409.
Enzyme and pathway databases
SABIO-RK	P04799.
Gene expression databases
Genevestigator	P04799.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. IPR008066. Cyt_P450_E_grp-I_CYP1. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR01683. EP450ICYP1A. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1075125.
NextBio	602906.

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:	April 3, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents