CP2A9_MESAU
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 03-AUG-2022, entry version 114.
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.XP_005086639.1; -.
DR GeneID; 101826326; -.
DR KEGG; ag:BAA25259; -.
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; IPR008067; Cyt_P450_E_grp-I_CYP2A-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01684; EP450ICYP2A.
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..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