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P04799 (CP1A2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 P-448
Cytochrome P-450d
Cytochrome P450-D
Gene names
Name:Cyp1a2
Synonyms:Cyp1a-2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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
   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 respiration

Inferred from electronic annotation. Source: Ensembl

cellular response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

dibenzo-p-dioxin metabolic process

Inferred from electronic annotation. Source: Ensembl

exogenous drug catabolic process

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from expression pattern PubMed 19122336. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 18992763. Source: RGD

response to immobilization stress

Inferred from expression pattern PubMed 17973897. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 18314883. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 18754104. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 19177741. Source: RGD

steroid catabolic process

Inferred from electronic annotation. Source: Ensembl

toxin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

xenobiotic metabolic process

Traceable author statement Ref.2. Source: RGD

   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 12162855. Source: RGD

   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

monooxygenase activity

Inferred from direct assay PubMed 12162855. Source: RGD

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 513512Cytochrome P450 1A2
PRO_0000051656

Sites

Metal binding4561Iron (heme axial ligand)

Experimental info

Sequence conflict261V → M AA sequence Ref.6
Sequence conflict1371R → H in AAA41053. Ref.2
Sequence conflict1371R → H no nucleotide entry Ref.3
Sequence conflict1851F → L no nucleotide entry Ref.3
Sequence conflict2621F → S in AAA41028. Ref.1
Sequence conflict4031C → R in AAA41053. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P04799 [UniParc].

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

FASTA51358,259
        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' 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.
PIRA61400.
RefSeqNP_036673.3. NM_012541.3.
UniGeneRn.5563.

3D structure databases

ProteinModelPortalP04799.
SMRP04799. Positions 33-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246478. 1 interaction.
MINTMINT-4564487.

Chemistry

ChEMBLCHEMBL1075125.

Proteomic databases

PRIDEP04799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000021653; ENSRNOP00000021653; ENSRNOG00000016173.
GeneID24297.
KEGGrno:24297.
UCSCRGD:2459. rat.

Organism-specific databases

CTD1544.
RGD2459. Cyp1a2.

Phylogenomic databases

GeneTreeENSGT00750000117317.
HOVERGENHBG106944.
KOK07409.
OMAVSKEANH.
OrthoDBEOG7RBZ85.
PhylomeDBP04799.

Enzyme and pathway databases

SABIO-RKP04799.

Gene expression databases

GenevestigatorP04799.

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

NextBio602906.
PROP04799.

Entry information

Entry nameCP1A2_RAT
AccessionPrimary (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 16, 2014
This is version 129 of the entry and version 2 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