ID   CP2BB_CANLF             Reviewed;         494 AA.
AC   P24460;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Cytochrome P450 2B11;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIB11;
DE   AltName: Full=Cytochrome P450 PBD-2;
GN   Name=CYP2B11;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle; TISSUE=Liver;
RX   PubMed=2116765; DOI=10.1016/0003-9861(90)90419-y;
RA   Graves P.E., Elhag G.A., Ciaccio P.J., Bourque D.P., Halpert J.R.;
RT   "cDNA and deduced amino acid sequences of a dog hepatic cytochrome P450IIB
RT   responsible for the metabolism of 2,2',4,4',5,5'-hexachlorobiphenyl.";
RL   Arch. Biochem. Biophys. 281:106-115(1990).
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   -!- INDUCTION: By phenobarbital.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M92447; AAA30881.1; -; mRNA.
DR   PIR; S11305; S11305.
DR   RefSeq; NP_001006653.1; NM_001006652.1.
DR   AlphaFoldDB; P24460; -.
DR   SMR; P24460; -.
DR   STRING; 9612.ENSCAFP00000032358; -.
DR   BindingDB; P24460; -.
DR   ChEMBL; CHEMBL1907981; -.
DR   PaxDb; P24460; -.
DR   GeneID; 474177; -.
DR   KEGG; cfa:474177; -.
DR   CTD; 1555; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P24460; -.
DR   OrthoDB; 702827at2759; -.
DR   SABIO-RK; P24460; -.
DR   PRO; PR:P24460; -.
DR   Proteomes; UP000002254; 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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..494
FT                   /note="Cytochrome P450 2B11"
FT                   /id="PRO_0000051686"
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                   /evidence="ECO:0000250"
FT   MOD_RES         128
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  56267 MW;  8E9EA639B4B5E4D3 CRC64;
     MELSVLLLLA LLTGLLLLMA RGHPKAYGHL PPGPRPLPIL GNFLQMDRKG LLKSFLRLQE
     KYGDVFTVYL GPRRTVMLCG IDAIREALVD NAEAFSGRGK IAVVEPVFQG YGVVFANGER
     WKTLRRFSLA TMRDFGMGKR SVEERIQEEA QCLVEELRKT EGVLQDPTFF FHSMTANIIC
     SIVFGKRFGY KDPEFLRLMN LFYVSFALIS SFSSQMFELF HSFLKYFPGT HRQVYNNLQE
     IKAFIARMVE KHRETLDPSA PRDFIDAYLI RMDKEKAEPS SEFHHRNLID TALSLFFAGT
     ETTSTTLRYG FLLMLKYPHI AERIYKEIDQ VIGPHRLPSL DDRAKMPYTD AVIHEIQRFG
     DLLPIGVPHM VTKDICFRGY IIPKGTEVFP ILHSALNDPH YFEKPDVFNP DHFLDANGAL
     KKNEAFIPFS IGKRICLGEG IARMELFLFF TTILQNFSVA SPMAPEDIDL TPQEIGVGKL
     PPVYQISFLS RGGC