ID   CP341_MOUSE             Reviewed;         504 AA.
AC   Q9JMA7; B2RQU5; E9QJT9;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Cytochrome P450 3A41;
DE            EC=1.14.14.1;
GN   Name=Cyp3a41a; Synonyms=Cyp3a41;
GN   and
GN   Name=Cyp3a41b;
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=10775455; DOI=10.1006/abbi.2000.1747;
RA   Sakuma T., Takai M., Endo Y., Kuroiwa M., Ohara A., Jarukamjorn K.,
RA   Honma R., Nemoto N.;
RT   "A novel female-specific member of the CYP3A gene subfamily in the mouse
RT   liver.";
RL   Arch. Biochem. Biophys. 377:153-162(2000).
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [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   -!- 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 {ECO:0000305};
CC       Peripheral membrane protein {ECO:0000305}. Microsome membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver. Also expressed in the kidneys
CC       of female mice, with traces in the stomach, ovary, and heart of female
CC       mice and in the testis of male mice.
CC   -!- DEVELOPMENTAL STAGE: Detected immediately after birth in the livers of
CC       animals of both sexes, but increases with age in females, whereas it is
CC       gradually reduced in males, resulting in predominantly female-specific
CC       expression in livers.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB033414; BAA95951.1; -; mRNA.
DR   EMBL; AC124483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC166648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC138083; AAI38084.1; -; mRNA.
DR   EMBL; BC138084; AAI38085.1; -; mRNA.
DR   CCDS; CCDS39389.1; -.
DR   RefSeq; NP_001098629.1; NM_001105159.1.
DR   RefSeq; NP_059092.2; NM_017396.3.
DR   AlphaFoldDB; Q9JMA7; -.
DR   SMR; Q9JMA7; -.
DR   STRING; 10090.ENSMUSP00000075234; -.
DR   ChEMBL; CHEMBL3637781; -.
DR   iPTMnet; Q9JMA7; -.
DR   PhosphoSitePlus; Q9JMA7; -.
DR   SwissPalm; Q9JMA7; -.
DR   jPOST; Q9JMA7; -.
DR   MaxQB; Q9JMA7; -.
DR   PaxDb; Q9JMA7; -.
DR   PeptideAtlas; Q9JMA7; -.
DR   PRIDE; Q9JMA7; -.
DR   ProteomicsDB; 283618; -.
DR   DNASU; 53973; -.
DR   Ensembl; ENSMUST00000075837; ENSMUSP00000075234; ENSMUSG00000075552.
DR   Ensembl; ENSMUST00000094111; ENSMUSP00000091659; ENSMUSG00000075551.
DR   GeneID; 100041375; -.
DR   GeneID; 53973; -.
DR   KEGG; mmu:100041375; -.
DR   KEGG; mmu:53973; -.
DR   UCSC; uc012egw.1; mouse.
DR   CTD; 100041375; -.
DR   CTD; 53973; -.
DR   MGI; MGI:1858451; Cyp3a41a.
DR   MGI; MGI:3714859; Cyp3a41b.
DR   VEuPathDB; HostDB:ENSMUSG00000075551; -.
DR   VEuPathDB; HostDB:ENSMUSG00000075552; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   GeneTree; ENSGT00950000182958; -.
DR   HOGENOM; CLU_001570_5_2_1; -.
DR   InParanoid; Q9JMA7; -.
DR   OMA; MHEMRLI; -.
DR   OrthoDB; 467733at2759; -.
DR   PhylomeDB; Q9JMA7; -.
DR   TreeFam; TF105087; -.
DR   Reactome; R-MMU-211981; Xenobiotics.
DR   Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR   BioGRID-ORCS; 100041375; 5 hits in 37 CRISPR screens.
DR   BioGRID-ORCS; 53973; 5 hits in 36 CRISPR screens.
DR   ChiTaRS; Cyp3a41b; mouse.
DR   PRO; PR:Q9JMA7; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9JMA7; protein.
DR   Bgee; ENSMUSG00000075551; Expressed in liver and 7 other tissues.
DR   Genevisible; Q9JMA7; 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; 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: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:0010468; P:regulation of gene expression; IDA:MGI.
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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..504
FT                   /note="Cytochrome P450 3A41"
FT                   /id="PRO_0000051813"
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        42
FT                   /note="K -> T (in Ref. 1; BAA95951 and 3; AAI38084/
FT                   AAI38085)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   504 AA;  57987 MW;  1F6455156C073479 CRC64;
     MNLFSALSLD TWVLLAIILV LLYRYGTRTH GLFKKQGIPG PKPLPFLGTV LNYYKGLWKF
     DMECYEKYGK TWGLFDGQMP LFVITDPEMI KNVLVKECFS VFTNRREFGP VGIMSKAISI
     SKDEEWKRYR ALLSPTFTSG KLKEMFPVIE QYGDILVKYL MQEAEKGKPV TMKDVLGAYS
     IDVITSTSFG VNVDSLNNPE DPFVEKAKGI LRVDFFDPLV FSVVLFPFLT PVYEMLNICM
     FPKDSIEFFK KFVNRMKESR LDSKQKHRVD FLQLMMNAHN NSKDKDSHKA LSDMEITAQS
     IVFIFAGYET TSSTLSFTLY CLATHPDIQK KLQEEIDETL PNKAPPTYDT VMEMEYLDMV
     LNETLRLYPI GNRLERFCKK DVELNGVYIP KGSTVMIPSY ALHHDPQHWP EPEEFQPERF
     SKENKGSIDP YLYMPFGIGP RNCIGMRFAF MTMKLALTKV MQNFSFQPCQ ETQIPLKLSR
     QGLLQPEKPI VLKVVPRDVV ITGA