CP2B3_RAT
ID CP2B3_RAT Reviewed; 491 AA.
AC P13107; A1L121; Q3B8R5; Q64585;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytochrome P450 2B3;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIB3;
GN Name=Cyp2b3; Synonyms=Cyp2b-3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3396451; DOI=10.1089/dna.1988.7.253;
RA Labbe D., Jean A., Anderson A.;
RT "A constitutive member of the rat cytochrome P450IIB subfamily: full-length
RT coding sequence of the P450IIB3 cDNA.";
RL DNA 7:253-260(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 295-491.
RX PubMed=3013548; DOI=10.1089/dna.1986.5.209;
RA Affolter M., Labbe D., Jean A., Raymond M., Noel D., Labelle Y.,
RA Parent-Vaugeois C., Lambert M., Bojanowski R., Anderson A.;
RT "cDNA clones for liver cytochrome P-450s from individual aroclor-treated
RT rats: constitutive expression of a new P-450 gene related to phenobarbital-
RT inducible forms.";
RL DNA 5:209-218(1986).
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: Liver. Not found in the lung, kidney and prostate.
CC -!- INDUCTION: Constitutively expressed.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M20406; AAA41006.1; -; mRNA.
DR EMBL; BC088103; AAH88103.1; -; mRNA.
DR EMBL; BC105823; AAI05824.1; -; mRNA.
DR EMBL; BC127479; AAI27480.1; -; mRNA.
DR EMBL; M19973; AAA41048.1; -; mRNA.
DR PIR; A29818; A29818.
DR RefSeq; NP_775416.1; NM_173294.2.
DR AlphaFoldDB; P13107; -.
DR SMR; P13107; -.
DR IntAct; P13107; 1.
DR STRING; 10116.ENSRNOP00000030069; -.
DR iPTMnet; P13107; -.
DR PhosphoSitePlus; P13107; -.
DR PaxDb; P13107; -.
DR PRIDE; P13107; -.
DR Ensembl; ENSRNOT00000034845; ENSRNOP00000030069; ENSRNOG00000033164.
DR GeneID; 286953; -.
DR KEGG; rno:286953; -.
DR CTD; 286953; -.
DR RGD; 628627; Cyp2b3.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000161658; -.
DR InParanoid; P13107; -.
DR OMA; MSISHSA; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P13107; -.
DR PRO; PR:P13107; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000033164; Expressed in liver and 11 other tissues.
DR Genevisible; P13107; RN.
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; IDA:RGD.
DR GO; GO:0062188; F:anandamide 11,12 epoxidase activity; ISO:RGD.
DR GO; GO:0062189; F:anandamide 14,15 epoxidase activity; ISO:RGD.
DR GO; GO:0062187; F:anandamide 8,9 epoxidase activity; ISO:RGD.
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:RGD.
DR GO; GO:0020037; F:heme binding; ISO:RGD.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; ISO:RGD.
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:RGD.
DR GO; GO:0062184; F:testosterone 16-beta-hydroxylase activity; ISO:RGD.
DR GO; GO:0042180; P:cellular ketone metabolic process; ISO:RGD.
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:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0035634; P:response to stilbenoid; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0008202; P:steroid metabolic process; ISO:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
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; Reference proteome.
FT CHAIN 1..491
FT /note="Cytochrome P450 2B3"
FT /id="PRO_0000051680"
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 CONFLICT 364
FT /note="P -> Q (in Ref. 3; AAA41048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 56384 MW; 0B5ACB77577AAF29 CRC64;
MDTSVLLLLA VLLSFLLFLV RGHAKVHGHL PPGPRPLPLL GNLLQMDRGG FRKSFIQLQE
KHGDVFTVYF GPRPVVMLCG TQTIREALVD HAEAFSGRGI IAVLQPIMQE YGVSFVNEER
WKILRRLFVA TMRDFGIGKQ SVEDQIKEEA KCLVEELKNH QGVSLDPTFL FQCVTGNIIC
SIVFGERFDY RDRQFLRLLD LLYRTFSLIS SFSSQMFEVY SDFLKYFPGV HREIYKNLKE
VLDYIDHSVE NHRATLDPNA PRDFIDTFLL HMEKEKLNHY TEFHHWNLMI SVLFLFLAGT
ESTSNTLCYG FLLMLKYPHV AEKVQKEIDQ VIGSQRVPTL DDRSKMPYTE AVIHEIQRFS
DVSPMGLPCR ITKDTLFRGY LLPKNTEVYF ILSSALHDPQ YFEQPDTFNP EHFLDANGAL
KKCEAFMPFS IGKRMCLGEG IARSELFLFF TTILQNYSVS SPVDPNTIDM TPKESGLAKV
APVYKICFVA R
