ID   CP2A9_MESAU             Reviewed;         493 AA.
AC   P24455; O70538;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Cytochrome P450 2A9;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIA9;
DE   AltName: Full=Cytochrome P450-MC1-R;
DE   AltName: Full=Testosterone 7-alpha-hydroxylase;
GN   Name=CYP2A9;
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=9500848; DOI=10.1006/abbi.1997.0544;
RA   Kurose K., Tohkin M., Ushio F., Fukuhara M.;
RT   "Cloning and characterization of Syrian hamster testosterone 7 alpha-
RT   hydroxylase, CYP2A9.";
RL   Arch. Biochem. Biophys. 351:60-65(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 208-493.
RC   TISSUE=Liver;
RX   PubMed=2275554; DOI=10.1016/0003-9861(90)90664-k;
RA   Lai T.S., Chiang J.Y.L.;
RT   "Cloning and characterization of two major 3-methylcholanthrene inducible
RT   hamster liver cytochrome P450s.";
RL   Arch. Biochem. Biophys. 283:429-439(1990).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       In liver microsomes, this enzyme is involved in an NADPH-dependent
CC       electron transport pathway. It oxidizes a variety of structurally
CC       unrelated compounds, including steroids, fatty acids, and xenobiotics.
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; D86953; BAA25259.1; -; mRNA.
DR   EMBL; M63789; AAA37069.1; -; mRNA.
DR   RefSeq; NP_001268294.1; NM_001281365.1.
DR   AlphaFoldDB; P24455; -.
DR   SMR; P24455; -.
DR   STRING; 10036.ENSMAUP00000015892; -.
DR   GeneID; 101826326; -.
DR   KEGG; ag:BAA25259; -.
DR   KEGG; maua:101826326; -.
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: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   CDD; cd20668; CYP2A; 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; IPR008067; Cyt_P450_E_grp-I_CYP2A-like.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   PANTHER; PTHR24300:SF103; CYTOCHROME P450-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01684; EP450ICYP2A.
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..493
FT                   /note="Cytochrome P450 2A9"
FT                   /id="PRO_0000051672"
FT   BINDING         438
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   CONFLICT        367
FT                   /note="L -> C (in Ref. 2; AAA37069)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   493 AA;  56418 MW;  E7376475D21AEC10 CRC64;
     MLGSGLILVA ILAYLSVMVL VFVWKQKFRG KLPPGPTPLP YIGNYLQLNT KDIYSSITEL
     SERYGPVFTI YLGPRPVVVL YGYDAVKEAL VDQAEEFSGR GEQATYNTLF KDYGVAFSSG
     ERAKQLRRFS IATLRDFGVG KRGVEERIQE EAAYLIKMLR STRGAPIDPN DYLSQTVSNV
     ISSVVFGDAF DYEDKEFLEL LHMMNEMNKF AASPVGQLYD MFHSVMKYLP GPQQQIIKNT
     KELEDFMIRK VKQNQSTLDL NSARNFIDSF LIHMHEEKKN PTSEFNIKNL VMTSLNLFFA
     GSETVSSTIR YGFLLLMKYP EVEAKVHEEI DRVIGRNRQP QFEDRMKMPY TEAVINEIQR
     FANLAPLGIP RKTIKNTTFR GFFLPKDTDV YPILGSLLTD PKFFTSPKHF NPQNFLDDRG
     QLKKIAAFVP FSVGKRFCLG DGLARMELFL FLTTILQNFR LKFPKKLEDI DASPKPLGFS
     RIIPRYTMSF LPI
//