CP3A2_RAT
ID CP3A2_RAT Reviewed; 504 AA.
AC P05183; Q5FVU5; Q64629; Q64672;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cytochrome P450 3A2;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA2;
DE AltName: Full=Cytochrome P450-PCN2;
DE AltName: Full=Cytochrome P450/6-beta-A;
DE AltName: Full=Testosterone 6-beta-hydroxylase;
GN Name=Cyp3a2; Synonyms=Cyp3a-2, Cyp3a11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3785219; DOI=10.1128/mcb.6.8.2969-2976.1986;
RA Gonzalez F.J., Song B.-J., Hardwick J.P.;
RT "Pregnenolone 16 alpha-carbonitrile-inducible P-450 gene family: gene
RT conversion and differential regulation.";
RL Mol. Cell. Biol. 6:2969-2976(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2043144; DOI=10.1016/0006-291x(91)91949-d;
RA Miyata M., Nagata K., Yamazoe Y., Kato R.;
RT "A gene structure of testosterone 6 beta-hydroxylase (P450IIIA).";
RL Biochem. Biophys. Res. Commun. 177:68-73(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7979376; DOI=10.1006/abbi.1994.1453;
RA Miyata M., Nagata K., Shimada M., Yamazoe Y., Kato R.;
RT "Structure of a gene and cDNA of a major constitutive form of testosterone
RT 6 beta-hydroxylase (P450/6 beta A) encoding CYP3A2: comparison of the cDNA
RT with P450PCN2.";
RL Arch. Biochem. Biophys. 314:351-359(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-36, AND INDUCTION.
RC TISSUE=Liver;
RX PubMed=1417000; DOI=10.1016/0003-9861(92)90471-8;
RA Telhada M.B., Pereira T.M., Lechner M.C.;
RT "Effect of dexamethasone and phenobarbital on run-on transcription rate and
RT CYP3A mRNA concentration in rat liver: changes during development.";
RL Arch. Biochem. Biophys. 298:715-725(1992).
RN [6]
RP PROTEIN SEQUENCE OF 1-33, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Liver;
RX PubMed=2398038; DOI=10.1093/oxfordjournals.jbchem.a123115;
RA Nagata K., Gonzalez F.J., Yamazoe Y., Kato R.;
RT "Purification and characterization of four catalytically active
RT testosterone 6 beta-hydroxylase P-450s from rat liver microsomes:
RT comparison of a novel form with three structurally and functionally related
RT forms.";
RL J. Biochem. 107:718-725(1990).
RN [7]
RP PROTEIN SEQUENCE OF 1-25, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=7681660; DOI=10.1006/abbi.1993.1154;
RA Cooper K.O., Reik L.M., Jayyosi Z., Bandiera S., Kelley M., Ryan D.E.,
RA Daniel R., McCluskey S.A., Levin W., Thomas P.E.;
RT "Regulation of two members of the steroid-inducible cytochrome P450
RT subfamily (3A) in rats.";
RL Arch. Biochem. Biophys. 301:345-354(1993).
CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC In liver microsomes, this enzyme is involved in an NADPH-dependent
CC electron transport pathway. It oxidizes a variety of structurally
CC unrelated compounds, including steroids, fatty acids, and xenobiotics.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein. Microsome membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:2398038,
CC ECO:0000269|PubMed:7681660}.
CC -!- INDUCTION: By pregnenolone 16-alpha-carbonitrile (PNCN) and
CC dexamethasone. {ECO:0000269|PubMed:1417000, ECO:0000269|PubMed:2398038,
CC ECO:0000269|PubMed:7681660}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M13646; AAA41051.1; -; mRNA.
DR EMBL; X79319; CAA55887.1; -; Genomic_DNA.
DR EMBL; X79320; CAA55888.1; -; mRNA.
DR EMBL; U09742; AAA82168.1; -; mRNA.
DR EMBL; U09734; AAB60492.1; -; Genomic_DNA.
DR EMBL; U09725; AAB60492.1; JOINED; Genomic_DNA.
DR EMBL; U09726; AAB60492.1; JOINED; Genomic_DNA.
DR EMBL; U09727; AAB60492.1; JOINED; Genomic_DNA.
DR EMBL; U09728; AAB60492.1; JOINED; Genomic_DNA.
DR EMBL; U09729; AAB60492.1; JOINED; Genomic_DNA.
DR EMBL; U09730; AAB60492.1; JOINED; Genomic_DNA.
DR EMBL; U09731; AAB60492.1; JOINED; Genomic_DNA.
DR EMBL; U09732; AAB60492.1; JOINED; Genomic_DNA.
DR EMBL; U09733; AAB60492.1; JOINED; Genomic_DNA.
DR EMBL; BC089765; AAH89765.1; -; mRNA.
DR PIR; A25222; A25222.
DR RefSeq; NP_695224.2; NM_153312.2.
DR AlphaFoldDB; P05183; -.
DR SMR; P05183; -.
DR BindingDB; P05183; -.
DR ChEMBL; CHEMBL3324; -.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB13975; Black cohosh.
DR DrugBank; DB00869; Dorzolamide.
DR DrugBank; DB01645; Genistein.
DR DrugBank; DB08834; Tauroursodeoxycholic acid.
DR iPTMnet; P05183; -.
DR PhosphoSitePlus; P05183; -.
DR PaxDb; P05183; -.
DR PRIDE; P05183; -.
DR GeneID; 266682; -.
DR KEGG; rno:266682; -.
DR CTD; 266682; -.
DR RGD; 708379; Cyp3a2.
DR InParanoid; P05183; -.
DR OrthoDB; 467733at2759; -.
DR PhylomeDB; P05183; -.
DR Reactome; R-RNO-211981; Xenobiotics.
DR Reactome; R-RNO-5423646; Aflatoxin activation and detoxification.
DR SABIO-RK; P05183; -.
DR PRO; PR:P05183; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0062181; F:1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity; ISO:RGD.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034875; F:caffeine oxidase activity; ISO:RGD.
DR GO; GO:0032451; F:demethylase activity; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; ISO:RGD.
DR GO; GO:0101021; F:estrogen 2-hydroxylase activity; ISO:RGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; ISO:RGD.
DR GO; GO:0004497; F:monooxygenase activity; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; ISO:RGD.
DR GO; GO:0005496; F:steroid binding; ISO:RGD.
DR GO; GO:0008395; F:steroid hydroxylase activity; ISO:RGD.
DR GO; GO:0050649; F:testosterone 6-beta-hydroxylase activity; IMP:RGD.
DR GO; GO:0070576; F:vitamin D 24-hydroxylase activity; ISO:RGD.
DR GO; GO:0030343; F:vitamin D3 25-hydroxylase activity; ISO:RGD.
DR GO; GO:0009822; P:alkaloid catabolic process; ISO:RGD.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:RGD.
DR GO; GO:0046483; P:heterocycle metabolic process; ISO:RGD.
DR GO; GO:0002933; P:lipid hydroxylation; ISO:RGD.
DR GO; GO:0016098; P:monoterpenoid metabolic process; ISO:RGD.
DR GO; GO:0070989; P:oxidative demethylation; IDA:RGD.
DR GO; GO:0042573; P:retinoic acid metabolic process; ISO:RGD.
DR GO; GO:0042572; P:retinol metabolic process; ISO:RGD.
DR GO; GO:0006706; P:steroid catabolic process; ISO:RGD.
DR GO; GO:0008202; P:steroid metabolic process; ISO:RGD.
DR GO; GO:0042369; P:vitamin D catabolic process; ISO:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:RGD.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR008072; Cyt_P450_E_CYP3A.
DR InterPro; IPR002402; Cyt_P450_E_grp-II.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00464; EP450II.
DR PRINTS; PR01689; EP450IICYP3A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..504
FT /note="Cytochrome P450 3A2"
FT /id="PRO_0000051784"
FT BINDING 443
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT CONFLICT 56..57
FT /note="GL -> AV (in Ref. 2; CAA55887)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="D -> H (in Ref. 1; AAA41051)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="G -> D (in Ref. 1; AAA41051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 57732 MW; C2C84AF736035AB2 CRC64;
MDLLSALTLE TWVLLAVILV LLYRLGTHRH GIFKKQGIPG PKPLPFLGTV LNYYKGLGRF
DMECYKKYGK IWGLFDGQTP VFAIMDTEMI KNVLVKECFS VFTNRRDFGP VGIMGKAVSV
AKDEEWKRYR ALLSPTFTSG RLKEMFPIIE QYGDILVKYL KQEAETGKPV TMKKVFGAYS
MDVITSTSFG VNVDSLNNPK DPFVEKTKKL LRFDFFDPLF LSVVLFPFLT PIYEMLNICM
FPKDSIAFFQ KFVHRIKETR LDSKHKHRVD FLQLMLNAHN NSKDEVSHKA LSDVEIIAQS
VIFIFAGYET TSSTLSFVLY FLATHPDIQK KLQEEIDGAL PSKAPPTYDI VMEMEYLDMV
LNETLRLYPI GNRLERVCKK DIELDGLFIP KGSVVTIPTY ALHHDPQHWP KPEEFHPERF
SKENKGSIDP YVYLPFGNGP RNCIGMRFAL MNMKLALTKV LQNFSFQPCK ETQIPLKLSR
QAILEPEKPI VLKVLPRDAV INGA
