ID   CP2CV_CAPHE             Reviewed;         284 AA.
AC   Q29478;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Cytochrome P450 2C31;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC31;
DE   Flags: Fragment;
GN   Name=CYP2C31;
OS   Capra hircus aegagrus (Wild goat) (Capra aegagrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9923;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=West-African dwarf; TISSUE=Liver;
RX   PubMed=7513154; DOI=10.1006/bbrc.1994.1423;
RA   Zeilmaker W.M., van 't Klooster G.A.E., Gremmels-Gehrmann J.F.,
RA   van Miert A.S.J.P.A., Horbach G.J.M.J.;
RT   "cDNA and deduced amino acid sequence of a dwarf goat liver cytochrome P450
RT   fragment belonging to the CYP2C gene subfamily.";
RL   Biochem. Biophys. Res. Commun. 200:120-125(1994).
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; X76502; CAA54037.1; -; mRNA.
DR   AlphaFoldDB; Q29478; -.
DR   SMR; Q29478; -.
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.
FT   CHAIN           <1..284
FT                   /note="Cytochrome P450 2C31"
FT                   /id="PRO_0000051719"
FT   BINDING         229
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   NON_TER         1
SQ   SEQUENCE   284 AA;  32627 MW;  C0A69EEAEC29E185 CRC64;
     LVSTPWIELF NAFPSLLRHF PGSHNTIFKN MTEQRKFILE EIKKHQESLD LNNPQDFIDY
     FLIKMEKEKH NKHSEFTMDN LITTVWDVFS AGTETTSLTL RYGLLLLLKH PEVTAKVQEE
     IDRVVGRNRS PCMQDRSRMP YTDAVLHEIQ RYIDLVPSNL PHVATQDVKF REYLIPKGTA
     ILTSLTSVLH DGKEFPNPGQ FDPAHFLDES GNFKKTDHFM AFSAGKRVCV GEGLARMELF
     LLLVSILQHF TLKPVVDPKH IDIAPSFKGM LSIPPFCEMC FIPV