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   27-MAR-2024, entry version 176.
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   iPTMnet; P04167; -.
DR   PaxDb; 10116-ENSRNOP00000045196; -.
DR   PeptideAtlas; P04167; -.
DR   GeneID; 361523; -.
DR   KEGG; rno:361523; -.
DR   UCSC; RGD:2467; rat. [P04167-1]
DR   AGR; RGD:2467; -.
DR   CTD; 361523; -.
DR   RGD; 2467; Cyp2b2.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P04167; -.
DR   OrthoDB; 2900138at2759; -.
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; IBA:GO_Central.
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:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR   GO; GO:0018933; P:nicotine metabolic process; IEP:RGD.
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   CDD; cd20672; CYP2B; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   PANTHER; PTHR24300:SF366; CYTOCHROME P450-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01685; EP450ICYP2B.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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
//