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 24-JAN-2024, entry version 117.
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}.
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; 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.ENSMAUP00000004849; -.
DR GeneID; 101832144; -.
DR KEGG; ag:BAA02003; -.
DR KEGG; maua:101832144; -.
DR eggNOG; KOG0156; Eukaryota.
DR OrthoDB; 2900138at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0019369; P:arachidonic acid metabolic process; IEA:Ensembl.
DR GO; GO:0043651; P:linoleic acid metabolic process; IEA:Ensembl.
DR CDD; cd20665; CYP2C-like; 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 PANTHER; PTHR24300:SF342; CYTOCHROME P450 2C55; 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 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
//
