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Cytochrome P450 1A2 (EC 1.14.14.1) (CYPIA2) (Cholesterol 25-hydroxylase) (Cytochrome P-448) (Cytochrome P-450d) (Cytochrome P450-D)

 CP1A2_RAT               Reviewed;         513 AA.
P04799; A1L120; Q64588;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
07-JUN-2017, entry version 152.
RecName: Full=Cytochrome P450 1A2;
EC=1.14.14.1 {ECO:0000250|UniProtKB:P05177};
AltName: Full=CYPIA2;
AltName: Full=Cholesterol 25-hydroxylase {ECO:0000250|UniProtKB:P05177};
AltName: Full=Cytochrome P-448;
AltName: Full=Cytochrome P-450d;
AltName: Full=Cytochrome P450-D;
Name=Cyp1a2; Synonyms=Cyp1a-2;
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 [MRNA].
PubMed=6584898; DOI=10.1073/pnas.81.6.1649;
Kawajiri K., Gotoh O., Sogawa K., Tagashira Y., Muramatsu M.,
Fujii-Kuriyama Y.;
"Coding nucleotide sequence of 3-methylcholanthrene-inducible
cytochrome P-450d cDNA from rat liver.";
Proc. Natl. Acad. Sci. U.S.A. 81:1649-1653(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2985574;
Sogawa K., Gotoh O., Kawajiri K., Harada T., Fujii-Kuriyama Y.;
"Complete nucleotide sequence of a methylcholanthrene-inducible
cytochrome P-450 (P-450d) gene in the rat.";
J. Biol. Chem. 260:5026-5032(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1793487; DOI=10.1002/mc.2940040613;
Wolfel C., Platt K.L., Dogra S., Glatt H., Wachter F., Doehmer J.;
"Stable expression of rat cytochrome P450IA2 cDNA and hydroxylation of
17 beta-estradiol and 2-aminofluorene in V79 Chinese hamster cells.";
Mol. Carcinog. 4:489-498(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=3947063; DOI=10.1016/0003-9861(86)90121-9;
Haniu M., Ryan D.E., Levin W., Shively J.E.;
"The primary structure of cytochrome P-450d purified from rat liver
microsomes: prediction of helical regions and domain analysis.";
Arch. Biochem. Biophys. 244:323-337(1986).
[6]
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).
[7]
PROTEIN SEQUENCE OF 2-20.
PubMed=7074072; DOI=10.1021/bi00535a007;
Botelho L.H., Ryan D.E., Yuan P.M., Kutny R., Shively J.E., Levin W.;
"Amino-terminal and carboxy-terminal sequence of hepatic microsomal
cytochrome P-450d, a unique hemoprotein from rats treated with
isosafrole.";
Biochemistry 21:1152-1155(1982).
[8]
PROTEIN SEQUENCE OF 67-78.
PubMed=1420171; DOI=10.1021/bi00158a019;
Yun C.H., Hammons G.J., Jones G., Martin M.V., Hopkins N.E.,
Alworth W.L., Guengerich F.P.;
"Modification of cytochrome P450 1A2 enzymes by the mechanism-based
inactivator 2-ethynylnaphthalene and the photoaffinity label 4-
azidobiphenyl.";
Biochemistry 31:10556-10563(1992).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 147-513.
PubMed=6548743;
Yabusaki Y., Murakami H., Nakamura K., Nomura N., Shimizu M., Oeda K.,
Ohkawa H.;
"Characterization of complementary DNA clones coding for two forms of
3-methylcholanthrene-inducible rat liver cytochrome P-450.";
J. Biochem. 96:793-804(1984).
[10]
GLYCOSYLATION AT SER-68.
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. Most active in catalyzing 2-hydroxylation.
{ECO:0000250|UniProtKB:P05177}.
-!- CATALYTIC ACTIVITY: RH + [reduced NADPH--hemoprotein reductase] +
O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
{ECO:0000250|UniProtKB:P05177}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane
{ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein.
-!- INDUCTION: By 3-methylcholanthrene (3MC).
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; K02422; AAA41028.1; -; mRNA.
EMBL; K03241; AAA41053.1; -; Genomic_DNA.
EMBL; BC127476; AAI27477.1; -; mRNA.
EMBL; X01031; CAA25516.1; -; mRNA.
PIR; A61400; A61400.
RefSeq; NP_036673.3; NM_012541.3.
UniGene; Rn.5563; -.
ProteinModelPortal; P04799; -.
SMR; P04799; -.
BioGrid; 246478; 1.
MINT; MINT-4564487; -.
STRING; 10116.ENSRNOP00000021653; -.
BindingDB; P04799; -.
ChEMBL; CHEMBL1075125; -.
iPTMnet; P04799; -.
PhosphoSitePlus; P04799; -.
PaxDb; P04799; -.
PRIDE; P04799; -.
Ensembl; ENSRNOT00000021653; ENSRNOP00000021653; ENSRNOG00000016173.
GeneID; 24297; -.
KEGG; rno:24297; -.
UCSC; RGD:2459; rat.
CTD; 1544; -.
RGD; 2459; Cyp1a2.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00880000137854; -.
HOVERGEN; HBG106944; -.
InParanoid; P04799; -.
KO; K07409; -.
OMA; IPAKWEV; -.
OrthoDB; EOG091G0BT8; -.
PhylomeDB; P04799; -.
BRENDA; 1.14.14.1; 5301.
Reactome; R-RNO-156581; Methylation.
Reactome; R-RNO-211957; Aromatic amines can be N-hydroxylated or N-dealkylated by CYP1A2.
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-5423646; Aflatoxin activation and detoxification.
SABIO-RK; P04799; -.
PRO; PR:P04799; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000016173; -.
Genevisible; P04799; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
GO; GO:0034875; F:caffeine oxidase activity; IEA:Ensembl.
GO; GO:0032451; F:demethylase activity; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IDA:RGD.
GO; GO:0016712; F: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; IDA:RGD.
GO; GO:0009820; P:alkaloid metabolic process; IEA:Ensembl.
GO; GO:0045333; P:cellular respiration; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0071280; P:cellular response to copper ion; IEP:RGD.
GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IEA:Ensembl.
GO; GO:0042738; P:exogenous drug catabolic process; IEA:Ensembl.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0032787; P:monocarboxylic acid metabolic process; IEA:Ensembl.
GO; GO:0016098; P:monoterpenoid metabolic process; IEA:Ensembl.
GO; GO:0071615; P:oxidative deethylation; IEA:Ensembl.
GO; GO:0070989; P:oxidative demethylation; IEA:Ensembl.
GO; GO:0006778; P:porphyrin-containing compound metabolic process; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; 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:0006706; P:steroid catabolic process; IEA:Ensembl.
GO; GO:0009403; P:toxin biosynthetic process; IEA:Ensembl.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:RGD.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
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; Direct protein sequencing; Endoplasmic reticulum;
Glycoprotein; Heme; Iron; Lipid metabolism; Membrane; Metal-binding;
Microsome; Monooxygenase; Oxidoreductase; Reference proteome;
Steroid metabolism; Sterol metabolism.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P56592}.
CHAIN 2 513 Cytochrome P450 1A2.
/FTId=PRO_0000051656.
METAL 456 456 Iron (heme axial ligand).
CARBOHYD 68 68 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:24098488}.
CONFLICT 26 26 V -> M (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 137 137 R -> H (in Ref. 2; AAA41053 and 3; no
nucleotide entry). {ECO:0000305}.
CONFLICT 185 185 F -> L (in Ref. 3; no nucleotide entry).
{ECO:0000305}.
CONFLICT 262 262 F -> S (in Ref. 1; AAA41028).
{ECO:0000305}.
CONFLICT 403 403 C -> R (in Ref. 2; AAA41053).
{ECO:0000305}.
SEQUENCE 513 AA; 58259 MW; B1F06FDE9B7B6FA7 CRC64;
MAFSQYISLA PELLLATAIF CLVFWVLRGT RTQVPKGLKS PPGPWGLPFI GHMLTLGKNP
HLSLTKLSQQ YGDVLQIRIG STPVVVLSGL NTIKQALVKQ GDDFKGRPDL YSFTLITNGK
SMTFNPDSGP VWAARRRLAQ DALKSFSIAS DPTSVSSCYL EEHVSKEANH LISKFQKLMA
EVGHFEPVNQ VVESVANVIG AMCFGKNFPR KSEEMLNLVK SSKDFVENVT SGNAVDFFPV
LRYLPNPALK RFKNFNDNFV LFLQKTVQEH YQDFNKNSIQ DITGALFKHS ENYKDNGGLI
PQEKIVNIVN DIFGAGFETV TTAIFWSILL LVTEPKVQRK IHEELDTVIG RDRQPRLSDR
PQLPYLEAFI LEIYRYTSFV PFTIPHSTTR DTSLNGFHIP KECCIFINQW QVNHDEKQWK
DPFVFRPERF LTNDNTAIDK TLSEKVMLFG LGKRRCIGEI PAKWEVFLFL AILLHQLEFT
VPPGVKVDLT PSYGLTMKPR TCEHVQAWPR FSK


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