CP2D9_MOUSE
ID CP2D9_MOUSE Reviewed; 504 AA.
AC P11714; Q64489; Q921V1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cytochrome P450 2D9;
DE EC=1.14.14.1;
DE AltName: Full=CYPIID9;
DE AltName: Full=Cytochrome P450-16-alpha;
DE AltName: Full=Cytochrome P450CA;
DE AltName: Full=Testosterone 16-alpha hydroxylase;
GN Name=Cyp2d9; Synonyms=Cyp2d-9;
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].
RX PubMed=2831949; DOI=10.1021/bi00400a029;
RA Wong G., Kawajiri K., Negishi M.;
RT "Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P-
RT 450(16) alpha) in mouse liver: cDNA sequences, neonatal imprinting, and
RT reversible regulation by androgen.";
RL Biochemistry 26:8683-8690(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/J; TISSUE=Liver;
RX PubMed=2788458; DOI=10.1021/bi00437a039;
RA Ichikawa T., Itakura T., Negishi M.;
RT "Functional characterization of two cytochrome P-450s within the mouse,
RT male-specific steroid 16 alpha-hydroxylase gene family: expression in
RT mammalian cells and chimeric proteins.";
RL Biochemistry 28:4779-4784(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2914938; DOI=10.1016/s0021-9258(19)81700-3;
RA Wong G., Itakura T., Kawajiri K., Skow L., Negishi M.;
RT "Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P-450(16
RT alpha)) in mice. Organization, differential regulation, and chromosome
RT localization.";
RL J. Biol. Chem. 264:2920-2927(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
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; M23998; AAA40427.1; -; mRNA.
DR EMBL; M23997; AAA40428.1; ALT_SEQ; mRNA.
DR EMBL; M27168; AAA39876.1; -; mRNA.
DR EMBL; M24267; AAA75462.1; -; Genomic_DNA.
DR EMBL; M24262; AAA75462.1; JOINED; Genomic_DNA.
DR EMBL; CH466550; EDL04501.1; -; Genomic_DNA.
DR EMBL; BC010593; AAH10593.1; -; mRNA.
DR EMBL; BC094015; AAH94015.1; -; mRNA.
DR CCDS; CCDS27691.1; -.
DR PIR; B27384; B27384.
DR PIR; S15806; A27384.
DR RefSeq; NP_034136.2; NM_010006.2.
DR AlphaFoldDB; P11714; -.
DR SMR; P11714; -.
DR STRING; 10090.ENSMUSP00000086530; -.
DR iPTMnet; P11714; -.
DR PhosphoSitePlus; P11714; -.
DR SwissPalm; P11714; -.
DR jPOST; P11714; -.
DR MaxQB; P11714; -.
DR PaxDb; P11714; -.
DR PeptideAtlas; P11714; -.
DR PRIDE; P11714; -.
DR ProteomicsDB; 285279; -.
DR DNASU; 13105; -.
DR Ensembl; ENSMUST00000089129; ENSMUSP00000086530; ENSMUSG00000068086.
DR GeneID; 13105; -.
DR KEGG; mmu:13105; -.
DR UCSC; uc007wzg.2; mouse.
DR CTD; 13105; -.
DR MGI; MGI:88606; Cyp2d9.
DR VEuPathDB; HostDB:ENSMUSG00000068086; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000153331; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; P11714; -.
DR OMA; HSCLNAN; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P11714; -.
DR TreeFam; TF352043; -.
DR BioGRID-ORCS; 13105; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Cyp2d9; mouse.
DR PRO; PR:P11714; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P11714; protein.
DR Bgee; ENSMUSG00000068086; Expressed in left lobe of liver and 36 other tissues.
DR ExpressionAtlas; P11714; baseline and differential.
DR Genevisible; P11714; MM.
DR GO; GO:0005737; C:cytoplasm; 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:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0062188; F:anandamide 11,12 epoxidase activity; ISO:MGI.
DR GO; GO:0062189; F:anandamide 14,15 epoxidase activity; ISO:MGI.
DR GO; GO:0062187; F:anandamide 8,9 epoxidase activity; ISO:MGI.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
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:0009822; P:alkaloid catabolic process; ISO:MGI.
DR GO; GO:0009820; P:alkaloid metabolic process; ISO:MGI.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IBA:GO_Central.
DR GO; GO:0009804; P:coumarin metabolic process; ISO:MGI.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:MGI.
DR GO; GO:0046483; P:heterocycle metabolic process; ISO:MGI.
DR GO; GO:0033076; P:isoquinoline alkaloid metabolic process; ISO:MGI.
DR GO; GO:0016098; P:monoterpenoid metabolic process; ISO:MGI.
DR GO; GO:0051100; P:negative regulation of binding; ISO:MGI.
DR GO; GO:0090350; P:negative regulation of cellular organofluorine metabolic process; ISO:MGI.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0070989; P:oxidative demethylation; ISO:MGI.
DR GO; GO:0042572; P:retinol metabolic process; ISO:MGI.
DR GO; GO:0008202; P:steroid metabolic process; ISO:MGI.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:MGI.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:MGI.
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; IPR008069; Cyt_P450_E_grp-I_CYP2D-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01686; EP450ICYP2D.
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; Phosphoprotein; Reference proteome.
FT CHAIN 1..504
FT /note="Cytochrome P450 2D9"
FT /id="PRO_0000051734"
FT BINDING 446
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 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10634"
FT CONFLICT 54..55
FT /note="LG -> QD (in Ref. 2; AAA39876)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="E -> Q (in Ref. 1; AAA40428/AAA40427, 2; AAA39876
FT and 3; AAA75462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56950 MW; 6DC93B3985EFB8A2 CRC64;
MELLTGTDLW PVAIFTVIFI LLVDLTHQRQ RWTSRYPPGP VPWPVLGNLL QVDLGNMPYS
LYKLQNRYGD VFSLQMAWKP MVVINGLKAM KEMLLTCGED TADRPPVPIF EYLGVKPGSQ
GVVLAPYGPE WREQRRFSVS TLRNFGLGKK SLEDWVTKEA NHLCDAFTAQ AGQPINPNPM
LNKSTCNVIA SLIFARRFEY EDPFLIRMLK VLEQSLTEVS GLIPEVLNAF PILLRIPRLA
DKALQGQKSF IAILDNLLTE NRTTWDPVQA PRNLTDAFLA EIEKAKGNPE SSFNDENLLM
VVRDLFGAGM LTTSTTLSWA LMLMILHPDV QRRVQQEIDE VIGQVRHPEM ADQAHMPYTN
AVIHEVQRFG DIVPVNLPRI TSHDIEVQDF LIPKGTILLP NMSSMLKDES VWEKPLRFHP
EHFLDAQGHF VKPEAFMPFS AGRRSCLGEA LARMELFLFF TCLLQRFSFS VPDGQPQPSN
SGVYGILVAP SPYQLCAVVR DQGH
