CP2CR_MESAU
ID CP2CR_MESAU Reviewed; 490 AA.
AC P33264;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytochrome P450 2C27;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIC27;
DE AltName: Full=Cytochrome P450 HSM3;
GN Name=CYP2C27;
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 -!- TISSUE SPECIFICITY: Specifically expressed by males in kidneys.
CC Expressed predominantly by males in livers.
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; D11436; BAA02002.1; -; mRNA.
DR PIR; I48163; I48163.
DR RefSeq; NP_001268504.1; NM_001281575.1.
DR AlphaFoldDB; P33264; -.
DR SMR; P33264; -.
DR GeneID; 101841752; -.
DR KEGG; ag:BAA02002; -.
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 2C27"
FT /id="PRO_0000051715"
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; 55767 MW; 450A208070D60D0A CRC64;
MDAFVVLVFI LSCLFLLSLW RQSSERGKLP PGPTPLPLIG NFFQIDVKDI SGSLTNFSKV
YGPVFTLYLG RKPAVVLHGY EAVKEALIDH GEEFAGRGSF PMAERYNKGL GIVFSNGNRW
KDIRRFSLMA LRSLGMGKRS IEDRVQEEAQ CLVEELRKTN GSPCDPTFIL SCAPCNVICS
IIFQNRFDYT DQDFLTFMEK VNENVRILSS PWLQVCNNFP SLIDYCPGSH HTITKNVNYI
RSYLSEKIKE HQETLDVANP RDFIDYYLIK LKQGNYNQQS EFTLENLATT VRDLFAAGTE
TTSTTLRYAL LLLLKHPHVT AKVQEEIDQV VGRHRNPCMQ DRSHMPYTDA MIHEVQRFID
LIPTNLPHAV TCDIKFRDYF IPKGTTIITS LSSVLHDSKE FPNPEVFDPG HFLDKNGKFK
KSDYFMPFST GKRMCAGEGL ARMELFLFLT TILQNFKLKS LVHPKDIDTT PVVNGLASLP
PSYQLCFIPV