[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/0003-9861(90)90664-K; PubMed=2275554 [NCBI, ExPASy, EBI, Israel, Japan] Lai T.S., Chiang J.Y.L.; "Cloning and characterization of two major 3-methylcholanthrene inducible hamster liver cytochrome P450s."; Arch. Biochem. Biophys. 283:429-439(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. 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).
[3]	PROTEIN SEQUENCE OF 2-19. TISSUE=Liver; PubMed=2391346 [NCBI, ExPASy, EBI, Israel, Japan] Koga N., Ariyoshi N., Nakashima H., Yoshimura H.; "Purification and characterization of two forms of 2,3,4,7,8-pentachlorodibenzofuran-inducible cytochrome P-450 in hamster liver."; J. Biochem. 107:826-833(1990).

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.
TISSUE SPECIFICITY: Found in lung and 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

M63787; AAA37070.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10252; BAA01097.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D10914; BAA01718.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JX0190; JX0190.

3D structure databases

HSSP

P00179; 1DT6. [HSSP ENTRY / PDB]

SMR

P24453; 33-512.

ModBase

P24453.

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

P24453.

Phylogenomic databases

HOVERGEN

P24453; -.

Other

UniRef

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

Keywords

Acetylation; Direct protein sequencing; 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.`
`CHAIN`	`2 513`	`512`	`Cytochrome P450 1A2.`	`PRO_0000051653`
`METAL`	`456 456`		`Iron (heme axial ligand) (By similarity).`
`MOD_RES`	`288 288`		`N6-acetyllysine (By similarity).`
`CONFLICT`	`49 49`		`I -> F (in Ref. 1; AAA37070).`
`CONFLICT`	`52 53`		`HV -> MC (in Ref. 1; AAA37070).`
`CONFLICT`	`253 254`		`KN -> GG (in Ref. 1; AAA37070).`
`CONFLICT`	`326 326`		`L -> W (in Ref. 1; AAA37070).`
`CONFLICT`	`356 356`		`R -> L (in Ref. 1; AAA37070).`
`CONFLICT`	`485 485`		`T -> Q (in Ref. 1; AAA37070).`

Sequence information

Length: 513 AA [This is the length of the unprocessed precursor]

Molecular weight: 58082 Da [This is the MW of the unprocessed precursor]

CRC64: D179B43386C19815 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALSQYTSLS TELVLATAIF CIVFWVARAL RTQVPKGLKT PPGPWGLPIL GHVLTLGKNP 

        70         80         90        100        110        120 
HLSLTKLSKQ YGDVLQIRIG STPVVVLSGL DTIRQALVRQ GDDFKGRPDL YSFTLITNGK 

       130        140        150        160        170        180 
SMTFNPDCGP VWAARRRLAQ DALKSFSIAS DPTSASSCYL EDHVIKEANH LVSKLQKLTA 

       190        200        210        220        230        240 
EVGHFEPVNQ VVESVANVIG AMCFGKNFPR KSEEMLRIVK GSSDFVENVS SGNAVDFFPI 

       250        260        270        280        290        300 
LRYLPNPDLK RFKNFNDNFV LFLQKTVQEH YQDFNKNSIQ DITGALFKHS ENSKDSGGLI 

       310        320        330        340        350        360 
PQEKIVNIVN DLFGAGFDTV TTAITLSILL LVTWPNVQRK IHKELDTVIG RDRQPRLSDR 

       370        380        390        400        410        420 
LQLPYMEAFI LELYRYTSFV PFTIPHSTTR DTSLNGFYIP KDRCIFINQW QVNHDEKQWK 

       430        440        450        460        470        480 
DPFVFRPERF LTDNDTVINK TLSEKVMLFG LGKRRCIGEI PAKWEVFLFL AILLQQLEFS 

       490        500        510 
VPPGTKVDLT PTYGLTMKPQ TCKYIQAWPR FSK

P24453 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