CP2CQ_MESAU
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 03-AUG-2022, entry version 111.
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;
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 + 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; 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.XP_005063678.1; -.
DR GeneID; 101831088; -.
DR KEGG; ag:BAA02001; -.
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: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; 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