CP2BJ_MOUSE
ID CP2BJ_MOUSE Reviewed; 492 AA.
AC O55071; B2RQK1;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cytochrome P450 2B19;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIB19;
GN Name=Cyp2b19;
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 STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=9799616; DOI=10.1006/geno.1998.5533;
RA Keeney D.S.;
RT "The novel skin-specific cytochrome P450 Cyp2b19 maps to proximal
RT chromosome 7 in the mouse, near a cluster of Cyp2 family genes.";
RL Genomics 53:417-419(1998).
RN [2]
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).
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 -!- TISSUE SPECIFICITY: Expressed only in differentiated keratinocytes in
CC skin.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF047529; AAC78770.1; -; mRNA.
DR EMBL; BC137965; AAI37966.1; -; mRNA.
DR EMBL; BC137966; AAI37967.1; -; mRNA.
DR CCDS; CCDS21006.1; -.
DR RefSeq; NP_031840.1; NM_007814.2.
DR AlphaFoldDB; O55071; -.
DR SMR; O55071; -.
DR STRING; 10090.ENSMUSP00000077021; -.
DR iPTMnet; O55071; -.
DR PhosphoSitePlus; O55071; -.
DR jPOST; O55071; -.
DR MaxQB; O55071; -.
DR PaxDb; O55071; -.
DR PeptideAtlas; O55071; -.
DR PRIDE; O55071; -.
DR ProteomicsDB; 283615; -.
DR DNASU; 13090; -.
DR Ensembl; ENSMUST00000077855; ENSMUSP00000077021; ENSMUSG00000066704.
DR GeneID; 13090; -.
DR KEGG; mmu:13090; -.
DR UCSC; uc009fus.2; mouse.
DR CTD; 13090; -.
DR MGI; MGI:107303; Cyp2b19.
DR VEuPathDB; HostDB:ENSMUSG00000066704; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000161658; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; O55071; -.
DR OMA; HMASEIF; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; O55071; -.
DR TreeFam; TF352043; -.
DR BioGRID-ORCS; 13090; 4 hits in 59 CRISPR screens.
DR PRO; PR:O55071; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O55071; protein.
DR Bgee; ENSMUSG00000066704; Expressed in tail skin and 38 other tissues.
DR Genevisible; O55071; 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; ISO:MGI.
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: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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..492
FT /note="Cytochrome P450 2B19"
FT /id="PRO_0000051689"
FT BINDING 437
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 129
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P00176"
SQ SEQUENCE 492 AA; 55997 MW; 9E685AF61EE2DFA2 CRC64;
MEFSVLLLLA LTTGFLIFLV SQSQPKTHGH FPPGPRPLPF LGNLLQMDRR GLLSSFIQLQ
EKYGDVFTVH LGPRPVVMLC GTDTIREALV NQAEAFSGRG TVAVLDPIVQ GYGVIFSSGE
RWKTLRRFSL ATMRDFGMGK RSVEERIKEE AQCLVEELKK YKGAPLNPTF YFQCIVANII
CSIVFGERFD YKDHQFLHLL NLIYQTFSLM SSLSSQVFEL FSAILKYFPG AHRQISKNLQ
EILDYIGHSV EKHRATLDPS APRDFIDTYL LRMEKEKSNH HTEFHHQNLV ISVLSLFFAG
TETTSTTLRY SFLIMLKYPH VAEKVQKEID QVIGSHRLPT LDDRTKMPYT DAVIHEIQRF
TDLAPIGLPH KVTKDTLFRG YLIPKNTEVY PILSSALHDP RYFEQPDSFN PEHFLDANGA
LKTNEAFMPF STGKRICLGE GIARNELFLF FTTILQNFSL ASPVAPENID LIPNNSGATK
TPPQYQIHFL SR
