CP3AD_MOUSE
ID CP3AD_MOUSE Reviewed; 503 AA.
AC Q64464;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cytochrome P450 3A13;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA13;
GN Name=Cyp3a13; Synonyms=Cyp3a-13;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ddY; TISSUE=Liver;
RX PubMed=7803471; DOI=10.1016/0304-4165(94)90069-8;
RA Yanagimoto T., Itoh S., Sawada M., Hashimoto H., Kamataki T.;
RT "Molecular cloning and functional expression of a mouse cytochrome P-450
RT (Cyp3a-13): examination of Cyp3a-13 enzyme to activate aflatoxin B1
RT (AFB1).";
RL Biochim. Biophys. Acta 1201:405-410(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Can activate aflatoxin B1 to a genotoxic product.
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: P450 can be induced to high levels in liver and other
CC tissues by various foreign compounds, including drugs, pesticides, and
CC carcinogens.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X63023; CAA44754.1; -; mRNA.
DR EMBL; BC046592; AAH46592.1; -; mRNA.
DR CCDS; CCDS19781.1; -.
DR PIR; S50211; S50211.
DR RefSeq; NP_031845.1; NM_007819.4.
DR AlphaFoldDB; Q64464; -.
DR SMR; Q64464; -.
DR STRING; 10090.ENSMUSP00000031741; -.
DR ChEMBL; CHEMBL3637781; -.
DR iPTMnet; Q64464; -.
DR PhosphoSitePlus; Q64464; -.
DR SwissPalm; Q64464; -.
DR jPOST; Q64464; -.
DR MaxQB; Q64464; -.
DR PaxDb; Q64464; -.
DR PRIDE; Q64464; -.
DR ProteomicsDB; 283931; -.
DR DNASU; 13113; -.
DR Ensembl; ENSMUST00000031741; ENSMUSP00000031741; ENSMUSG00000029727.
DR GeneID; 13113; -.
DR KEGG; mmu:13113; -.
DR UCSC; uc009aef.2; mouse.
DR CTD; 13113; -.
DR MGI; MGI:88610; Cyp3a13.
DR VEuPathDB; HostDB:ENSMUSG00000029727; -.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00950000182958; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q64464; -.
DR OMA; TCLEYRK; -.
DR OrthoDB; 467733at2759; -.
DR PhylomeDB; Q64464; -.
DR TreeFam; TF105087; -.
DR Reactome; R-MMU-211958; Miscellaneous substrates.
DR Reactome; R-MMU-211981; Xenobiotics.
DR BioGRID-ORCS; 13113; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Cyp3a13; mouse.
DR PRO; PR:Q64464; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q64464; protein.
DR Bgee; ENSMUSG00000029727; Expressed in small intestine Peyer's patch and 74 other tissues.
DR ExpressionAtlas; Q64464; baseline and differential.
DR Genevisible; Q64464; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:MGI.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034875; F:caffeine oxidase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; ISO:MGI.
DR GO; GO:0101021; F:estrogen 2-hydroxylase activity; ISO:MGI.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR GO; GO:0004497; F:monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; ISO:MGI.
DR GO; GO:0005496; F:steroid binding; ISO:MGI.
DR GO; GO:0008395; F:steroid hydroxylase activity; ISO:MGI.
DR GO; GO:0050649; F:testosterone 6-beta-hydroxylase activity; ISO:MGI.
DR GO; GO:0070576; F:vitamin D 24-hydroxylase activity; ISO:MGI.
DR GO; GO:0030343; F:vitamin D3 25-hydroxylase activity; ISO:MGI.
DR GO; GO:0070989; P:oxidative demethylation; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
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 Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..503
FT /note="Cytochrome P450 3A13"
FT /id="PRO_0000051796"
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"
SQ SEQUENCE 503 AA; 57492 MW; 15DDE2606B337FCF CRC64;
MDLIPNFSME TWMLLATSLV LLYLYGTHSH GIFKKLGIPG PKPLPFLGTI LAYQKGFWEC
DIQCHKKYGK MWGLYDGRQP VLAITDPDII KTVLVKECYS TFTNRRRFGP VGILKKAISI
SENEEWKRIR ALLSPTFTSG RLKEMFPIIN QFTDVLVRNM RQGLGEGKPT SMKDIFGAYS
MDVITATSFG VNIDSLNNPQ DPFVEKIKKL LKFDIFDPLF LSVTLFPFLT PVFDALNVSL
FPRDVISFFT TSVERMKENR MKEKEKQRVD FLQLMINSQN YKTKESHKAL SDVEIVAQSV
IFIFAGYETT SSALSFALYL LAIHPDVQKK LQDEIDAALP NKAPATYDTL LQMEYLDMVV
NETLRLYPIA GRLERVCKTD VEINGLFIPK GTVVMIPTFA LHKDPKYWPE PEEFRPERFS
KKNQDSINPY MYLPFGSGPR NCIGMRFALI NMKVALVRVL QNFTVQPCKE TEIPLKLSKQ
GLLQPENPLL LKVVSRDETV SDE
