ID   CP2CS_MESAU             Reviewed;         490 AA.
AC   P33265;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Cytochrome P450 2C28;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC28;
DE   AltName: Full=Cytochrome P450 HSM4;
GN   Name=CYP2C28;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7771794; DOI=10.1006/abbi.1995.1291;
RA   Sakuma T., Yokoi T., Kamataki T.;
RT   "Isolation and characterization of a new cDNA clone belonging to the
RT   cytochrome P450 2C gene subfamily in hamsters.";
RL   Arch. Biochem. Biophys. 319:267-273(1995).
CC   -!- FUNCTION: Catalyzes the N-demethylation of aminopyrine and
CC       benzphetamine, but does not catalyze the hydroxylation of tolbutamide,
CC       testosterone, and progesterone.
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   -!- TISSUE SPECIFICITY: Liver.
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; D11437; BAA02003.1; -; mRNA.
DR   PIR; I48164; I48164.
DR   RefSeq; NP_001268612.1; NM_001281683.1.
DR   AlphaFoldDB; P33265; -.
DR   SMR; P33265; -.
DR   STRING; 10036.XP_005063684.1; -.
DR   GeneID; 101832144; -.
DR   KEGG; ag:BAA02003; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   OrthoDB; 702827at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0008392; F:arachidonic acid epoxygenase activity; IEA:Ensembl.
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   GO; GO:0071614; F:linoleic acid epoxygenase activity; IEA:Ensembl.
DR   GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; IEA:Ensembl.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0043651; P:linoleic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0042573; P:retinoic acid metabolic process; IEA:Ensembl.
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   Acetylation; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW   Microsome; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..490
FT                   /note="Cytochrome P450 2C28"
FT                   /id="PRO_0000051716"
FT   BINDING         435
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         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P00176"
FT   MOD_RES         249
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64458"
FT   MOD_RES         375
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64458"
SQ   SEQUENCE   490 AA;  55703 MW;  DD567183B3A51801 CRC64;
     MDPVLVLVLT LSCLLLFSVW RQSSGRGRLP PGPTPLPLIG NILQIDIKDI SKSLANFSKV
     YGPVFTLYFG TKPTVVVHGY EAVKEALEDL GEEFSGRGNF PIVERMNSGL GIIFSNGTKW
     KELRRFSLMT LRNFGMGKRS IEDCIQEEAR CLVEELRKTN GSPCDPTFFL SCAPSNVICS
     VVFHNRFDYN DKNFLNLMEK LNENFEILNS PWLQVCNVIP AFLDYLPGSH NKALKNFAEI
     KSYILKRVKE HQETLDMNNP RDFIDCFLIK MEKEKDNPHS EFTTESLMAT VADVFVAGSE
     TTSTTLRYGL LLLLKHKEVT AKVQKEIDHV IGRDRSPCMQ DRTRMPYTDA MVHEVQRYVN
     LIPNNVPHAA TCNVKFRNYV IPKGTDLITS LTSVLHDDKE FPNPKIFDPA HFLDENGNFK
     KSDYFMPFSI GKRMCMGEAL ARMELFLLLT TILQNFDLKS LADTKDIDTT PVASTFGCVP
     PSYQLYFIPR