ID   CP242_PIG               Reviewed;         327 AA.
AC   P79402;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Cytochrome P450 2C42;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC42;
DE   Flags: Fragment;
GN   Name=CYP2C42;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Small intestine;
RX   PubMed=9682441; DOI=10.1046/j.1365-2052.1998.00225.x;
RA   Nissen P.H., Winteroe A.K., Fredholm M.;
RT   "Mapping of porcine genes belonging to two different cytochrome P450
RT   subfamilies.";
RL   Anim. Genet. 29:7-11(1998).
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; Z93098; CAB07512.1; -; mRNA.
DR   AlphaFoldDB; P79402; -.
DR   SMR; P79402; -.
DR   STRING; 9823.ENSSSCP00000021926; -.
DR   PaxDb; P79402; -.
DR   PeptideAtlas; P79402; -.
DR   PRIDE; P79402; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_22_3_1; -.
DR   InParanoid; P79402; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; P79402; SS.
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; 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..327
FT                   /note="Cytochrome P450 2C42"
FT                   /id="PRO_0000051725"
FT   BINDING         272
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   327 AA;  37458 MW;  0EA0CA0E1B9B94D9 CRC64;
     CDPTFILDCA PCNVICSIIF QNRFDYTDQD FLTLLEKFHE NLNILSSPWI QVCNNFPALI
     DYSPGIHNKL LKNIAYLKSY VLKKVKEHQE SLDINNPRDF IDCFLIKMEQ EKHNQQSEYT
     IENLIATVSD MFSAGTETTS TTMRYGLLLL LKHPEVTAKV QEEIDRVIGR HRSACMQDRS
     HMPYTDAVVH EIQRYIDLVP TNLPHAVTCD IKFRNYLIPK GTTILTSLTS VLYDCKAFPN
     PEVFDPGHFL DESGNFKKSD YFMPFSTGKR ICVGEGLARM ELFLFLTTIL QKFNLKSVVD
     PKDIDTTPVA NGFASVPPFY QICFIPL