CP3A9_RAT
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 03-AUG-2022, entry version 136.
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 + 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: 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 AlphaFoldDB; P51538; -.
DR SMR; P51538; -.
DR STRING; 10116.ENSRNOP00000067681; -.
DR ChEMBL; CHEMBL3430866; -.
DR UCSC; RGD:708392; rat.
DR RGD; 708392; Cyp3a9.
DR InParanoid; P51538; -.
DR PhylomeDB; P51538; -.
DR Reactome; R-RNO-211958; Miscellaneous substrates.
DR Reactome; R-RNO-211981; Xenobiotics.
DR PRO; PR:P51538; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0101020; F:estrogen 16-alpha-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:0008401; F:retinoic acid 4-hydroxylase activity; ISO:RGD.
DR GO; GO:0008395; F:steroid hydroxylase activity; TAS: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:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; ISO:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO: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 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
