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Cytochrome P450 1A1 (CYP1A1) (EC 1.14.14.1) (CYPIA1) (Cytochrome P450-C) (Cytochrome P450MT2) [Cleaved into: Cytochrome P450MT2A; Cytochrome P450MT2B]

 CP1A1_RAT               Reviewed;         524 AA.
P00185;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
12-SEP-2018, entry version 165.
RecName: Full=Cytochrome P450 1A1;
Short=CYP1A1;
EC=1.14.14.1;
AltName: Full=CYPIA1;
AltName: Full=Cytochrome P450-C;
AltName: Full=Cytochrome P450MT2;
Contains:
RecName: Full=Cytochrome P450MT2A;
Contains:
RecName: Full=Cytochrome P450MT2B;
Name=Cyp1a1; Synonyms=Cyp1a-1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6089174; DOI=10.1073/pnas.81.16.5066;
Sogawa K., Gotoh O., Kawajiri K., Fujii-Kuriyama Y.;
"Distinct organization of methylcholanthrene- and phenobarbital-
inducible cytochrome P-450 genes in the rat.";
Proc. Natl. Acad. Sci. U.S.A. 81:5066-5070(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6324135; DOI=10.1093/nar/12.6.2929;
Yabusaki Y., Shimizu M., Murakami H., Nakamura K., Oeda K., Ohkawa H.;
"Nucleotide sequence of a full-length cDNA coding for 3-
methylcholanthrene-induced rat liver cytochrome P-450MC.";
Nucleic Acids Res. 12:2929-2938(1984).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3838427; DOI=10.1016/0003-9861(85)90300-5;
Hines R.N., Levy J.B., Conrad R.D., Iversen P.L., Shen M.-L.,
Renli A.M., Bresnick E.;
"Gene structure and nucleotide sequence for rat cytochrome P-450c.";
Arch. Biochem. Biophys. 237:465-476(1985).
[4]
PROTEIN SEQUENCE OF 2-26.
PubMed=3718958; DOI=10.1021/bi00357a015;
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).
[5]
PROTEIN SEQUENCE OF 2-22.
PubMed=3041969; DOI=10.1016/0006-2952(88)90634-X;
Amelizad Z., Narbonne J.F., Wolf C.R., Robertson L.W., Oesch F.;
"Effect of nutritional imbalances on cytochrome P-450 isozymes in rat
liver.";
Biochem. Pharmacol. 37:3245-3249(1988).
[6]
PARTIAL PROTEIN SEQUENCE.
PubMed=8651689; DOI=10.1006/abbi.1996.0236;
Cvrk T., Hodek P., Strobel H.W.;
"Identification and characterization of cytochrome P4501A1 amino acid
residues interacting with a radiolabeled photoaffinity diazido-
benzphetamine analogue.";
Arch. Biochem. Biophys. 330:142-152(1996).
[7]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 32-VAL-THR-33.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=9348277; DOI=10.1083/jcb.139.3.589;
Addya S., Anandatheerthavarada H.K., Biswas G., Bhagwat S.V.,
Mullick J., Avadhani N.G.;
"Targeting of NH2-terminal-processed microsomal protein to
mitochondria: a novel pathway for the biogenesis of hepatic
mitochondrial P450MT2.";
J. Cell Biol. 139:589-599(1997).
[8]
GLYCOSYLATION AT SER-71.
PubMed=24098488; DOI=10.1371/journal.pone.0076399;
Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.;
"Discovery and confirmation of O-GlcNAcylated proteins in rat liver
mitochondria by combination of mass spectrometry and immunological
methods.";
PLoS ONE 8:E76399-E76399(2013).
-!- 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 NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Cytochrome P450 1A1: Cytoplasm.
-!- SUBCELLULAR LOCATION: Cytochrome P450MT2A: Endoplasmic reticulum
membrane. Mitochondrion membrane. Microsome membrane.
-!- SUBCELLULAR LOCATION: Cytochrome P450MT2B: Endoplasmic reticulum.
Mitochondrion.
-!- TISSUE SPECIFICITY: Liver.
-!- INDUCTION: By 3-methylcholanthrene (3MC) and beta-naphthoflavone
(BNF).
-!- DOMAIN: Contains a chimeric signal that facilitates targeting of
the protein to both the endoplasmic reticulum and mitochondria. A
12 amino acid sequence between 33 and 44 functions as a putative
mitochondrial-targeting signal. The removal of the first 4- or 32-
amino acid residues from the intact protein positions the
mitochondrial targeting signal for efficient binding to the
mitochondrial import receptors. The membrane-free P4501A1 seems to
be more sensitive to proteolysis.
-!- PTM: Two forms; MT2A (long form) and MT2B (short form); are
produced by NH2-terminal proteolytic cleavage. This cleavage
activates a cryptic mitochondrial targeting signal.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; K02246; AAA41027.1; -; Genomic_DNA.
EMBL; X00469; CAA25153.1; -; mRNA.
EMBL; M26129; AAA41025.1; -; Genomic_DNA.
PIR; A00185; O4RTMC.
RefSeq; NP_036672.2; NM_012540.2.
RefSeq; XP_006243212.1; XM_006243150.2.
UniGene; Rn.10352; -.
ProteinModelPortal; P00185; -.
SMR; P00185; -.
BioGrid; 246477; 2.
STRING; 10116.ENSRNOP00000026473; -.
BindingDB; P00185; -.
ChEMBL; CHEMBL2922; -.
SwissLipids; SLP:000001590; -.
iPTMnet; P00185; -.
PhosphoSitePlus; P00185; -.
PaxDb; P00185; -.
PRIDE; P00185; -.
Ensembl; ENSRNOT00000026473; ENSRNOP00000026473; ENSRNOG00000019500.
GeneID; 24296; -.
KEGG; rno:24296; -.
UCSC; RGD:2458; rat.
CTD; 1543; -.
RGD; 2458; Cyp1a1.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00900000140831; -.
HOVERGEN; HBG106944; -.
InParanoid; P00185; -.
KO; K07408; -.
OMA; NNWQDYI; -.
OrthoDB; EOG091G0BT8; -.
PhylomeDB; P00185; -.
TreeFam; TF105095; -.
Reactome; R-RNO-211981; Xenobiotics.
Reactome; R-RNO-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
Reactome; R-RNO-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
Reactome; R-RNO-9018681; Biosynthesis of protectins.
SABIO-RK; P00185; -.
PRO; PR:P00185; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000019500; Expressed in 6 organ(s), highest expression level in lung.
Genevisible; P00185; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0003824; F:catalytic activity; IDA:RGD.
GO; GO:0032451; F:demethylase activity; IDA:RGD.
GO; GO:0019899; F:enzyme binding; IDA:RGD.
GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; IEA:Ensembl.
GO; GO:0016711; F:flavonoid 3'-monooxygenase activity; IDA:RGD.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IDA:RGD.
GO; GO:0016491; F:oxidoreductase activity; IDA:RGD.
GO; GO:0016679; F:oxidoreductase activity, acting on diphenols and related substances as donors; IDA:RGD.
GO; GO:0008395; F:steroid hydroxylase activity; IDA:RGD.
GO; GO:0070576; F:vitamin D 24-hydroxylase activity; IEA:Ensembl.
GO; GO:0042904; P:9-cis-retinoic acid biosynthetic process; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0009308; P:amine metabolic process; IEA:Ensembl.
GO; GO:0043010; P:camera-type eye development; IEP:RGD.
GO; GO:0008283; P:cell proliferation; IEP:RGD.
GO; GO:0071280; P:cellular response to copper ion; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0009804; P:coumarin metabolic process; IDA:RGD.
GO; GO:0032502; P:developmental process; IEP:RGD.
GO; GO:0019341; P:dibenzo-p-dioxin catabolic process; IDA:RGD.
GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IDA:RGD.
GO; GO:0048565; P:digestive tract development; IEP:RGD.
GO; GO:0009812; P:flavonoid metabolic process; IDA:RGD.
GO; GO:0070365; P:hepatocyte differentiation; IEP:RGD.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
GO; GO:0017143; P:insecticide metabolic process; IDA:RGD.
GO; GO:0002933; P:lipid hydroxylation; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0060137; P:maternal process involved in parturition; IEP:RGD.
GO; GO:0006778; P:porphyrin-containing compound metabolic process; IDA:RGD.
GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:RGD.
GO; GO:0046677; P:response to antibiotic; IEP:RGD.
GO; GO:0046685; P:response to arsenic-containing substance; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032094; P:response to food; IEP:RGD.
GO; GO:0009635; P:response to herbicide; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
GO; GO:0010041; P:response to iron(III) ion; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0009624; P:response to nematode; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0009615; P:response to virus; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
GO; GO:0009611; P:response to wounding; IEP:RGD.
GO; GO:0008202; P:steroid metabolic process; IEA:Ensembl.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR01683; EP450ICYP1A.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing;
Endoplasmic reticulum; Glycoprotein; Heme; Iron; Membrane;
Metal-binding; Microsome; Mitochondrion; Monooxygenase;
Oxidoreductase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000305}.
CHAIN 2 524 Cytochrome P450 1A1.
/FTId=PRO_0000003564.
CHAIN 5 524 Cytochrome P450MT2A.
/FTId=PRO_0000003565.
CHAIN 33 524 Cytochrome P450MT2B.
/FTId=PRO_0000003566.
REGION 33 44 Mitochondrial targeting signal.
METAL 461 461 Iron (heme axial ligand).
BINDING 228 228 Substrate. {ECO:0000250}.
CARBOHYD 71 71 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:24098488}.
MUTAGEN 32 33 VT->AI: No proteolytic cleavage.
{ECO:0000269|PubMed:9348277}.
CONFLICT 21 22 TT -> VV (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 53 53 I -> M (in Ref. 2; CAA25153).
{ECO:0000305}.
CONFLICT 494 494 M -> S (in Ref. 3; AAA41025).
{ECO:0000305}.
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


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