ID   CP2BC_RAT               Reviewed;         492 AA.
AC   P33272;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Cytochrome P450 2B12;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIB12;
GN   Name=Cyp2b12; Synonyms=Cyp2b-12;
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=1445240; DOI=10.1042/bj2870775;
RA   Friedberg T., Grassow M.A., Bartlomowicz-Oesch B., Siegert P., Arand M.,
RA   Adesnik M., Oesch F.;
RT   "Sequence of a novel cytochrome CYP2B cDNA coding for a protein which is
RT   expressed in a sebaceous gland, but not in the liver.";
RL   Biochem. J. 287:775-783(1992).
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. This isozyme seems responsible for
CC       metabolism of 2,2',4,4',5,5'-hexachlorobiphenyl.
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: Preputial gland, but not in liver.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; X63545; CAA45107.1; -; mRNA.
DR   PIR; S27160; S27160.
DR   RefSeq; NP_058852.1; NM_017156.1.
DR   AlphaFoldDB; P33272; -.
DR   SMR; P33272; -.
DR   STRING; 10116.ENSRNOP00000048784; -.
DR   PaxDb; P33272; -.
DR   PRIDE; P33272; -.
DR   GeneID; 29295; -.
DR   KEGG; rno:29295; -.
DR   CTD; 29295; -.
DR   RGD; 620088; Cyp2b12.
DR   eggNOG; KOG0156; Eukaryota.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; P33272; -.
DR   PRO; PR:P33272; -.
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; IDA:RGD.
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: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:0019373; P:epoxygenase P450 pathway; IDA:RGD.
DR   GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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 2B12"
FT                   /id="PRO_0000051687"
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"
FT                   /evidence="ECO:0000250|UniProtKB:P00176"
SQ   SEQUENCE   492 AA;  55797 MW;  A21B1D4F9D77445B CRC64;
     MEFGVLLLLT LTVGFLLFLV SQSQPKTHGH LPPGPRPLPF LGNLLQMNRR GFLNSFMQLQ
     EKYGDVFTVH LGPRPVVILC GTDTIREALV DQAEAFSGRG TVAVLHPVVQ GYGVIFATGE
     RWKTLRRFSL VTMKEFGMGK RSVDERIKEE AQCLVEELKK YKGAPLNPTF LFQSIAANTI
     CSIVFGERFD YKDHQFLHLL DLVYKTSVLM GSLSSQVFEL YSGFLKYFPG AHKQIFKNLQ
     EMLNYIGHIV EKHRATLDPS APRDFIDTYL LRMEKEKSNH HTEFNHQNLV ISVLSLFFAG
     TETTSTTLRC TFLIMLKYPH VAEKVQKEID QVIGSHRLPT PDDRTKMPYT DAVIHEIQRF
     ADLTPIGLPH RVTKDTVFRG YLLPKNTEVY PILSSALHDP RYFEQPDTFN PEHFLDANGA
     LKKSEAFLPF STGKRICLGE GIARNELFIF FTAILQNFTL ASPVAPEDID LTPINIGVGK
     IPSPYQINFL SR