NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=Hudson river;
TISSUE=Liver;
DOI=10.1006/abbi.1995.1453; PubMed=7574676 [NCBI, ExPASy, EBI, Israel, Japan]
Roy N.K., Kreamer G.L., Konkle B., Grunwald C., Wirgin I.;
"Characterization and prevalence of a polymorphism in the 3' untranslated region of cytochrome P4501A1 in cancer-prone Atlantic tomcod.";
Arch. Biochem. Biophys. 322:204-213(1995).

[2]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8807670 [NCBI, ExPASy, EBI, Israel, Japan]
Roy N.K., Konkle B., Wirgin I.;
"Characterization of CYP1A1 gene regulatory elements in cancer-prone Atlantic tomcod.";
Pharmacogenetics 6:273-277(1996).

Comments

FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize 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 benzo[a]pyrene (B[A]P) and beta-naphthoflavone (beta-NF).
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

L41917; AAB00085.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L41886; AAB00082.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S66464; S66464.

3D structure databases

HSSP

P00179; 1DT6. [HSSP ENTRY / PDB]

ModBase

Q92148.

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; 2.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR01683; EP450ICYP1A.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.

Phylogenomic databases

HOVERGEN

Q92148; -.

Other

ProtoNet

Q92148.

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`	`1 515`	`515`	`Cytochrome P450 1A1.`	`PRO_0000051640`
`METAL`	`459 459`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 515 AA [This is the length of the unprocessed precursor]

Molecular weight: 57826 Da [This is the MW of the unprocessed precursor]

CRC64: CB73707629A01C25 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALMILPLIG SVSVSETLVA MITVCMIYML MKFLHPDVPE APPAPGPQAL PIIGNVWSWE 

        70         80         90        100        110        120 
NGLPEPHGHG QRYGDILQIQ IGMRSVVVLS GHETVRQALI KQGHDLRPPD LYSFQFINDG 

       130        140        150        160        170        180 
KSLAFSTDQA GVWSPPKAGH ECPALLFHAR GHHAAVLLHV GGACLQGGRL PRQAAVQRHG 

       190        200        210        220        230        240 
TDASFDPFRH IVVSVANVIC GMCFGRRYGH EDQELLSLVN LTDEFGKVVG SGNLADFIPL 

       250        260        270        280        290        300 
LRFLPNATMK RFMAINERFM TFVQKIVTEH YNTYDKDNIR DITDSLIDHC EDRKLDENSN 

       310        320        330        340        350        360 
IQMSDEKIVG IVNDLFGAGF DTVSTALSWS VMYLVAHPEI QERLHQEIKD KVGLSRSPVL 

       370        380        390        400        410        420 
TDRHNLPILE AFIFEIFRHS SFLPFTIPHC ATKDTSLDGY FIPKDTCVFI NQWQINHDPE 

       430        440        450        460        470        480 
LWKEPSTFNP DRFLSADASE LNKLAGEKVM LFGMGKRRCI GEMVARNEVF LFLAILVQRL 

       490        500        510 
TFHAVPGEPL DMTPEYGLTM KHKRCHLRAT VRTTE

Q92148 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