NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND CHARACTERIZATION.
TISSUE=Liver;
DOI=10.1016/S0006-2952(98)00100-2; PubMed=9698097 [NCBI, ExPASy, EBI, Israel, Japan]
Sakuma T., Hieda M., Igarashi T., Ohgiya S., Nagata R., Nemoto N., Kamataki T.;
"Molecular cloning and functional analysis of cynomolgus monkey CYP1A2.";
Biochem. Pharmacol. 56:131-139(1998).

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.
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.
TISSUE SPECIFICITY: Liver.
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

D86474; BAA33789.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P00179; 1DT6. [HSSP ENTRY / PDB]

SMR

O77809; 34-514.

ModBase

O77809.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
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 electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Phylogenomic databases

HOVERGEN

O77809; -.

Other

ProtoNet

O77809.

UniRef

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

Keywords

Acetylation; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 516`	`515`	`Cytochrome P450 1A2.`	`PRO_0000051652`
`METAL`	`458 458`		`Iron (heme axial ligand) (By similarity).`
`MOD_RES`	`289 289`		`N6-acetyllysine (By similarity).`

Sequence information

Length: 516 AA [This is the length of the unprocessed precursor]

Molecular weight: 58197 Da [This is the MW of the unprocessed precursor]

CRC64: 3F71E3999EC4CDF7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALSQSVPFL ATELLLASAI FCLVFWVLRG SRPRVPKGLK SPPEPWGWPL LGHVLTLGKN 

        70         80         90        100        110        120 
PHLALSRMSQ LYGDVLQIRI GSTPVLVLSG LDTIRQALVR QGDDFKGRPD LYSFTFITDG 

       130        140        150        160        170        180 
QSMSFSPDSG PVWAARRRLA QNALNTFSIA SDPASSSSCY LEEHVSKEAE ALISRLQELM 

       190        200        210        220        230        240 
AGPGHFDPYN QVVVSVANVI GAMCFGQHFP ESSDEMLSLV KNSHEFVESA SSGNPVDFFP 

       250        260        270        280        290        300 
ILRYLPNPAL QRFKAFNQRF RRFLQKTVQE HYQDFDKNSV QDITGALFKH SKKGPRASGN 

       310        320        330        340        350        360 
LIPQEKIVNL VNDIFGAGFD TIATAISWSL MYLVTKPEIQ RKIQKELDAV IGRGRRPRLS 

       370        380        390        400        410        420 
DRPQLPYLEA FILETFRHSS FVPFTIPHST TRDTTLNGFY IPRECCVFIN QWQVNHDPQL 

       430        440        450        460        470        480 
WGDPSEFRPE RFLTAEGTTI NKPLSEKIML FGLGKRRCIG EVLGKWEVFL FLAILLQQLE 

       490        500        510 
FSVPPGVKVD LTPIYGLTMK HARCEHFQAR LRFSIK

O77809 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