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   27-MAR-2024, entry version 176.
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; 10090-ENSMUSP00000065585; -.
DR   PeptideAtlas; O09158; -.
DR   ProteomicsDB; 283813; -.
DR   DNASU; 56388; -.
DR   Ensembl; ENSMUST00000068317.13; ENSMUSP00000065585.7; ENSMUSG00000029630.16.
DR   GeneID; 56388; -.
DR   KEGG; mmu:56388; -.
DR   UCSC; uc009amz.2; mouse.
DR   AGR; MGI:1930638; -.
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; FIHGNNE; -.
DR   OrthoDB; 1611592at2759; -.
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 47 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 cell types or tissues.
DR   ExpressionAtlas; O09158; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
DR   GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; 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:0070989; P:oxidative demethylation; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR   GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR   CDD; cd20650; CYP3A; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24302:SF8; CYTOCHROME P450 3A-RELATED; 1.
DR   PANTHER; PTHR24302; CYTOCHROME P450 FAMILY 3; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01689; EP450IICYP3A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   Genevisible; O09158; MM.
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
//