ID   CP2DR_MESAU             Reviewed;         500 AA.
AC   Q9QYG6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cytochrome P450 2D27;
DE            EC=1.14.14.-;
DE   AltName: Full=CYPIID27;
GN   Name=CYP2D27;
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], AND CHARACTERIZATION.
RX   PubMed=11083025; DOI=10.1016/s0742-8413(00)00142-0;
RA   Oka T., Fukuhara M., Ushio F., Kurose K.;
RT   "Molecular cloning and characterization of three novel cytochrome P450 2D
RT   isoforms, CYP2D20, CYP2D27, and CYP2D28 in the Syrian hamster (Mesocricetus
RT   auratus).";
RL   Comp. Biochem. Physiol. 127C:143-152(2000).
CC   -!- FUNCTION: Has bufuralol 1'-hydroxylase and debrisoquine 4-hydroxylase
CC       activities.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Microsome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, but not in kidney, small
CC       intestine, and brain.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AB031863; BAA89312.1; -; mRNA.
DR   AlphaFoldDB; Q9QYG6; -.
DR   SMR; Q9QYG6; -.
DR   PRIDE; Q9QYG6; -.
DR   Proteomes; UP000189706; 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: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; IPR008069; Cyt_P450_E_grp-I_CYP2D-like.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01686; EP450ICYP2D.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..500
FT                   /note="Cytochrome P450 2D27"
FT                   /id="PRO_0000051748"
FT   BINDING         446
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   500 AA;  56489 MW;  7A5DE5878F97A954 CRC64;
     MALLIGDGLW SGVIFTALFL LLVDLMHRRK FWRARYPPGP MPLPGLGNLL QVDFEHMPYS
     LYKFRQRYGD VFSLQMAWKP VVVINGLKAV REVLVNCGED TADRPPVPIF NHVGFGHNSQ
     GVAFARYGPQ WREQRRFCVS TMRDFGVGKK SLEQWVTEEA GHLCDAFTQE AGHPFNPTTL
     LNKSVCNVIS SLIYAHRFDY EDPFFNSLLK MLQESFGEDT GFIAEVLNAV PVLLRIPGLP
     GKAFPKLTAF MDSLYKMLIE HKTTWDPAQP PRGLTDAFLA EVEKAKGRPE SSFNDENLRM
     VVADMFIAGM VTTSTTLSWA LLLMILHPDV QSRVQQEIDD VIGQVRRPEM ADQARMPYTN
     AVIHEVQRFG DIAPVNIPHM TSHDVEVQGF LIPKGTTLIP NLSSVLKDET VWEKPLHFHP
     EHFLDAQGRF VKHEAFMPFS AGRRACLGEP LARMELFLFF TCLLQRFSFS VPAGQPRPSD
     QGIFALPVTP TPYELCAVVR