CP3AB_MOUSE
ID CP3AB_MOUSE Reviewed; 504 AA.
AC Q64459;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Cytochrome P450 3A11;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA11;
DE AltName: Full=Cytochrome P-450IIIAM1;
DE AltName: Full=Cytochrome P-450UT;
GN Name=Cyp3a11; Synonyms=Cyp3a-11;
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=1339292; DOI=10.1016/0167-4781(92)90447-8;
RA Yanagimoto T., Itoh S., Muller-Enoch D., Kamataki T.;
RT "Mouse liver cytochrome P-450 (P-450IIIAM1): its cDNA cloning and
RT inducibility by dexamethasone.";
RL Biochim. Biophys. Acta 1130:329-332(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 PROTEIN SEQUENCE OF 1-17 AND 22-24.
RX PubMed=2402224;
RA Bornheim L.M., Correia M.A.;
RT "Selective inactivation of mouse liver cytochrome P-450IIIA by
RT cannabidiol.";
RL Mol. Pharmacol. 38:319-326(1990).
RN [4]
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: Catalyzes erythromycin N-demethylation, nifedipine oxidation
CC and testosterone 6 beta-hydroxylation.
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: Highly expressed in liver.
CC -!- INDUCTION: By dexamethasone.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X60452; CAA42981.1; -; mRNA.
DR EMBL; BC010528; AAH10528.1; -; mRNA.
DR CCDS; CCDS19865.1; -.
DR PIR; S22334; A60564.
DR RefSeq; NP_031844.1; NM_007818.3.
DR AlphaFoldDB; Q64459; -.
DR SMR; Q64459; -.
DR IntAct; Q64459; 3.
DR STRING; 10090.ENSMUSP00000037665; -.
DR ChEMBL; CHEMBL1907984; -.
DR iPTMnet; Q64459; -.
DR PhosphoSitePlus; Q64459; -.
DR SwissPalm; Q64459; -.
DR jPOST; Q64459; -.
DR MaxQB; Q64459; -.
DR PaxDb; Q64459; -.
DR PRIDE; Q64459; -.
DR ProteomicsDB; 283999; -.
DR DNASU; 13112; -.
DR Ensembl; ENSMUST00000035918; ENSMUSP00000037665; ENSMUSG00000056035.
DR GeneID; 13112; -.
DR KEGG; mmu:13112; -.
DR UCSC; uc009amy.1; mouse.
DR CTD; 13112; -.
DR MGI; MGI:88609; Cyp3a11.
DR VEuPathDB; HostDB:ENSMUSG00000056035; -.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00950000182958; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; Q64459; -.
DR OMA; DRGQADF; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; Q64459; -.
DR TreeFam; TF105087; -.
DR BRENDA; 1.14.99.38; 3474.
DR Reactome; R-MMU-211981; Xenobiotics.
DR Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-MMU-9027307; Biosynthesis of maresin-like SPMs.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR Reactome; R-MMU-9754706; Atorvastatin ADME.
DR BioGRID-ORCS; 13112; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Cyp3a11; mouse.
DR PRO; PR:Q64459; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q64459; protein.
DR Bgee; ENSMUSG00000056035; Expressed in small intestine Peyer's patch and 127 other tissues.
DR ExpressionAtlas; Q64459; baseline and differential.
DR Genevisible; Q64459; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:0032451; F:demethylase 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; IDA: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: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:0009617; P:response to bacterium; IEP: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 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 3A11"
FT /id="PRO_0000051794"
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"
SQ SEQUENCE 504 AA; 57855 MW; E369AF71CE23F180 CRC64;
MDLVSALSLE TWVLLAISLV LLYRYGTRKH ELFKKQGIPG PKPLPFLGTV LNYYKGLWKF
DMECYKKYGK TWGLFDGQTP LLAVTDPETI KNVLVKECFS VFTNRRDFGP VGIMSKAISI
SKDDEWKRYR ALLSPTFTSG KLKEMFPVIE QYGDILVKYL RQKAKKGKPV TMKDVLGAYS
MDVITSTSFG VNVDSLNNPE DPFVEKAKKL LRFDFFDPLL FSVVLFPFLT PVYEMLNICM
FPKDSIEFFK KFVDRMKESR LDSKQKHRVD FLQLMMNSHN NSKDKVSHKA LSDMEITAQS
IIFIFAGYET TSSTLSFTLH SLATHPDIQK KLQDEIDEAL PNKAPPTYDT VMEMEYLDMV
LNETLRLYPI ANRLERVCKK DVELNGVYIP KGSTVMIPSY ALHHDPQHWS EPEEFQPERF
SKENKGSIDP YVYLPFGNGP RNCLGMRFAL MNMKLALTKI MQNFSFQPCK ETQIPLKLSR
QGLLQPEKPI VLKVVPRDAV ITGA
