CP2CF_RABIT
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 03-AUG-2022, entry version 114.
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 + 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: 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}.
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DR EMBL; M19234; AAA31218.1; -; mRNA.
DR PIR; B27718; B27718.
DR AlphaFoldDB; P11372; -.
DR SMR; P11372; -.
DR STRING; 9986.ENSOCUP00000012210; -.
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:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
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; 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