[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Lung; PubMed=1778988 [NCBI, ExPASy, EBI, Israel, Japan] Sagami I., Ohmachi T., Fujii H., Kikuchi H., Watanabe M.; "Hamster cytochrome P-450 IA gene family, P-450IA1 and P-450IA2 in lung and liver: cDNA cloning and sequence analysis."; J. Biochem. 110:641-647(1991).
[2]	NUCLEOTIDE SEQUENCE. Ohgiya S., Goda T., Ishizaki K., Morimoto M., Sakamoto T., Kamataki T., Shinriki N.; "Molecular cloning and expression of hamster cytochrome P450 1A1 and cytochrome P450 reductase."; Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.

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.
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

D10251; BAA01096.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D12977; BAA02354.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10913; BAA01717.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JX0189; JX0189.

3D structure databases

HSSP

P00179; 1DT6. [HSSP ENTRY / PDB]

ModBase

Q00557.

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.

ProtoNet

Q00557.

Phylogenomic databases

HOVERGEN

Q00557; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 524`	`524`	`Cytochrome P450 1A1.`	`PRO_0000051630`
`METAL`	`461 461`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`18 18`		`L -> V (in Ref. 1; BAA01096).`
`CONFLICT`	`521 521`		`H -> Y (in Ref. 1; BAA01096).`

Sequence information

Length: 524 AA [This is the length of the unprocessed precursor]

Molecular weight: 59136 Da [This is the MW of the unprocessed precursor]

CRC64: 2A4C6AF9AE5FD8E0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSIYGLLNF MSATELLLAI TVFCLGFWVV RALRTQVPKG LKTPPGPWGL PILGHVLTLG 

        70         80         90        100        110        120 
KNPHLSLTKL SKQYGDVLQI RIGSTPVVVL SGLDTIRQAL VRQGDDFKGR PDFYSFTLIT 

       130        140        150        160        170        180 
NGKSMTFNPD CGPVWAARRR LAQDALKSFS IALDPASASS CYLEEYVIKE ADYLISKFQK 

       190        200        210        220        230        240 
LMAEVGHFDP DRYLVVSVTN VICAMCFGQR YDHDDQELLS IVNLSNEFGK VTGSGYPPDF 

       250        260        270        280        290        300 
IPILRYLPNS SLDAFKDLNK KFYSFMQKSV KEHYRTFEKG HIRDITDSLI EHCQDKSLDE 

       310        320        330        340        350        360 
NANVQLSDDR VINIIVDLFG AGFDTVTTAI SWSLMYLVTN PGVQRKIQEE LDTVIGRSRR 

       370        380        390        400        410        420 
PRLCDRSQLP YLEAFILETF RHSSFLPFTI PHSTTRDTSL CGFYIPKGHC VFVNQWQINH 

       430        440        450        460        470        480 
NQELWGDPNK FRPERFLTSS GTLDKVLSGK VTLFGLGKRK CIGETIGRLE VFLFLAILLQ 

       490        500        510        520 
QIEFTVSPGE KVDMTPIYGL TLKHARCEYF QAQTRSSGPQ HPQA

Q00557 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