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UniProtKB/Swiss-Prot entry P00184


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CP1A1_MOUSE
Primary accession number P00184
Secondary accession number Q61455
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on February 1, 1996 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 83)
Name and origin of the protein
Protein name Cytochrome P450 1A1
Synonyms EC 1.14.14.1
CYPIA1
P450-P1
Gene name
Name: Cyp1a1
Synonyms: Cyp1a-1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=C57BL/6;
TISSUE=Liver;
PubMed=6547952 [NCBI, ExPASy, EBI, Israel, Japan]
Kimura S., Gonzalez F.J., Nebert D.W.;
"The murine Ah locus. Comparison of the complete cytochrome P1-450 and P3-450 cDNA nucleotide and amino acid sequences.";
J. Biol. Chem. 259:10705-10713(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3988744 [NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez F.J., Kimura S., Nebert D.W.;
"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.";
J. Biol. Chem. 260:5040-5049(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6;
PubMed=3308449 [NCBI, ExPASy, EBI, Israel, Japan]
Kimura S., Smith H.H., Hankinson O., Nebert D.W.;
"Analysis of two benzo[a]pyrene-resistant mutants of the mouse hepatoma Hepa-1 P(1)450 gene via cDNA expression in yeast.";
EMBO J. 6:1929-1933(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(84)90057-X; PubMed=6548461 [NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez F.J., McKenzie P.I., Kimura S., Nebert D.W.;
"Isolation and characterization of full-length mouse cDNA and genomic clones of 3-methylcholanthrene-inducible cytochrome P1-450 and P3-450.";
Gene 29:281-292(1984).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Liver;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
PROTEIN SEQUENCE OF 2-25.
STRAIN=C57BL/6;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 280-321.
DOI=10.1016/0006-2952(86)90577-0; PubMed=2425809 [NCBI, ExPASy, EBI, Israel, Japan]
Peterson T.C., Gonzalez F.J., Nebert D.W.;
"Methylation differences in the murine P-1-450 and P-3-450 genes in wild-type and mutant hepatoma cell culture.";
Biochem. Pharmacol. 35:2107-2114(1986).
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
Y00071; CAA68277.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01681; CAA25836.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02588; AAA37506.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10021; AAA37507.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK005000; BAB23734.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M25623; AAA39868.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A23923; O4MSM1.
RefSeq NP_001129531.1; -.
NP_034122.1; -.
UniGene Mm.14089
3D structure databases
HSSP P00179; 1DT6. [HSSP ENTRY / PDB]
SMR P00184; 37-513.
ModBase P00184.
PTM databases
PhosphoSite P00184; -.
Organism-specific databases
MGI MGI:88588; Cyp1a1.
Gene expression databases
ArrayExpress P00184; -.
GermOnline ENSMUSG00000032315; Mus musculus.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792; Cellular component: microsome (inferred from direct assay from MGI).
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 direct assay from MGI).
GO:0009308; Biological process: cellular amine metabolic process (inferred from mutant phenotype from MGI).
GO:0050665; Biological process: hydrogen peroxide biosynthetic process (inferred from mutant phenotype from MGI).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009404; Biological process: toxin metabolic process (inferred from mutant phenotype from MGI).
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.
Proteomics databases
PRIDE P00184; -.
Genome annotation databases
Ensembl ENSMUSG00000032315; Mus musculus. [Contig view]
GeneID 13076; -.
KEGG mmu:13076; -.
Phylogenomic databases
HOGENOM P00184; -.
HOVERGEN P00184; -.
Other
NextBio 283020; -.
SOURCE Cyp1a1; Mus musculus.
ProtoNet P00184.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   524  524     Cytochrome P450 1A1. PRO_0000051631
METAL   461   461        Iron (heme axial ligand) (By similarity). 
MOD_RES   364   364        Phosphoserine (By similarity). 
Sequence information
Length: 524 AA [This is the length of the unprocessed precursor] Molecular weight: 59230 Da [This is the MW of the unprocessed precursor] CRC64: E31D9E9CBA7B2B02 [This is a checksum on the sequence]
        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 

P00184 in FASTA format

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