CP2A5_MOUSE
ID CP2A5_MOUSE Reviewed; 494 AA.
AC P20852;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Cytochrome P450 2A5;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIA5;
DE AltName: Full=Coumarin 7-hydroxylase;
DE AltName: Full=Cytochrome P450-15-COH;
DE AltName: Full=Cytochrome P450-IIA3.2;
GN Name=Cyp2a5; Synonyms=Cyp2a-5;
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 [GENOMIC DNA].
RC TISSUE=Kidney;
RX PubMed=2703500; DOI=10.1016/s0021-9258(18)83371-3;
RA Lindberg R., Burkhart B., Ichikawa T., Negishi M.;
RT "The structure and characterization of type I P-450(15) alpha gene as major
RT steroid 15 alpha-hydroxylase and its comparison with type II P-450(15)
RT alpha gene.";
RL J. Biol. Chem. 264:6465-6471(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=17NC/Z;
RA Jounaidi Y.;
RT "cDNA and amino acid sequence of a new cyp2a isoform overexpressed in
RT chemically induced mouse hepatoma.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP MUTAGENESIS.
RX PubMed=2733794; DOI=10.1038/339632a0;
RA Lindberg R., Negishi M.;
RT "Alteration of mouse cytochrome P450coh substrate specificity by mutation
RT of a single amino-acid residue.";
RL Nature 339:632-634(1989).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10490589; DOI=10.1128/mcb.19.10.6488;
RA Lavery D.J., Lopez-Molina L., Margueron R., Fleury-Olela F., Conquet F.,
RA Schibler U., Bonfils C.;
RT "Circadian expression of the steroid 15 alpha-hydroxylase (Cyp2a4) and
RT coumarin 7-hydroxylase (Cyp2a5) genes in mouse liver is regulated by the
RT PAR leucine zipper transcription factor DBP.";
RL Mol. Cell. Biol. 19:6488-6499(1999).
CC -!- FUNCTION: Exhibits a high coumarin 7-hydroxylase activity.
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: Liver, with a strong circadian rhythmicity.
CC Circadian expression is regulated by DBP.
CC {ECO:0000269|PubMed:10490589}.
CC -!- DEVELOPMENTAL STAGE: In liver; activity 6 fold higher in females than
CC in males.
CC -!- MISCELLANEOUS: There are only 11 differences between the sequence of
CC testosterone 15-alpha-hydroxylase and that of coumarin 7-hydroxylase.
CC By site-directed mutagenesis it has been shown that modification of
CC position 209 is sufficient to convert the specificity of the two forms
CC of the enzyme.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M25211; AAA37798.1; -; Genomic_DNA.
DR EMBL; M26204; AAA37798.1; JOINED; Genomic_DNA.
DR EMBL; M25205; AAA37798.1; JOINED; Genomic_DNA.
DR EMBL; M25206; AAA37798.1; JOINED; Genomic_DNA.
DR EMBL; M25207; AAA37798.1; JOINED; Genomic_DNA.
DR EMBL; M25208; AAA37798.1; JOINED; Genomic_DNA.
DR EMBL; M25209; AAA37798.1; JOINED; Genomic_DNA.
DR EMBL; M25210; AAA37798.1; JOINED; Genomic_DNA.
DR EMBL; X89864; CAA61963.1; -; mRNA.
DR CCDS; CCDS21008.1; -.
DR PIR; B33531; B33531.
DR AlphaFoldDB; P20852; -.
DR SMR; P20852; -.
DR STRING; 10090.ENSMUSP00000005685; -.
DR BindingDB; P20852; -.
DR ChEMBL; CHEMBL4085; -.
DR iPTMnet; P20852; -.
DR PhosphoSitePlus; P20852; -.
DR jPOST; P20852; -.
DR MaxQB; P20852; -.
DR PaxDb; P20852; -.
DR PeptideAtlas; P20852; -.
DR PRIDE; P20852; -.
DR ProteomicsDB; 285276; -.
DR MGI; MGI:88597; Cyp2a5.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P20852; -.
DR PhylomeDB; P20852; -.
DR Reactome; R-MMU-211935; Fatty acids.
DR Reactome; R-MMU-211981; Xenobiotics.
DR Reactome; R-MMU-211999; CYP2E1 reactions.
DR SABIO-RK; P20852; -.
DR PRO; PR:P20852; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P20852; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008389; F:coumarin 7-hydroxylase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0071276; P:cellular response to cadmium ion; IDA:MGI.
DR GO; GO:0009804; P:coumarin metabolic process; IBA:GO_Central.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0042168; P:heme metabolic process; IDA:MGI.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR008067; Cyt_P450_E_grp-I_CYP2A-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01684; EP450ICYP2A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW Microsome; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..494
FT /note="Cytochrome P450 2A5"
FT /id="PRO_0000051667"
FT BINDING 439
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 MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00176"
FT MOD_RES 379
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
SQ SEQUENCE 494 AA; 56741 MW; 1C2516D5FA2551D0 CRC64;
MLTSGLLLVA AVAFLSVLVL MSVWKQRKLS GKLPPGPTPL PFIGNFLQLN TEQMYNSLMK
ISQRYGPVFT IYLGPRRIVV LCGQEAVKEA LVDQAEEFSG RGEQATFDWL FKGYGVVFSS
GERAKQLRRF SIATLRDFGV GKRGIEERIQ EEAGFLIDSF RKTNGAFIDP TFYLSRTVSN
VISSIVFGDR FDYEDKEFLS LLRMMLGSFQ FTATSMGQLY EMFSSVMKHL PGPQQQAFKE
LQGLEDFITK KVEHNQRTLD PNSPRDFIDS FLIRMLEEKK NPNTEFYMKN LVLTTLNLFF
AGTETVSTTL RYGFLLLMKH PDIEAKVHEE IDRVIGRNRQ PKYEDRMKMP YTEAVIHEIQ
RFADMIPMGL ARRVTKDTKF RDFLLPKGTE VFPMLGSVLK DPKFFSNPKD FNPKHFLDDK
GQFKKNDAFV PFSIGKRYCF GEGLARMELF LFLTNIMQNF HFKSTQAPQD IDVSPRLVGF
ATIPPTYTMS FLSR
