ID   CP2BF_RAT               Reviewed;         495 AA.
AC   Q64583;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Cytochrome P450 2B15;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIB15;
GN   Name=Cyp2b15;
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].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=8294026; DOI=10.1016/0378-1119(93)90490-t;
RA   Nakayama K., Suwa Y., Mizukami Y., Sogawa K., Fujii-Kuriyama Y.;
RT   "Cloning and sequencing of a novel rat cytochrome P450 2B-encoding gene.";
RL   Gene 136:333-336(1993).
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       (By similarity). {ECO:0000250}.
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 {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Microsome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D17349; BAB72140.1; -; Genomic_DNA.
DR   PIR; I53690; I53690.
DR   PIR; I67791; I67791.
DR   RefSeq; NP_001129140.1; NM_001135668.1.
DR   AlphaFoldDB; Q64583; -.
DR   SMR; Q64583; -.
DR   STRING; 10116.ENSRNOP00000002054; -.
DR   iPTMnet; Q64583; -.
DR   PhosphoSitePlus; Q64583; -.
DR   PaxDb; Q64583; -.
DR   PRIDE; Q64583; -.
DR   GeneID; 685222; -.
DR   KEGG; rno:685222; -.
DR   UCSC; RGD:620088; rat.
DR   CTD; 685222; -.
DR   RGD; 1596474; Cyp2b15.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; Q64583; -.
DR   OrthoDB; 702827at2759; -.
DR   PhylomeDB; Q64583; -.
DR   PRO; PR:Q64583; -.
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: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; IBA:GO_Central.
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   3: Inferred from homology;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..495
FT                   /note="Cytochrome P450 2B15"
FT                   /id="PRO_0000051688"
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   495 AA;  56320 MW;  035C2E084E0B26C3 CRC64;
     MELGVLLLLT FTVGFLLLLA SQNRPKTHGH LPPGPRPLPF LGNLLQMNRR GLLRSFMQLQ
     EKYGDVFTVH LGPRPVVILC GTDTIREALV DQAEAFSGRG TVAVLHPVVQ GYGVIFANGE
     RWKILRRFSL VTMRNFGMGK RSVEERIKEE AQCLVEELKK YKGALLNPTS IFQSIAANII
     CSIVFGERFD YKDHQFLRLL DLIYQTFSLM GSLSSQVFEL FSGFLKYFPG VHKQISKNLQ
     EILNYIDHSV EKHRATLDPN TPRDFINTYL LRMEKEKSNH HTEFHHQNLV ISVLSLFFTG
     TETTSTTLRY SFLIMLKYPH VAEKVQKEID QVIGSHRLPT LDDRTKMPYT DAVIHEIQRF
     ADLIPIGLPH RVTNDTMFLG YLLPKNTEVY PILSSALHDP RYFDHPDTFN PEHFLDVNGT
     LKKSEAFLPF STGKRICLGE GIAQNELFIF FTAILQNFSL ASPVAPEDID LSPINSGISK
     IPSPYQIHFL SRCVG