CP2B9_MOUSE
ID CP2B9_MOUSE Reviewed; 491 AA.
AC P12790; Q64463;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytochrome P450 2B9;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIB9;
DE AltName: Full=Cytochrome P450 clone PF26;
DE AltName: Full=Cytochrome P450-16-alpha;
DE AltName: Full=Testosterone 16-alpha hydroxylase;
GN Name=Cyp2b9; Synonyms=Cyp2b-9, Rip;
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 TISSUE=Liver;
RX PubMed=3219345; DOI=10.1021/bi00417a035;
RA Noshiro M., Lakso M., Kawajiri K., Negishi M.;
RT "Rip locus: regulation of female-specific isozyme (I-P-450(16 alpha) of
RT testosterone 16 alpha-hydroxylase in mouse liver, chromosome localization,
RT and cloning of P-450 cDNA.";
RL Biochemistry 27:6434-6443(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1997326; DOI=10.1111/j.1432-1033.1991.tb15728.x;
RA Lakso M., Masaki R., Noshiro M., Negishi M.;
RT "Structures and characterization of sex-specific mouse cytochrome P-450
RT genes as members within a large family. Duplication boundary and
RT evolution.";
RL Eur. J. Biochem. 195:477-486(1991).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M21855; AAA40424.1; -; mRNA.
DR EMBL; M60273; AAA03648.1; -; Genomic_DNA.
DR EMBL; M60267; AAA03648.1; JOINED; Genomic_DNA.
DR EMBL; M60268; AAA03648.1; JOINED; Genomic_DNA.
DR EMBL; M60269; AAA03648.1; JOINED; Genomic_DNA.
DR EMBL; M60270; AAA03648.1; JOINED; Genomic_DNA.
DR EMBL; M60271; AAA03648.1; JOINED; Genomic_DNA.
DR EMBL; M60272; AAA03648.1; JOINED; Genomic_DNA.
DR EMBL; AC157782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120525; AAI20526.1; -; mRNA.
DR EMBL; BC120527; AAI20528.1; -; mRNA.
DR CCDS; CCDS21001.1; -.
DR PIR; A31047; A31047.
DR PIR; I84735; I84735.
DR RefSeq; NP_034130.1; NM_010000.2.
DR AlphaFoldDB; P12790; -.
DR SMR; P12790; -.
DR STRING; 10090.ENSMUSP00000080846; -.
DR DrugBank; DB08834; Tauroursodeoxycholic acid.
DR iPTMnet; P12790; -.
DR PhosphoSitePlus; P12790; -.
DR SwissPalm; P12790; -.
DR jPOST; P12790; -.
DR PaxDb; P12790; -.
DR PeptideAtlas; P12790; -.
DR PRIDE; P12790; -.
DR ProteomicsDB; 278005; -.
DR TopDownProteomics; P12790; -.
DR DNASU; 13094; -.
DR Ensembl; ENSMUST00000082214; ENSMUSP00000080846; ENSMUSG00000040660.
DR GeneID; 13094; -.
DR KEGG; mmu:13094; -.
DR UCSC; uc009fuh.1; mouse.
DR CTD; 13094; -.
DR MGI; MGI:88600; Cyp2b9.
DR VEuPathDB; HostDB:ENSMUSG00000040660; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000161658; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; P12790; -.
DR OMA; KFIYVEA; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P12790; -.
DR TreeFam; TF352043; -.
DR BioGRID-ORCS; 13094; 0 hits in 73 CRISPR screens.
DR PRO; PR:P12790; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P12790; protein.
DR Bgee; ENSMUSG00000040660; Expressed in morula and 29 other tissues.
DR Genevisible; P12790; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; 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:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0101021; F:estrogen 2-hydroxylase activity; ISO:MGI.
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: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:0008390; F:testosterone 16-alpha-hydroxylase activity; ISO:MGI.
DR GO; GO:0062184; F:testosterone 16-beta-hydroxylase activity; ISO:MGI.
DR GO; GO:0042180; P:cellular ketone metabolic process; ISO:MGI.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
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: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; IPR008068; Cyt_P450_E_grp-I_CYP2B-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01685; EP450ICYP2B.
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..491
FT /note="Cytochrome P450 2B9"
FT /id="PRO_0000051684"
FT BINDING 436
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 MOD_RES 128
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P00176"
FT CONFLICT 298
FT /note="A -> V (in Ref. 1; AAA40424)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="H -> Q (in Ref. 1; AAA40424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 55741 MW; C1E790A7DD1A7298 CRC64;
MDPSVLLLLA VLLSLFLLLV RGHAKIHGHL PPGPHPLPLL GNLLQMDRGG LLKCFIQLQE
KHGDVFTVHL GPRPVVVLCG TQTIREALVD HAEAFSGRGT IAAAQLVMQD YGIFFASGQR
WKTLRRFSLA TMKEFGMGKR SVEERIKEEA QCLVEELKKY QGVPLDPTFL FQCITANIIC
SIVFGERFDY TDDQFLHLLN LMYKIFSLLS SFSGQMFELF SGFLKYFPGV HRQIVKKQQE
LLDYIAHSVE KHKATLDPSA PRDYIDTYLL RMEKEKSNHN TEFHHQNLMM SVLSLFFAGT
ETTSATLHYG VLLMLKYPHV TEKVQKEIDQ VIGSHRLPTL DDRTKMPYTD AVIHEIQRFS
DLVPIGLPHK VIKDTLFRGY LLPKNTEVYP VLSSALHDPQ YFEQPDKFNP EHFLDANGAL
KKCEAFLPFS TGKRICLGES IARNELFIFF TTILQNFSVA SPVAPKDIDL TPKESGIGKI
PPAHQIYFLA R
