P00184 (CP1A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome P450 1A1
EC=1.14.14.1

Alternative name(s):
CYPIA1
Cytochrome P450-P1

Gene names

Name:	Cyp1a1
Synonyms:	Cyp1a-1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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).
Sequence similarities	Belongs to the cytochrome P450 family.
Sequence caution	The sequence AAA37506.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	9-cis-retinoic acid biosynthetic process Inferred from electronic annotation. Source: Compara aging Inferred from electronic annotation. Source: Compara amine metabolic process Inferred from mutant phenotype PubMed 17052995. Source: MGI camera-type eye development Inferred from electronic annotation. Source: Compara cell proliferation Inferred from electronic annotation. Source: Compara coumarin metabolic process Inferred from electronic annotation. Source: Compara digestive tract development Inferred from electronic annotation. Source: Compara drug metabolic process Inferred from electronic annotation. Source: Compara embryo development ending in birth or egg hatching Inferred from electronic annotation. Source: Compara flavonoid metabolic process Inferred from electronic annotation. Source: Compara hepatocyte differentiation Inferred from electronic annotation. Source: Compara heterocycle metabolic process Inferred from mutant phenotype PubMed 17052995. Source: MGI hydrogen peroxide biosynthetic process Inferred from mutant phenotype PubMed 14980704. Source: MGI insecticide metabolic process Inferred from electronic annotation. Source: Compara maternal process involved in parturition Inferred from electronic annotation. Source: Compara porphyrin-containing compound metabolic process Inferred from electronic annotation. Source: Compara positive regulation of S phase of mitotic cell cycle Inferred from electronic annotation. Source: Compara response to antibiotic Inferred from electronic annotation. Source: Compara response to arsenic-containing substance Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to food Inferred from electronic annotation. Source: Compara response to herbicide Inferred from electronic annotation. Source: Compara response to hyperoxia Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to iron(III) ion Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to nematode Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara response to toxin Inferred from mutant phenotype PubMed 16377763. Source: MGI response to virus Inferred from electronic annotation. Source: Compara response to vitamin A Inferred from electronic annotation. Source: Compara response to wounding Inferred from electronic annotation. Source: Compara toxin metabolic process Inferred from mutant phenotype PubMed 17166882. Source: MGI
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	aromatase activity Inferred from electronic annotation. Source: EC demethylase activity Inferred from electronic annotation. Source: Compara electron carrier activity Inferred from electronic annotation. Source: InterPro flavonoid 3'-monooxygenase activity Inferred from electronic annotation. Source: Compara heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on diphenols and related substances as donors Inferred from electronic annotation. Source: Compara oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Inferred from direct assay PubMed 8274012. Source: MGI steroid hydroxylase activity Inferred from electronic annotation. Source: Compara vitamin D 24-hydroxylase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 524	524	Cytochrome P450 1A1		PRO_0000051631
Sites
	Metal binding	461	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P00184 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: E31D9E9CBA7B2B02	FASTA	524	59,230
	10 20 30 40 50 60 MPSMYGLPAF VSATELLLAV TVFCLGFWVV RATRTWVPKG LKTPPGPWGL PFIGHMLTVG 70 80 90 100 110 120 KNPHLSLTRL SQQYGDVLQI RIGSTPVVVL SGLNTIKQAL VRQGDDFKGR PDLYSFTLIT 130 140 150 160 170 180 NGKSMTFNPD SGPVWAARRR LAQNALKSFS IASDPTSASS CYLEEHVSKE ANYLVSKLQK 190 200 210 220 230 240 VMAEVGHFDP YKYLVVSVAN VICAICFGQR YDHDDQELLS IVNLSNEFGE VTGSGYPADF 250 260 270 280 290 300 IPVLRYLPNS SLDAFKDLND KFYSFMKKLI KEHYRTFEKG HIRDITDSLI EHCQDRKLDE 310 320 330 340 350 360 NANVQLSDDK VITIVLDLFG AGFDTVTTAI SWSLMYLVTN PRVQRKIQEE LDTVIGRDRQ 370 380 390 400 410 420 PRLSDRPQLP YLEAFILETF RHSSFVPFTI PHSTTRDTSL NGFYIPKGCC VFVNQWQVNH 430 440 450 460 470 480 DRELWGDPNE FRPERFLTPS GTLDKRLSEK VTLFGLGKRK CIGETIGRSE VFLFLAILLQ 490 500 510 520 QIEFKVSPGE KVDMTPTYGL TLKHARCEHF QVQMRSSGPQ HLQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The murine Ah locus. Comparison of the complete cytochrome P1-450 and P3-450 cDNA nucleotide and amino acid sequences." Kimura S., Gonzalez F.J., Nebert D.W. J. Biol. Chem. 259:10705-10713(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: C57BL/6. Tissue: Liver.
[2]	"Comparison of the flanking regions and introns of the mouse 2,3,7,8-tetrachlorodibenzo-p-dioxin-inducible cytochrome P1-450 and P3-450 genes." Gonzalez F.J., Kimura S., Nebert D.W. J. Biol. Chem. 260:5040-5049(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Analysis of two benzo[a]pyrene-resistant mutants of the mouse hepatoma Hepa-1 P(1)450 gene via cDNA expression in yeast." Kimura S., Smith H.H., Hankinson O., Nebert D.W. EMBO J. 6:1929-1933(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6.
[4]	"Isolation and characterization of full-length mouse cDNA and genomic clones of 3-methylcholanthrene-inducible cytochrome P1-450 and P3-450." Gonzalez F.J., McKenzie P.I., Kimura S., Nebert D.W. Gene 29:281-292(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Liver.
[6]	"Amino-terminal sequence and structure of monoclonal antibody immunopurified cytochromes P-450." Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V., Friedman F.K. Biochemistry 25:2397-2402(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-25. Strain: C57BL/6.
[7]	"Methylation differences in the murine P-1-450 and P-3-450 genes in wild-type and mutant hepatoma cell culture." Peterson T.C., Gonzalez F.J., Nebert D.W. Biochem. Pharmacol. 35:2107-2114(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 280-321.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y00071 mRNA. Translation: CAA68277.1. X01681 Genomic DNA. Translation: CAA25836.1. K02588 mRNA. Translation: AAA37506.1. Different initiation. M10021 Genomic DNA. Translation: AAA37507.1. AK005000 mRNA. Translation: BAB23734.1. M25623 Genomic DNA. Translation: AAA39868.1.
IPI	IPI00128286.
PIR	O4MSM1. A23923.
RefSeq	NP_001129531.1. NM_001136059.2. NP_034122.1. NM_009992.4.
UniGene	Mm.14089.
3D structure databases
ProteinModelPortal	P00184.
SMR	P00184. Positions 37-513.
ModBase	Search...
PTM databases
PhosphoSite	P00184.
Proteomic databases
PaxDb	P00184.
PRIDE	P00184.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034865; ENSMUSP00000034865; ENSMUSG00000032315.
GeneID	13076.
KEGG	mmu:13076.
Organism-specific databases
CTD	1543.
MGI	MGI:88588. Cyp1a1.
Phylogenomic databases
eggNOG	COG2124.
HOGENOM	HOG000036991.
HOVERGEN	HBG106944.
InParanoid	P00184.
KO	K07408.
OrthoDB	EOG4WSW9D.
Gene expression databases
ArrayExpress	P00184.
Bgee	P00184.
Genevestigator	P00184.
GermOnline	ENSMUSG00000032315. Mus musculus.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. IPR008066. Cyt_P450_E_grp-I_CYP1. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR01683. EP450ICYP1A. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL6171.
NextBio	283020.
SOURCE	Search...

Entry information

Entry name

CP1A1_MOUSE

Accession

Primary (citable) accession number: P00184
Secondary accession number(s): Q61455

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program