CP3AG_MOUSE
ID CP3AG_MOUSE Reviewed; 504 AA.
AC Q64481; E9QP65;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cytochrome P450 3A16;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA16;
GN Name=Cyp3a16; Synonyms=Cyp3a-16;
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=ICR; TISSUE=Liver;
RX PubMed=7813478; DOI=10.1111/j.1432-1033.1994.t01-1-00877.x;
RA Itoh S., Satoh M., Abe Y., Hashimoto H., Yanagimoto T., Kamataki T.;
RT "A novel form of mouse cytochrome P450 3A (Cyp3a-16). Its cDNA cloning and
RT expression in fetal liver.";
RL Eur. J. Biochem. 226:877-882(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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 -!- DEVELOPMENTAL STAGE: Fetal- and puberty-specific.
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; D26137; BAA05133.1; -; mRNA.
DR EMBL; AC115895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS19862.1; -.
DR PIR; S50892; S50892.
DR RefSeq; NP_031846.2; NM_007820.2.
DR AlphaFoldDB; Q64481; -.
DR SMR; Q64481; -.
DR STRING; 10090.ENSMUSP00000031633; -.
DR ChEMBL; CHEMBL3637781; -.
DR iPTMnet; Q64481; -.
DR PhosphoSitePlus; Q64481; -.
DR EPD; Q64481; -.
DR jPOST; Q64481; -.
DR MaxQB; Q64481; -.
DR PaxDb; Q64481; -.
DR PRIDE; Q64481; -.
DR ProteomicsDB; 284000; -.
DR DNASU; 13114; -.
DR Ensembl; ENSMUST00000031633; ENSMUSP00000031633; ENSMUSG00000038656.
DR GeneID; 13114; -.
DR KEGG; mmu:13114; -.
DR UCSC; uc009amv.2; mouse.
DR CTD; 13114; -.
DR MGI; MGI:106099; Cyp3a16.
DR VEuPathDB; HostDB:ENSMUSG00000038656; -.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00950000182958; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q64481; -.
DR OMA; FYLCLTH; -.
DR OrthoDB; 467733at2759; -.
DR PhylomeDB; Q64481; -.
DR TreeFam; TF105087; -.
DR Reactome; R-MMU-211981; Xenobiotics.
DR Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR BioGRID-ORCS; 13114; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q64481; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q64481; protein.
DR Bgee; ENSMUSG00000038656; Expressed in hepatobiliary system and 15 other tissues.
DR Genevisible; Q64481; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0032451; F:demethylase activity; ISO:MGI.
DR GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; ISO:MGI.
DR GO; GO:0050649; F:testosterone 6-beta-hydroxylase activity; ISO:MGI.
DR GO; GO:0070989; P:oxidative demethylation; IBA:GO_Central.
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; Oxidoreductase; Reference proteome.
FT CHAIN 1..504
FT /note="Cytochrome P450 3A16"
FT /id="PRO_0000051799"
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 /evidence="ECO:0000250"
FT CONFLICT 28
FT /note="C -> Y (in Ref. 1; BAA05133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 57870 MW; 49C1B9E570DB5BC1 CRC64;
MNLFSALSLD TLVLLAIILV LLYRYGTCTH GLFKKQGIPG PKPLPFLGTV LNYYKGLWKF
DMECYEKYGK TWGLFDGQIP LFVITDPETI KNVLVKECFS VFTNRQDFFP VGIMSKSISL
AKDEEWKRYR ALLSPTFTSG NLKEMFPVIE QYGDILVKYL RQEAEKGKPV AVKDVLGAYS
MDVIISTTFG VNIDSLNNPE DPFVENAKKV LRFDYFDPLS LSVALFPFLT PIYEMLNICM
FPKDSIEFFK KFVDRMTENR LDSKQKHRVD FIYLMMEAYN KSKDKDSHKA LSEIEITAQS
IIFIFAGYET TSSILSFTVY SLATHPDIQK KLQEEIDEAL PNKAPPTYDT VMAMEYLDMV
LNETLRLYPI TNRLQRVCKK DVEINGIYIP KGSTVIIPSY VLHHDPQHWP EPEEFQPERF
SKENKGSIDP YVYLPFGNGP RNCIGMRFAL MNMKLALIKV LQNFSFQPCK ETQIPLKLSR
ELLLQPVKPI VLKVVPRDAV ITGA
