ID   CP2CF_RABIT             Reviewed;         378 AA.
AC   P11372;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 125.
DE   RecName: Full=Cytochrome P450 2C15;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC15;
DE   AltName: Full=Cytochrome P450 B32-3;
DE   Flags: Fragment;
GN   Name=CYP2C15;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2831965; DOI=10.1021/bi00401a014;
RA   Imai Y., Komori M., Sato R.;
RT   "Comparison of primary structures deduced from cDNA nucleotide sequences
RT   for various forms of liver microsomal cytochrome P-450 from phenobarbital-
RT   treated rabbits.";
RL   Biochemistry 27:80-88(1988).
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 + reduced [NADPH--hemoprotein reductase] +
CC         O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O +
CC         H(+); 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: P450 can be induced to high levels in liver and other
CC       tissues by various foreign compounds, including drugs, pesticides, and
CC       carcinogens.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M19234; AAA31218.1; -; mRNA.
DR   PIR; B27718; B27718.
DR   AlphaFoldDB; P11372; -.
DR   SMR; P11372; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P11372; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IEA:TreeGrafter.
DR   CDD; cd20665; CYP2C-like; 1.
DR   FunFam; 1.10.630.10:FF:000299; Cytochrome P450 2C9; 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; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR050182; Cytochrome_P450_fam2.
DR   PANTHER; PTHR24300:SF400; CYTOCHROME P450 2C9; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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; Reference proteome.
FT   CHAIN           <1..378
FT                   /note="Cytochrome P450 2C15"
FT                   /id="PRO_0000051705"
FT   BINDING         323
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   NON_TER         1
SQ   SEQUENCE   378 AA;  43514 MW;  14D524173EB07480 CRC64;
     LGILFSNANT WKEMRRFSLM TLRNFGMGKR SIEDRVQEEA RCLVEELRKT NASPCDPTFI
     LGCAPCNVIC SIIFHNRFDY KDEHFLKLME KFNENVRILS SPWLQICNNF PVLTDYLPGI
     HNTLVKNIEY TKNFIMEKVK EHQKSLDVNN PRDFIDCFLI KMDQENHLEF TLESLVTTVS
     DLFGAGTETT STTLSISLLL LLKHPEVAAK VQEEIERVIG RHRSPCMQDR SRMPYTDAVI
     HEIQRYIDLI PINLPHAVTR DIKFRNYFIP KGMNIITSLT SVLHDEKEFP NPKVFDPGHF
     LDESGNFKKS DYFMPFSAGK RMCVGEGLAR MELFLFLTSI LQNFKLQSLV EPKDLDITAV
     VNGFASVPPA YQLCFSPV
//