ID   CP1A1_RAT               Reviewed;         524 AA.
AC   P00185;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   16-JUN-2009, entry version 94.
DE   RecName: Full=Cytochrome P450 1A1;
DE            Short=CYP1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
DE   AltName: Full=P450-C;
DE   AltName: Full=P450MT2;
DE   Contains:
DE     RecName: Full=Cytochrome P450MT2A;
DE   Contains:
DE     RecName: Full=Cytochrome P450MT2B;
GN   Name=Cyp1a1; Synonyms=Cyp1a-1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=84298082; PubMed=6089174; DOI=10.1073/pnas.81.16.5066;
RA   Sogawa K., Gotoh O., Kawajiri K., Fujii-Kuriyama Y.;
RT   "Distinct organization of methylcholanthrene- and phenobarbital-
RT   inducible cytochrome P-450 genes in the rat.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5066-5070(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=84169583; PubMed=6324135; DOI=10.1093/nar/12.6.2929;
RA   Yabusaki Y., Shimizu M., Murakami H., Nakamura K., Oeda K., Ohkawa H.;
RT   "Nucleotide sequence of a full-length cDNA coding for 3-
RT   methylcholanthrene-induced rat liver cytochrome P-450MC.";
RL   Nucleic Acids Res. 12:2929-2938(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=85147736; PubMed=3838427; DOI=10.1016/0003-9861(85)90300-5;
RA   Hines R.N., Levy J.B., Conrad R.D., Iversen P.L., Shen M.-L.,
RA   Renli A.M., Bresnick E.;
RT   "Gene structure and nucleotide sequence for rat cytochrome P-450c.";
RL   Arch. Biochem. Biophys. 237:465-476(1985).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-26.
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   [5]
RP   PROTEIN SEQUENCE OF 2-22.
RX   PubMed=3041969; DOI=10.1016/0006-2952(88)90634-X;
RA   Amelizad Z., Narbonne J.F., Wolf C.R., Robertson L.W., Oesch F.;
RT   "Effect of nutritional imbalances on cytochrome P-450 isozymes in rat
RT   liver.";
RL   Biochem. Pharmacol. 37:3245-3249(1988).
RN   [6]
RP   PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=96230251; PubMed=8651689; DOI=10.1006/abbi.1996.0236;
RA   Cvrk T., Hodek P., Strobel H.W.;
RT   "Identification and characterization of cytochrome P4501A1 amino acid
RT   residues interacting with a radiolabeled photoaffinity diazido-
RT   benzphetamine analogue.";
RL   Arch. Biochem. Biophys. 330:142-152(1996).
RN   [7]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   MEDLINE=98012193; PubMed=9348277; DOI=10.1083/jcb.139.3.589;
RA   Addya S., Anandatheerthavarada H.K., Biswas G., Bhagwat S.V.,
RA   Mullick J., Avadhani N.G.;
RT   "Targeting of NH2-terminal-processed microsomal protein to
RT   mitochondria: a novel pathway for the biogenesis of hepatic
RT   mitochondrial P450MT2.";
RL   J. Cell Biol. 139:589-599(1997).
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: Cytochrome P450 1A1: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Cytochrome P450MT2A: Endoplasmic reticulum
CC       membrane. Mitochondrion membrane. Microsome membrane.
CC   -!- SUBCELLULAR LOCATION: Cytochrome P450MT2B: Endoplasmic reticulum.
CC       Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- INDUCTION: By 3-methylcholanthrene (3MC) and beta-naphthoflavone
CC       (BNF).
CC   -!- DOMAIN: Contains a chimeric signal that facilitates targeting of
CC       the protein to both the endoplasmic reticulum and mitochondria. A
CC       12 amino acid sequence between 33 and 44 functions as a putative
CC       mitochondrial-targeting signal. The removal of the first 4- or 32-
CC       amino acid residues from the intact protein positions the
CC       mitochondrial targeting signal for efficient binding to the
CC       mitochondrial import receptors. The membrane-free P4501A1 seems to
CC       be more sensible to proteolysis.
CC   -!- PTM: Two forms; MT2A (long form) and MT2B (short form); are
CC       produced by NH2-terminal proteolytic cleavage. This cleavage
CC       activates a cryptic mitochondrial targeting signal.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; K02246; AAA41027.1; -; Genomic_DNA.
DR   EMBL; X00469; CAA25153.1; -; mRNA.
DR   EMBL; M26129; AAA41025.1; -; Genomic_DNA.
DR   IPI; IPI00206995; -.
DR   PIR; A00185; O4RTMC.
DR   RefSeq; NP_036672.2; -.
DR   UniGene; Rn.10352; -.
DR   HSSP; P00179; 1N6B.
DR   Ensembl; ENSRNOG00000019500; Rattus norvegicus.
DR   GeneID; 24296; -.
DR   KEGG; rno:24296; -.
DR   RGD; 2458; Cyp1a1.
DR   HOVERGEN; P00185; -.
DR   OMA; P00185; KEHYRTF.
DR   BRENDA; 1.14.14.1; 248.
DR   NextBio; 602902; -.
DR   ArrayExpress; P00185; -.
DR   GermOnline; ENSRNOG00000019500; Rattus norvegicus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IDA:RGD.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:EC.
DR   GO; GO:0032451; F:demethylase activity; IDA:RGD.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR   GO; GO:0016711; F:flavonoid 3'-monooxygenase activity; IDA:RGD.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016679; F:oxidoreductase activity, acting on diphenol...; IDA:RGD.
DR   GO; GO:0008395; F:steroid hydroxylase activity; IDA:RGD.
DR   GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:RGD.
DR   GO; GO:0043010; P:camera-type eye development; IEP:RGD.
DR   GO; GO:0008283; P:cell proliferation; IEP:RGD.
DR   GO; GO:0009804; P:coumarin metabolic process; IDA:RGD.
DR   GO; GO:0019341; P:dibenzo-p-dioxin catabolic process; IDA:RGD.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IEP:RGD.
DR   GO; GO:0009812; P:flavonoid metabolic process; IDA:RGD.
DR   GO; GO:0048565; P:gut development; IEP:RGD.
DR   GO; GO:0070365; P:hepatocyte differentiation; IEP:RGD.
DR   GO; GO:0017143; P:insecticide metabolic process; IDA:RGD.
DR   GO; GO:0060137; P:maternal process involved in parturition; IEP:RGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006778; P:porphyrin metabolic process; IDA:RGD.
DR   GO; GO:0045750; P:positive regulation of S phase of mitotic c...; IDA:RGD.
DR   GO; GO:0046677; P:response to antibiotic; IEP:RGD.
DR   GO; GO:0046685; P:response to arsenic; IEP:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0032094; P:response to food; IEP:RGD.
DR   GO; GO:0009635; P:response to herbicide; IEP:RGD.
DR   GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0010041; P:response to iron(III) ion; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0009624; P:response to nematode; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic substance; IEP:RGD.
DR   GO; GO:0009615; P:response to virus; IEP:RGD.
DR   GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR   GO; GO:0009611; P:response to wounding; IEP:RGD.
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   Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Heme;
KW   Iron; Membrane; Metal-binding; Microsome; Mitochondrion;
KW   Monooxygenase; Oxidoreductase; Phosphoprotein.
FT   CHAIN         2    524       Cytochrome P450 1A1.
FT                                /FTId=PRO_0000003564.
FT   CHAIN         5    524       Cytochrome P450MT2A.
FT                                /FTId=PRO_0000003565.
FT   CHAIN        33    524       Cytochrome P450MT2B.
FT                                /FTId=PRO_0000003566.
FT   REGION       33     44       Mitochondrial targeting signal.
FT   METAL       461    461       Iron (heme axial ligand).
FT   MOD_RES     364    364       Phosphoserine (By similarity).
FT   MUTAGEN      32     33       VT->AI: No proteolytic cleavage.
FT   CONFLICT     21     22       TT -> VV (in Ref. 5; AA sequence).
FT   CONFLICT     53     53       I -> M (in Ref. 2; CAA25153).
FT   CONFLICT    494    494       M -> S (in Ref. 3; AAA41025).
SQ   SEQUENCE   524 AA;  59393 MW;  C766DF8044D598C5 CRC64;
     MPSVYGFPAF TSATELLLAV TTFCLGFWVV RVTRTWVPKG LKSPPGPWGL PFIGHVLTLG
     KNPHLSLTKL SQQYGDVLQI RIGSTPVVVL SGLNTIKQAL VKQGDDFKGR PDLYSFTLIA
     NGQSMTFNPD SGPLWAARRR LAQNALKSFS IASDPTLASS CYLEEHVSKE AEYLISKFQK
     LMAEVGHFDP FKYLVVSVAN VICAICFGRR YDHDDQELLS IVNLSNEFGE VTGSGYPADF
     IPILRYLPNS SLDAFKDLNK KFYSFMKKLI KEHYRTFEKG HIRDITDSLI EHCQDRRLDE
     NANVQLSDDK VITIVFDLFG AGFDTITTAI SWSLMYLVTN PRIQRKIQEE LDTVIGRDRQ
     PRLSDRPQLP YLEAFILETF RHSSFVPFTI PHSTIRDTSL NGFYIPKGHC VFVNQWQVNH
     DQELWGDPNE FRPERFLTSS GTLDKHLSEK VILFGLGKRK CIGETIGRLE VFLFLAILLQ
     QMEFNVSPGE KVDMTPAYGL TLKHARCEHF QVQMRSSGPQ HLQA
//