CP3AP_MOUSE
ID CP3AP_MOUSE Reviewed; 503 AA.
AC O09158;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cytochrome P450 3A25;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA25;
GN Name=Cyp3a25;
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].
RA Mahnke A., Roos P., Hanstein W.G.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 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: 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 -!- 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; Y11995; CAA72720.1; -; mRNA.
DR EMBL; BC028855; AAH28855.1; -; mRNA.
DR CCDS; CCDS19866.1; -.
DR RefSeq; NP_062766.2; NM_019792.2.
DR AlphaFoldDB; O09158; -.
DR SMR; O09158; -.
DR BioGRID; 207946; 6.
DR STRING; 10090.ENSMUSP00000065585; -.
DR ChEMBL; CHEMBL3637781; -.
DR iPTMnet; O09158; -.
DR PhosphoSitePlus; O09158; -.
DR SwissPalm; O09158; -.
DR jPOST; O09158; -.
DR MaxQB; O09158; -.
DR PaxDb; O09158; -.
DR PeptideAtlas; O09158; -.
DR PRIDE; O09158; -.
DR ProteomicsDB; 283813; -.
DR DNASU; 56388; -.
DR Ensembl; ENSMUST00000068317; ENSMUSP00000065585; ENSMUSG00000029630.
DR GeneID; 56388; -.
DR KEGG; mmu:56388; -.
DR UCSC; uc009amz.2; mouse.
DR CTD; 56388; -.
DR MGI; MGI:1930638; Cyp3a25.
DR VEuPathDB; HostDB:ENSMUSG00000029630; -.
DR eggNOG; KOG0158; Eukaryota.
DR GeneTree; ENSGT00950000182958; -.
DR HOGENOM; CLU_001570_5_2_1; -.
DR InParanoid; O09158; -.
DR OMA; CITWFGT; -.
DR OrthoDB; 467733at2759; -.
DR PhylomeDB; O09158; -.
DR TreeFam; TF105087; -.
DR Reactome; R-MMU-211958; Miscellaneous substrates.
DR Reactome; R-MMU-211981; Xenobiotics.
DR BioGRID-ORCS; 56388; 2 hits in 42 CRISPR screens.
DR ChiTaRS; Cyp3a25; mouse.
DR PRO; PR:O09158; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O09158; protein.
DR Bgee; ENSMUSG00000029630; Expressed in small intestine Peyer's patch and 31 other tissues.
DR ExpressionAtlas; O09158; baseline and differential.
DR Genevisible; O09158; 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; 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:0008390; F:testosterone 16-alpha-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 Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..503
FT /note="Cytochrome P450 3A25"
FT /id="PRO_0000051805"
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; 58122 MW; 9EE9EAF1746595C8 CRC64;
MELIPNLSIE TWVLLVTSLV LFYIYGTYSH GLFKKLGIPG PKPLPLLGTI FNYYDGMWKF
DEDCYKKYGK IWGFYEGPQP ILAIMDPEII KIVLVKECYS VFTNRRFFGP VGFMKKAITI
SEDEEWKRLR TLLSPTFTSG KLKEMFPIMR QYGDILVRNL RREEEKGEPI SMKDIFGAYS
MDVITGTSFG VNVDSLNNPQ DPFVQKAKKI LKFKIFDPFL LSIILFPFLT PIYEMLNFSI
FPRDSMNFFK KFVKRMKKER LASNQKNRVD FLQLMMNTQN SKGQESQKAL SDLEMAAQAV
IFIFGGYDAT STSISLIMYE LATHPDVQKK LQDEIDRTLP NKAPVTYDAL MDMEYLDMVV
NESLRLYPIA IRLERVSKKD VEINGVFIPK GTVVMIPIYP LHRNPEYWPE PQEFCPERFS
KENKGNIDPY IYMPFGNGPR NCIGMRFALI SIKLAVIGVL QNFTVQPCEE TQIPLKISRE
PIFQPEKPII LKVVSRDKPR TGS
