[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=6089174 [NCBI, ExPASy, EBI, Israel, Japan] Sogawa K., Gotoh O., Kawajiri K., Fujii-Kuriyama Y.; "Distinct organization of methylcholanthrene- and phenobarbital-inducible cytochrome P-450 genes in the rat."; Proc. Natl. Acad. Sci. U.S.A. 81:5066-5070(1984).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1093/nar/12.6.2929; PubMed=6324135 [NCBI, ExPASy, EBI, Israel, Japan] Yabusaki Y., Shimizu M., Murakami H., Nakamura K., Oeda K., Ohkawa H.; "Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-induced rat liver cytochrome P-450MC."; Nucleic Acids Res. 12:2929-2938(1984).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0003-9861(85)90300-5; PubMed=3838427 [NCBI, ExPASy, EBI, Israel, Japan] Hines R.N., Levy J.B., Conrad R.D., Iversen P.L., Shen M.-L., Renli A.M., Bresnick E.; "Gene structure and nucleotide sequence for rat cytochrome P-450c."; Arch. Biochem. Biophys. 237:465-476(1985).
[4]	PROTEIN SEQUENCE OF 2-26. DOI=10.1021/bi00357a015; PubMed=3718958 [NCBI, ExPASy, EBI, Israel, Japan] Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V., Friedman F.K.; "Amino-terminal sequence and structure of monoclonal antibody immunopurified cytochromes P-450."; Biochemistry 25:2397-2402(1986).
[5]	PROTEIN SEQUENCE OF 2-22. DOI=10.1016/0006-2952(88)90634-X; PubMed=3041969 [NCBI, ExPASy, EBI, Israel, Japan] Amelizad Z., Narbonne J.F., Wolf C.R., Robertson L.W., Oesch F.; "Effect of nutritional imbalances on cytochrome P-450 isozymes in rat liver."; Biochem. Pharmacol. 37:3245-3249(1988).
[6]	PARTIAL PROTEIN SEQUENCE. DOI=10.1006/abbi.1996.0236; PubMed=8651689 [NCBI, ExPASy, EBI, Israel, Japan] Cvrk T., Hodek P., Strobel H.W.; "Identification and characterization of cytochrome P4501A1 amino acid residues interacting with a radiolabeled photoaffinity diazido-benzphetamine analogue."; Arch. Biochem. Biophys. 330:142-152(1996).
[7]	SUBCELLULAR LOCATION. STRAIN=Sprague-Dawley; TISSUE=Liver; DOI=10.1083/jcb.139.3.589; PubMed=9348277 [NCBI, ExPASy, EBI, Israel, Japan] Addya S., Anandatheerthavarada H.K., Biswas G., Bhagwat S.V., Mullick J., Avadhani N.G.; "Targeting of NH2-terminal-processed microsomal protein to mitochondria: a novel pathway for the biogenesis of hepatic mitochondrial P450MT2."; J. Cell Biol. 139:589-599(1997).

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: Cytochrome P450 1A1: Cytoplasm.
SUBCELLULAR LOCATION: Cytochrome P450MT2A: Endoplasmic reticulum membrane. Mitochondrion membrane. Microsome membrane.
SUBCELLULAR LOCATION: Cytochrome P450MT2B: Endoplasmic reticulum. Mitochondrion.
TISSUE SPECIFICITY: Liver.
INDUCTION: By 3-methylcholanthrene (3MC) and beta-naphthoflavone (BNF).
DOMAIN: Contains a chimeric signal that facilitates targeting of the protein to both the endoplasmic reticulum and mitochondria. A 12 amino acid sequence between 33 and 44 functions as a putative mitochondrial-targeting signal. The removal of the first 4- or 32-amino acid residues from the intact protein positions the mitochondrial targeting signal for efficient binding to the mitochondrial import receptors. The membrane-free P4501A1 seems to be more sensible to proteolysis.
PTM: Two forms; MT2A (long form) and MT2B (short form); are produced by NH2-terminal proteolytic cleavage. This cleavage activates a cryptic mitochondrial targeting signal.
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

K02246; AAA41027.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00469; CAA25153.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26129; AAA41025.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A00185; O4RTMC.

NP_036672.2; -.

3D structure databases

HSSP

P00179; 1N6B. [HSSP ENTRY / PDB]

ModBase

P00185.

Organism-specific databases

RGD

2458; Cyp1a1.

Gene expression databases

ArrayExpress

P00185; -.

GermOnline

ENSRNOG00000019500; Rattus norvegicus.

Ontologies

GO:0005783;	Cellular component: endoplasmic reticulum (inferred from electronic annotation from UniProtKB-KW).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0031966;	Cellular component: mitochondrial membrane (inferred from electronic annotation from UniProtKB-SubCell).
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

P00185.

Genome annotation databases

Ensembl

ENSRNOG00000019500; Rattus norvegicus. [Contig view]

GeneID

24296; -.

KEGG

rno:24296; -.

Phylogenomic databases

HOVERGEN

P00185; -.

Other

NextBio

602902; -.

UniRef

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

Keywords

Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Mitochondrion; Monooxygenase; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`2 524`	`523`	`Cytochrome P450 1A1.`	`PRO_0000003564`
`CHAIN`	`5 524`	`520`	`Cytochrome P450MT2A.`	`PRO_0000003565`
`CHAIN`	`33 524`	`492`	`Cytochrome P450MT2B.`	`PRO_0000003566`
`REGION`	`33 44`	`12`	`Mitochondrial targeting signal.`
`METAL`	`461 461`		`Iron (heme axial ligand).`
`MOD_RES`	`364 364`		`Phosphoserine (By similarity).`
`MUTAGEN`	`32 33`		`VT->AI: No proteolytic cleavage.`
`CONFLICT`	`21 22`		`TT -> VV (in Ref. 5; AA sequence).`
`CONFLICT`	`53 53`		`I -> M (in Ref. 2; CAA25153).`
`CONFLICT`	`494 494`		`M -> S (in Ref. 3; AAA41025).`

Sequence information

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

Molecular weight: 59393 Da [This is the MW of the unprocessed precursor]

CRC64: C766DF8044D598C5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPSVYGFPAF TSATELLLAV TTFCLGFWVV RVTRTWVPKG LKSPPGPWGL PFIGHVLTLG 

        70         80         90        100        110        120 
KNPHLSLTKL SQQYGDVLQI RIGSTPVVVL SGLNTIKQAL VKQGDDFKGR PDLYSFTLIA 

       130        140        150        160        170        180 
NGQSMTFNPD SGPLWAARRR LAQNALKSFS IASDPTLASS CYLEEHVSKE AEYLISKFQK 

       190        200        210        220        230        240 
LMAEVGHFDP FKYLVVSVAN VICAICFGRR YDHDDQELLS IVNLSNEFGE VTGSGYPADF 

       250        260        270        280        290        300 
IPILRYLPNS SLDAFKDLNK KFYSFMKKLI KEHYRTFEKG HIRDITDSLI EHCQDRRLDE 

       310        320        330        340        350        360 
NANVQLSDDK VITIVFDLFG AGFDTITTAI SWSLMYLVTN PRIQRKIQEE LDTVIGRDRQ 

       370        380        390        400        410        420 
PRLSDRPQLP YLEAFILETF RHSSFVPFTI PHSTIRDTSL NGFYIPKGHC VFVNQWQVNH 

       430        440        450        460        470        480 
DQELWGDPNE FRPERFLTSS GTLDKHLSEK VILFGLGKRK CIGETIGRLE VFLFLAILLQ 

       490        500        510        520 
QMEFNVSPGE KVDMTPAYGL TLKHARCEHF QVQMRSSGPQ HLQA

P00185 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