ID   CP3A9_RAT               Reviewed;         503 AA.
AC   P51538; Q64557; Q64631;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   04-NOV-2026, entry version 152.
DE   RecName: Full=Cytochrome P450 3A9;
DE            EC=1.14.14.1;
DE   AltName: Full=3AH15;
DE   AltName: Full=CYPIIIA9;
DE   AltName: Full=Cytochrome P450 olfactive 3;
DE   AltName: Full=Cytochrome P450-OLF3;
GN   Name=Cyp3a9; Synonyms=Cyp3a13;
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].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=8990268; DOI=10.1006/abbi.1996.9752;
RA   Mahnke A., Strotkamp D., Roos P.H., Hanstein W.G., Chabot G.G., Nef P.;
RT   "Expression and inducibility of cytochrome P450 3A9 (CYP3A9) and other
RT   members of the CYP3A subfamily in rat liver.";
RL   Arch. Biochem. Biophys. 337:62-68(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8660328; DOI=10.1006/bbrc.1996.0562;
RA   Wang H., Kawashima H., Strobel H.W.;
RT   "cDNA cloning of a novel CYP3A from rat brain.";
RL   Biochem. Biophys. Res. Commun. 221:157-162(1996).
CC   -!- FUNCTION: This isozyme seems to be implicated in olfaction. Active in
CC       the demethylation of erythromycin as well as benzphetamine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + reduced [NADPH--hemoprotein reductase] +
CC         O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O +
CC         H(+); 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: Mainly expressed in olfactory epithelium.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U60085; AAB03662.1; -; mRNA.
DR   EMBL; U46118; AAC52582.1; -; mRNA.
DR   PIR; JC4702; JC4702.
DR   SMR; P51538; -.
DR   STRING; 10116.ENSRNOP00000067681; -.
DR   ChEMBL; CHEMBL3430866; -.
DR   PhosphoSitePlus; P51538; -.
DR   PaxDb; 10116-ENSRNOP00000067681; -.
DR   UCSC; RGD:708392; rat.
DR   AGR; RGD:708392; -.
DR   RGD; 708392; Cyp3a9.
DR   InParanoid; P51538; -.
DR   OMA; ADKYDRP; -.
DR   PhylomeDB; P51538; -.
DR   Reactome; R-RNO-211945; Phase I - Functionalization of compounds.
DR   Reactome; R-RNO-211958; Miscellaneous substrates.
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   Reactome; R-RNO-9757110; Prednisone ADME.
DR   PRO; PR:P51538; -.
DR   CDD; cd20650; CYP3A; 1.
DR   FunFam; 1.10.630.10:FF:000096; Cytochrome P450 3A4; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   InterPro; IPR050705; Cytochrome_P450_3A.
DR   PANTHER; PTHR24302:SF38; CYTOCHROME P450 3A5; 1.
DR   PANTHER; PTHR24302; CYTOCHROME P450 FAMILY 3; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01689; EP450IICYP3A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
DR   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; ISO:RGD.
DR   GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; ISO:RGD.
DR   GO; GO:0008395; F:steroid hydroxylase activity; TAS:RGD.
DR   GO; GO:0050649; F:testosterone 6-beta-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:0007565; P:female pregnancy; IEP:RGD.
DR   GO; GO:0002933; P:lipid hydroxylation; ISO:RGD.
DR   GO; GO:0070989; P:oxidative demethylation; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR   GO; GO:0042573; P:retinoic acid metabolic process; ISO:RGD.
DR   GO; GO:0008202; P:steroid metabolic process; ISO:RGD.
DR   GO; GO:0042178; P:xenobiotic catabolic process; ISO:RGD.
DR   GO; GO:0042908; P:xenobiotic transport; ISO:RGD.
DR   Proteomes; UP000002494; Unplaced.
DR   AlphaFoldDB; P51538; -.
DR   FunCoup; P51538; 53.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Olfaction; Oxidoreductase; Reference proteome;
KW   Sensory transduction.
FT   CHAIN           1..503
FT                   /note="Cytochrome P450 3A9"
FT                   /id="PRO_0000051792"
FT   BINDING         442
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                   /evidence="ECO:0000250"
FT   CONFLICT        457
FT                   /note="F -> V (in Ref. 2; AAC52582)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  57812 MW;  9BBB13E690675EB4 CRC64;
     MDLIPNFSME TWLLLVISLV LLYLYGTHSH GIFKKLGIPG PKPLPFLGTI LAYRKGFWEF
     DKYCHKKYGK LWGLYDGRQP VLAITDPDII KTVLVKECYS TFTNRRNFGP VGILKKAISI
     SEDEEWKRIR ALLSPTFTSG KLKEMFPIIN QYTDMLVRNM RQGSEEGKPT SMKDIFGAYS
     MDVITATSFG VNVDSLNNPQ DPFVEKVKKL LKFDIFDPLF LSVTLFPFLT PLFEALNVSM
     FPRDVIDFFK TSVERMKENR MKEKEKQRMD FLQLMINSQN SKVKDSHKAL SDVEIVAQSV
     IFIFAGYETT SSALSFVLYL LAIHPDIQKK LQDEIDAALP NKAHATYDTL LQMEYLDMVV
     NETLRLYPIA GRLERVCKTD VEINGVFIPK GTVVMIPTFA LHKDPHYWPE PEEFRPERFS
     KKNQDNINPY MYLPFGNGPR NCIGMRFALM NMKVALFRVL QNFSFQPCKE TQIPLKLSKQ
     GLLQPEKPLL LKVVSRDETV NGA
//