ID   CP2CQ_MESAU             Reviewed;         490 AA.
AC   P33263;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 122.
DE   RecName: Full=Cytochrome P450 2C26;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIC26;
DE   AltName: Full=Cytochrome P450 HSM2;
GN   Name=CYP2C26;
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=8114672; DOI=10.1016/s0026-895x(25)09918-3;
RA   Sakuma T., Masaki K., Itoh S., Yokoi T., Kamataki T.;
RT   "Sex-related differences in the expression of cytochrome P450 in hamsters:
RT   cDNA cloning and examination of the expression of three distinct CYP2C
RT   cDNAs.";
RL   Mol. Pharmacol. 45:228-236(1994).
CC   -!- FUNCTION: Catalyzes the hydroxylation of tolbutamide and the N-
CC       demethylation of aminopyrine and benzphetamine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + reduced [NADPH--hemoprotein reductase] +
CC         O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O +
CC         H(+); 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; D11435; BAA02001.1; -; mRNA.
DR   PIR; I48162; I48162.
DR   RefSeq; NP_001268582.1; NM_001281653.1.
DR   AlphaFoldDB; P33263; -.
DR   SMR; P33263; -.
DR   STRING; 10036.ENSMAUP00000001742; -.
DR   Ensembl; ENSMAUT00000001780; ENSMAUP00000001742; ENSMAUG00000001291.
DR   GeneID; 101831088; -.
DR   KEGG; ag:BAA02001; -.
DR   KEGG; maua:101831088; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000154299; -.
DR   OrthoDB; 1103324at2759; -.
DR   Proteomes; UP000886700; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IEA:TreeGrafter.
DR   CDD; cd20665; CYP2C-like; 1.
DR   FunFam; 1.10.630.10:FF:000299; Cytochrome P450 2C9; 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   InterPro; IPR050182; Cytochrome_P450_fam2.
DR   PANTHER; PTHR24300:SF384; CYTOCHROME P450 2C29-RELATED; 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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..490
FT                   /note="Cytochrome P450 2C26"
FT                   /id="PRO_0000051714"
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"
SQ   SEQUENCE   490 AA;  55724 MW;  01C4F6DB99772D24 CRC64;
     MDAFVVLVFI LSCLFLLSLW RQSSERGKLP PGPTPLPIIG NFLQIDVKDI SGSLTNFSKV
     YGPVFTLYLG MKPTVVLHGY EAVKEALIDH GEEFAGRGSF PVAERVNKGL GIVFSNGSRW
     KETRRFSLMT LRNLGMGKRS IEDRVQEEAQ CLVEELRKTN GSPCDPTFIL GCAPCNVICS
     IIFQNRFDYK DKDFLTFMKK LNENARILSS PWFQVCNNFP LLIDYCPGSH HRITKNINYI
     RSYLSEKMKE HQESLDVANP RDFIDYYLIK LKQGNYNQQS EFSPENLATT VSDLFAAGTE
     TTSTTLRYAL LLLLKHPHVT AKVQEEIDQV VGRHRNPCMQ DRSHMPYTDA MIHEVQRFID
     LIPTNLPHAV TCDIKFRDYF IPKGTTIITS LSSVLHDSKE FPNPEVFDPG HFLDKNGNFK
     KSDYFMPFST GKRMCAGEGL ARMELFLFLT TILQNFKLKS LVHPKDIDTT PVLNGFASLP
     PSYQLCFIPV
//