CP2BA_MOUSE
ID CP2BA_MOUSE Reviewed; 500 AA.
AC P12791; Q62397;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cytochrome P450 2B10;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIB10;
DE AltName: Full=CYPIIB20;
DE AltName: Full=Cytochrome P450 2B20;
DE AltName: Full=Cytochrome P450 clone PF3/46;
DE AltName: Full=Cytochrome P450-16-alpha;
DE AltName: Full=P24;
DE AltName: Full=Testosterone 16-alpha hydroxylase;
GN Name=Cyp2b10; Synonyms=Cyp2b-10, Cyp2b20;
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] (ISOFORM 1).
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 [MRNA] OF 1-452 (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8831708; DOI=10.1006/bbrc.1996.1447;
RA Damon M., Fautrel A., Marc N., Guillouzo A., Corcos L.;
RT "Isolation of a new mouse cDNA clone: hybrid form of cytochrome P450 2b10
RT and NADPH-cytochrome P450 oxidoreductase.";
RL Biochem. Biophys. Res. Commun. 226:900-905(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-15, AND INDUCTION.
RX PubMed=2779523;
RA Bornheim L.M., Correia M.A.;
RT "Purification and characterization of a mouse liver cytochrome P-450
RT induced by cannabidiol.";
RL Mol. Pharmacol. 36:377-383(1989).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Lung;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P12791-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12791-2; Sequence=VSP_022500;
CC -!- INDUCTION: Up-regulated by cannabidiol. {ECO:0000269|PubMed:2779523}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M21856; AAA40425.1; -; mRNA.
DR EMBL; X99715; CAA68051.1; ALT_SEQ; mRNA.
DR CCDS; CCDS20999.1; -. [P12791-2]
DR PIR; B31047; B31047.
DR AlphaFoldDB; P12791; -.
DR SMR; P12791; -.
DR STRING; 10090.ENSMUSP00000072264; -.
DR ChEMBL; CHEMBL1907983; -.
DR iPTMnet; P12791; -.
DR PhosphoSitePlus; P12791; -.
DR SwissPalm; P12791; -.
DR jPOST; P12791; -.
DR MaxQB; P12791; -.
DR PaxDb; P12791; -.
DR PeptideAtlas; P12791; -.
DR PRIDE; P12791; -.
DR ProteomicsDB; 285277; -. [P12791-1]
DR ProteomicsDB; 285278; -. [P12791-2]
DR MGI; MGI:88598; Cyp2b10.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P12791; -.
DR PhylomeDB; P12791; -.
DR Reactome; R-MMU-211935; Fatty acids.
DR Reactome; R-MMU-211981; Xenobiotics.
DR Reactome; R-MMU-211999; CYP2E1 reactions.
DR ChiTaRS; Cyp2b10; mouse.
DR PRO; PR:P12791; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P12791; protein.
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:0005743; C:mitochondrial inner membrane; 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:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0051879; F:Hsp90 protein 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; ISO:MGI.
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:0009617; P:response to bacterium; IEP: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; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Endoplasmic reticulum;
KW Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..500
FT /note="Cytochrome P450 2B10"
FT /id="PRO_0000051685"
FT BINDING 445
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 128
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT VAR_SEQ 433..441
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8831708"
FT /id="VSP_022500"
FT CONFLICT 55
FT /note="L -> F (in Ref. 2; CAA68051)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="V -> I (in Ref. 2; CAA68051)"
FT /evidence="ECO:0000305"
FT CONFLICT 251..253
FT /note="RHK -> KHR (in Ref. 2; CAA68051)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..281
FT /note="NA -> HT (in Ref. 2; CAA68051)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="V -> A (in Ref. 2; CAA68051)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="H -> R (in Ref. 2; CAA68051)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="T -> A (in Ref. 2; CAA68051)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="S -> T (in Ref. 2; CAA68051)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="L -> M (in Ref. 2; CAA68051)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="Q -> H (in Ref. 2; CAA68051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 56744 MW; F660A00D8D0FBA94 CRC64;
MEPSVLLLLA LLVGFLLLLA RGHPKSRGNF PPGPRPLPLL GNLLQMDRGG LLKSLIQLRE
KYGDVFTVHL GPRPVVMLCG TDTIREALVG QAEAFSGRGT VAVVEPTFKE YGVIFANGER
WKTLRRFSLA TMRDFGMGKR SVEERIQEEA QCLVEELRKS QGAPLDPTFL FQCITANVIC
SIVFGERFEY TDRQFLRLLE LFYQTFSLIS SFSSQMFELF SGFLKYFPGA HRQISKNLQE
LLDYIGHSVE RHKATLDPSV PRDFIDIYLL RMEKEKSNQN AEFHHQNLMM SVLSLFFVGT
ETSSTTLHYG FLLMLKYPHV TEKVQKEIDQ VIGSHRLPTL DDRTKMPYSD AVIHEIQRFS
DLIPIGVPHR VTKDTLFRGY LLPKNTEVYP ILSSALHDPQ YFEQPDSFNP DQFLDANGAL
KKSEAFLPFS TGQIFDQKSV GKRICLGESI ARSELFLFFT SILQNFSVAS HVAPKDIDLT
PKESGIGKIP PTYQICFLAR
