ID   CP1A1_MOUSE             Reviewed;         524 AA.
AC   P00184; Q61455;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   05-MAY-2009, entry version 89.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
DE   AltName: Full=P450-P1;
GN   Name=Cyp1a1; Synonyms=Cyp1a-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=C57BL/6; TISSUE=Liver;
RX   MEDLINE=84289486; PubMed=6547952;
RA   Kimura S., Gonzalez F.J., Nebert D.W.;
RT   "The murine Ah locus. Comparison of the complete cytochrome P1-450 and
RT   P3-450 cDNA nucleotide and amino acid sequences.";
RL   J. Biol. Chem. 259:10705-10713(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=85182627; PubMed=3988744;
RA   Gonzalez F.J., Kimura S., Nebert D.W.;
RT   "Comparison of the flanking regions and introns of the mouse 2,3,7,8-
RT   tetrachlorodibenzo-p-dioxin-inducible cytochrome P1-450 and P3-450
RT   genes.";
RL   J. Biol. Chem. 260:5040-5049(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=88004400; PubMed=3308449;
RA   Kimura S., Smith H.H., Hankinson O., Nebert D.W.;
RT   "Analysis of two benzo[a]pyrene-resistant mutants of the mouse
RT   hepatoma Hepa-1 P(1)450 gene via cDNA expression in yeast.";
RL   EMBO J. 6:1929-1933(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=85028449; PubMed=6548461; DOI=10.1016/0378-1119(84)90057-X;
RA   Gonzalez F.J., McKenzie P.I., Kimura S., Nebert D.W.;
RT   "Isolation and characterization of full-length mouse cDNA and genomic
RT   clones of 3-methylcholanthrene-inducible cytochrome P1-450 and P3-
RT   450.";
RL   Gene 29:281-292(1984).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-25.
RC   STRAIN=C57BL/6;
RX   MEDLINE=86243357; PubMed=3718958; DOI=10.1021/bi00357a015;
RA   Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V.,
RA   Friedman F.K.;
RT   "Amino-terminal sequence and structure of monoclonal antibody
RT   immunopurified cytochromes P-450.";
RL   Biochemistry 25:2397-2402(1986).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 280-321.
RX   MEDLINE=86269072; PubMed=2425809; DOI=10.1016/0006-2952(86)90577-0;
RA   Peterson T.C., Gonzalez F.J., Nebert D.W.;
RT   "Methylation differences in the murine P-1-450 and P-3-450 genes in
RT   wild-type and mutant hepatoma cell culture.";
RL   Biochem. Pharmacol. 35:2107-2114(1986).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
CC       monooxygenases. In liver microsomes, this enzyme is involved in an
CC       NADPH-dependent electron transport pathway. It oxidizes a variety
CC       of structurally unrelated compounds, including steroids, fatty
CC       acids, and xenobiotics.
CC   -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH +
CC       oxidized flavoprotein + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: By 3-methylcholanthrene (3MC).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Y00071; CAA68277.1; -; mRNA.
DR   EMBL; X01681; CAA25836.1; -; Genomic_DNA.
DR   EMBL; K02588; AAA37506.1; ALT_INIT; mRNA.
DR   EMBL; M10021; AAA37507.1; -; Genomic_DNA.
DR   EMBL; AK005000; BAB23734.1; -; mRNA.
DR   EMBL; M25623; AAA39868.1; -; Genomic_DNA.
DR   IPI; IPI00128286; -.
DR   PIR; A23923; O4MSM1.
DR   RefSeq; NP_001129531.1; -.
DR   RefSeq; NP_034122.1; -.
DR   UniGene; Mm.14089; -.
DR   HSSP; P00179; 1DT6.
DR   SMR; P00184; 37-513.
DR   PhosphoSite; P00184; -.
DR   PRIDE; P00184; -.
DR   Ensembl; ENSMUSG00000032315; Mus musculus.
DR   GeneID; 13076; -.
DR   KEGG; mmu:13076; -.
DR   MGI; MGI:88588; Cyp1a1.
DR   HOGENOM; P00184; -.
DR   HOVERGEN; P00184; -.
DR   OMA; P00184; KEHYRTF.
DR   BRENDA; 1.14.14.1; 244.
DR   NextBio; 283020; -.
DR   ArrayExpress; P00184; -.
DR   Bgee; P00184; -.
DR   GermOnline; ENSMUSG00000032315; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0070330; F:aromatase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0009308; P:cellular amine metabolic process; IMP:MGI.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009404; P:toxin metabolic process; IMP:MGI.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   PANTHER; PTHR19383:SF63; Cyt_P450_E_grp-I_CYP1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01683; EP450ICYP1A.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron;
KW   Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW   Phosphoprotein.
FT   CHAIN         1    524       Cytochrome P450 1A1.
FT                                /FTId=PRO_0000051631.
FT   METAL       461    461       Iron (heme axial ligand) (By similarity).
FT   MOD_RES     364    364       Phosphoserine (By similarity).
SQ   SEQUENCE   524 AA;  59230 MW;  E31D9E9CBA7B2B02 CRC64;
     MPSMYGLPAF VSATELLLAV TVFCLGFWVV RATRTWVPKG LKTPPGPWGL PFIGHMLTVG
     KNPHLSLTRL SQQYGDVLQI RIGSTPVVVL SGLNTIKQAL VRQGDDFKGR PDLYSFTLIT
     NGKSMTFNPD SGPVWAARRR LAQNALKSFS IASDPTSASS CYLEEHVSKE ANYLVSKLQK
     VMAEVGHFDP YKYLVVSVAN VICAICFGQR YDHDDQELLS IVNLSNEFGE VTGSGYPADF
     IPVLRYLPNS SLDAFKDLND KFYSFMKKLI KEHYRTFEKG HIRDITDSLI EHCQDRKLDE
     NANVQLSDDK VITIVLDLFG AGFDTVTTAI SWSLMYLVTN PRVQRKIQEE LDTVIGRDRQ
     PRLSDRPQLP YLEAFILETF RHSSFVPFTI PHSTTRDTSL NGFYIPKGCC VFVNQWQVNH
     DRELWGDPNE FRPERFLTPS GTLDKRLSEK VTLFGLGKRK CIGETIGRSE VFLFLAILLQ
     QIEFKVSPGE KVDMTPTYGL TLKHARCEHF QVQMRSSGPQ HLQA
//