CP3A1_RAT
ID CP3A1_RAT Reviewed; 504 AA.
AC P04800; Q64580;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cytochrome P450 3A1;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA1;
DE AltName: Full=Cytochrome P450-PCN1;
GN Name=Cyp3a1; Synonyms=Cyp3a-1;
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=3838989; DOI=10.1016/s0021-9258(17)39626-6;
RA Gonzalez F.J., Nebert D.W., Hardwick J.P., Kasper C.B.;
RT "Complete cDNA and protein sequence of a pregnenolone 16 alpha-
RT carbonitrile-induced cytochrome P-450. A representative of a new gene
RT family.";
RL J. Biol. Chem. 260:7435-7441(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=1731631; DOI=10.1016/0003-9861(92)90377-9;
RA Ribeiro V., Lechner M.C.;
RT "Cloning and characterization of a novel CYP3A1 allelic variant: analysis
RT of CYP3A1 and CYP3A2 sex-hormone-dependent expression reveals that the
RT CYP3A2 gene is regulated by testosterone.";
RL Arch. Biochem. Biophys. 293:147-152(1992).
RN [3]
RP PROTEIN SEQUENCE OF 1-26.
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 [4]
RP PROTEIN SEQUENCE OF 1-25.
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
RX PubMed=1372436; DOI=10.1073/pnas.89.6.2145;
RA Burger H.J., Schuetz J.D., Schuetz E.G., Guzelian P.S.;
RT "Paradoxical transcriptional activation of rat liver cytochrome P-450 3A1
RT by dexamethasone and the antiglucocorticoid pregnenolone 16 alpha-
RT carbonitrile: analysis by transient transfection into primary monolayer
RT cultures of adult rat hepatocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2145-2149(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 1-24.
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).
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 -!- INDUCTION: By pregnenolone 16-alpha-carbonitrile (PNCN).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M10161; AAA41035.1; -; mRNA.
DR EMBL; X64401; CAA45743.1; -; mRNA.
DR EMBL; M86850; AAA41780.1; -; Genomic_DNA.
DR EMBL; X62086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A22631; A22631.
DR AlphaFoldDB; P04800; -.
DR SMR; P04800; -.
DR STRING; 10116.ENSRNOP00000041138; -.
DR BindingDB; P04800; -.
DR ChEMBL; CHEMBL3323; -.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB01645; Genistein.
DR DrugBank; DB00603; Medroxyprogesterone acetate.
DR DrugBank; DB08834; Tauroursodeoxycholic acid.
DR iPTMnet; P04800; -.
DR PhosphoSitePlus; P04800; -.
DR PaxDb; P04800; -.
DR RGD; 628626; Cyp3a1.
DR eggNOG; KOG0158; Eukaryota.
DR InParanoid; P04800; -.
DR PhylomeDB; P04800; -.
DR BRENDA; 1.14.14.1; 5301.
DR Reactome; R-RNO-211981; Xenobiotics.
DR Reactome; R-RNO-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-RNO-9027307; Biosynthesis of maresin-like SPMs.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR Reactome; R-RNO-9754706; Atorvastatin ADME.
DR SABIO-RK; P04800; -.
DR PRO; PR:P04800; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0032451; F:demethylase activity; IDA:RGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050649; F:testosterone 6-beta-hydroxylase activity; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0070989; P:oxidative demethylation; IDA:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0010038; P:response to metal ion; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP: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 3A1"
FT /id="PRO_0000051783"
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 VARIANT 207
FT /note="T -> A (in strain: Wistar)"
FT VARIANT 213
FT /note="F -> I (in strain: Wistar)"
FT VARIANT 232
FT /note="I -> V (in strain: Wistar)"
SQ SEQUENCE 504 AA; 57918 MW; CFD5AC8C37E9CADB CRC64;
MDLLSALTLE TWVLLAVVLV LLYGFGTRTH GLFKKQGIPG PKPLPFFGTV LNYYMGLWKF
DVECHKKYGK IWGLFDGQMP LFAITDTEMI KNVLVKECFS VFTNRRDFGP VGIMGKAVSV
AKDEEWKRYR ALLSPTFTSG RLKEMFPIIE QYGDILVKYL KQEAETGKPV TMKKVFGAYS
MDVITSTSFG VNVDSLNNPK DPFVEKTKKL LRFDFFDPLF LSVVLFPFLT PIYEMLNICM
FPKDSIEFFK KFVYRMKETR LDSVQKHRVD FLQLMMNAHN DSKDKESHTA LSDMEITAQS
IIFIFAGYEP TSSTLSFVLH SLATHPDTQK KLQEEIDRAL PNKAPPTYDT VMEMEYLDMV
LNETLRLYPI GNRLERVCKK DVEINGVFMP KGSVVMIPSY ALHRDPQHWP EPEEFRPERF
SKENKGSIDP YVYLPFGNGP RNCIGMRFAL MNMKLALTKV LQNFSFQPCK ETQIPLKLSR
QGLLQPTKPI ILKVVPRDEI ITGS
