CP2B2_RAT
ID CP2B2_RAT Reviewed; 491 AA.
AC P04167; Q64579; Q64582;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cytochrome P450 2B2;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIB2;
DE AltName: Full=Cytochrome P450 PB4;
DE AltName: Full=Cytochrome P450E;
GN Name=Cyp2b2; Synonyms=Cyp2b-2;
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 [GENOMIC DNA] (ISOFORM 1).
RX PubMed=6306654; DOI=10.1073/pnas.80.13.3958;
RA Mizukami Y., Sogawa K., Suwa Y., Muramatsu M., Fujii-Kuriyama Y.;
RT "Gene structure of a phenobarbital-inducible cytochrome P-450 in rat
RT liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3958-3962(1983).
RN [2]
RP PROTEIN SEQUENCE (ISOFORM 1).
RX PubMed=3877725; DOI=10.1016/s0021-9258(18)95729-7;
RA Frey A.B., Waxman D.J., Kreibich G.;
RT "The structure of phenobarbital-inducible rat liver cytochrome P-450
RT isoenzyme PB-4. Production and characterization of site-specific
RT antibodies.";
RL J. Biol. Chem. 260:15253-15265(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-491 (ISOFORM 2).
RX PubMed=2323573; DOI=10.1016/0378-1119(90)90280-5;
RA Lacroix D., Desrochers M., Lambert M., Anderson A.;
RT "Alternative splicing of mRNA encoding rat liver cytochrome P450e
RT (P450IIB2).";
RL Gene 86:201-207(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 168-491 (ISOFORM 1).
RX PubMed=6689485; DOI=10.1016/0378-1119(83)90034-3;
RA Phillips I.R., Shephard E.A., Ashworth A., Rabin B.R.;
RT "Cloning and sequence analysis of a rat liver cDNA coding for a
RT phenobarbital-inducible microheterogenous cytochrome P-450 variant:
RT regulation of its messenger level by xenobiotics.";
RL Gene 26:41-52(1983).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 281-491.
RX PubMed=6688421; DOI=10.1016/s0021-9258(17)44415-2;
RA Kumar A., Raphael C., Adesnik M.;
RT "Cloned cytochrome P-450 cDNA. Nucleotide sequence and homology to multiple
RT phenobarbital-induced mRNA species.";
RL J. Biol. Chem. 258:11280-11284(1983).
RN [6]
RP ERRATUM OF PUBMED:6688421.
RA Kumar A., Raphael C., Adesnik M.;
RL J. Biol. Chem. 259:6039-6039(1984).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 323-431.
RX PubMed=3458196; DOI=10.1073/pnas.83.8.2300;
RA Atchison M.L., Adesnik M.;
RT "Gene conversion in a cytochrome P-450 gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2300-2304(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 329-380 AND 402-423.
RX PubMed=2539047; DOI=10.1016/0003-9861(89)90003-9;
RA Oesch F., Waxman D.J., Morrissey J.J., Honscha W., Kissel W., Friedberg T.;
RT "Antibodies targeted against hypervariable and constant regions of
RT cytochromes P450IIB1 and P450IIB2.";
RL Arch. Biochem. Biophys. 270:23-32(1989).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 385-491.
RX PubMed=6322758; DOI=10.1016/0006-291x(84)91353-6;
RA Affolter M., Anderson A.;
RT "Segmental homologies in the coding and 3' non-coding sequences of rat
RT liver cytochrome P-450e and P-450b cDNAs and cytochrome P-450e-like
RT genes.";
RL Biochem. Biophys. Res. Commun. 118:655-662(1984).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RX PubMed=2839467; DOI=10.1093/oxfordjournals.jbchem.a122297;
RA Hashimoto T., Matsumoto T., Nishizawa M., Kawabata S., Morohashi K.,
RA Handa S., Omura T.;
RT "A mutant rat strain deficient in induction of a phenobarbital-inducible
RT form of cytochrome P-450 in liver microsomes.";
RL J. Biochem. 103:487-492(1988).
RN [11]
RP PROTEIN SEQUENCE OF 1-20.
RC TISSUE=Liver;
RX PubMed=3041969; DOI=10.1016/0006-2952(88)90634-x;
RA Amelizad Z., Narbonne J.F., Wolf C.R., Robertson L.W., Oesch F.;
RT "Effect of nutritional imbalances on cytochrome P-450 isozymes in rat
RT liver.";
RL Biochem. Pharmacol. 37:3245-3249(1988).
RN [12]
RP PHOSPHORYLATION AT SER-128.
RX PubMed=2583091; DOI=10.1002/j.1460-2075.1989.tb08450.x;
RA Pyerin W., Taniguchi H.;
RT "Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450.";
RL EMBO J. 8:3003-3010(1989).
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=P04167-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04167-2; Sequence=VSP_011939;
CC -!- INDUCTION: By phenobarbital.
CC -!- PTM: Phosphorylation is accompanied by a decrease in enzyme activity.
CC {ECO:0000269|PubMed:2583091}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; J00728; AAA41056.1; -; Genomic_DNA.
DR EMBL; J00720; AAA41056.1; JOINED; Genomic_DNA.
DR EMBL; J00721; AAA41056.1; JOINED; Genomic_DNA.
DR EMBL; J00722; AAA41056.1; JOINED; Genomic_DNA.
DR EMBL; J00723; AAA41056.1; JOINED; Genomic_DNA.
DR EMBL; J00724; AAA41056.1; JOINED; Genomic_DNA.
DR EMBL; J00725; AAA41056.1; JOINED; Genomic_DNA.
DR EMBL; J00726; AAA41056.1; JOINED; Genomic_DNA.
DR EMBL; M34452; AAA41004.1; -; mRNA.
DR EMBL; K01721; AAA41026.1; -; mRNA.
DR EMBL; K00996; AAA41029.1; -; mRNA.
DR EMBL; M13234; AAA41057.1; -; Genomic_DNA.
DR EMBL; K01626; AAA41037.1; -; mRNA.
DR EMBL; D00250; BAA00181.1; -; Genomic_DNA.
DR PIR; A21162; O4RTP2.
DR PIR; A60822; A60822.
DR RefSeq; NP_001185605.1; NM_001198676.1.
DR AlphaFoldDB; P04167; -.
DR SMR; P04167; -.
DR STRING; 10116.ENSRNOP00000045196; -.
DR DrugBank; DB08834; Tauroursodeoxycholic acid.
DR iPTMnet; P04167; -.
DR PaxDb; P04167; -.
DR PeptideAtlas; P04167; -.
DR GeneID; 361523; -.
DR KEGG; rno:361523; -.
DR UCSC; RGD:2467; rat. [P04167-1]
DR CTD; 361523; -.
DR RGD; 2467; Cyp2b2.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P04167; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P04167; -.
DR PRO; PR:P04167; -.
DR Proteomes; UP000002494; Unplaced.
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:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IDA: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; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0018933; P:nicotine metabolic process; IEP:RGD.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0010038; P:response to metal ion; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA: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 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..491
FT /note="Cytochrome P450 2B2"
FT /id="PRO_0000051679"
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 MOD_RES 128
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:2583091"
FT VAR_SEQ 274
FT /note="K -> KVSPAWMRE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2323573"
FT /id="VSP_011939"
FT CONFLICT 114
FT /note="I -> F (in Ref. 3; AAA41004)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="L -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="T -> A (in Ref. 2; AA sequence and 5; AAA41029)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="E -> V (in Ref. 1; AAA41056)"
FT /evidence="ECO:0000305"
FT CONFLICT 359..360
FT /note="FA -> AS (in Ref. 8; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="G -> D (in Ref. 5; AAA41029)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="N -> K (in Ref. 4; AAA41026)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="K -> M (in Ref. 1; AAA41056)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="G -> D (in Ref. 2; AA sequence and 5; AAA41029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 55933 MW; 00CB6B937FDD44BC CRC64;
MEPSILLLLA LLVGFLLLLV RGHPKSRGNF PPGPRPLPLL GNLLQLDRGG LLNSFMQLRE
KYGDVFTVHL GPRPVVMLCG TDTIKEALVG QAEDFSGRGT IAVIEPIFKE YGVIFANGER
WKALRRFSLA TMRDFGMGKR SVEERIQEEA QCLVEELRKS QGAPLDPTFL FQCITANIIC
SIVFGERFDY TDRQFLRLLE LFYRTFSLLS SFSSQVFEFF SGFLKYFPGA HRQISKNLQE
ILDYIGHIVE KHRATLDPSA PRDFIDTYLL RMEKEKSNHH TEFHHENLMI SLLSLFFAGT
ETGSTTLRYG FLLMLKYPHV TEKVQKEIDQ VIGSHRPPSL DDRTKMPYTD AVIHEIQRFA
DLAPIGLPHR VTKDTMFRGY LLPKNTEVYP ILSSALHDPQ YFDHPDTFNP EHFLDADGTL
KKSEAFMPFS TGKRICLGEG IARNELFLFF TTILQNFSVS SHLAPKDIDL TPKESGIAKI
PPTYQICFSA R
