CP2A2_RAT
ID CP2A2_RAT Reviewed; 492 AA.
AC P15149; Q5EBB3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cytochrome P450 2A2;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIA2;
DE AltName: Full=Cytochrome P450-UT-4;
DE AltName: Full=Testosterone 15-alpha-hydroxylase;
GN Name=Cyp2a2; Synonyms=Cyp2a-2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=3192524; DOI=10.1016/s0021-9258(19)81314-5;
RA Matsunaga T., Nagata K., Holsztynska E.J., Lapenson D.P., Smith A.,
RA Kato R., Gelboin H.V., Waxman D.J., Gonzalez F.J.;
RT "Gene conversion and differential regulation in the rat P-450 IIA gene
RT subfamily. Purification, catalytic activity, cDNA and deduced amino acid
RT sequence, and regulation of an adult male-specific hepatic testosterone 15
RT alpha-hydroxylase.";
RL J. Biol. Chem. 263:17995-18002(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2322568; DOI=10.1021/bi00457a032;
RA Matsunaga T., Nomoto M., Kozak C.A., Gonzalez F.J.;
RT "Structure and in vitro transcription of the rat CYP2A1 and CYP2A2 genes
RT and regional localization of the CYP2A gene subfamily on mouse chromosome
RT 7.";
RL Biochemistry 29:1329-1341(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 1-27.
RC TISSUE=Liver;
RX PubMed=2434473; DOI=10.1093/oxfordjournals.jbchem.a121842;
RA Matsumoto T., Emi Y., Kawabata S., Omura T.;
RT "Purification and characterization of three male-specific and one female-
RT specific forms of cytochrome P-450 from rat liver microsomes.";
RL J. Biochem. 100:1359-1371(1986).
RN [5]
RP PROTEIN SEQUENCE OF 1-20.
RC TISSUE=Liver;
RX PubMed=2650624; DOI=10.1016/0003-9861(89)90526-2;
RA Arlotto M.P., Greenway D.J., Parkinson A.;
RT "Purification of two isozymes of rat liver microsomal cytochrome P450 with
RT testosterone 7 alpha-hydroxylase activity.";
RL Arch. Biochem. Biophys. 270:441-457(1989).
CC -!- FUNCTION: Highly active in the 15-alpha-hydroxylation of testosterone.
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 specific.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; J04187; AAA41424.1; -; mRNA.
DR EMBL; M34392; AAA41021.1; -; Genomic_DNA.
DR EMBL; M33313; AAA41021.1; JOINED; Genomic_DNA.
DR EMBL; M33325; AAA41021.1; JOINED; Genomic_DNA.
DR EMBL; BC089818; AAH89818.1; -; mRNA.
DR PIR; B34272; A31887.
DR RefSeq; NP_036825.1; NM_012693.1.
DR AlphaFoldDB; P15149; -.
DR SMR; P15149; -.
DR BindingDB; P15149; -.
DR ChEMBL; CHEMBL3705; -.
DR DrugBank; DB08834; Tauroursodeoxycholic acid.
DR PRIDE; P15149; -.
DR Ensembl; ENSRNOT00000085008; ENSRNOP00000075563; ENSRNOG00000069320.
DR GeneID; 24895; -.
DR KEGG; rno:24895; -.
DR CTD; 24895; -.
DR RGD; 2464; Cyp2a2.
DR GeneTree; ENSGT00940000154117; -.
DR InParanoid; P15149; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P15149; -.
DR TreeFam; TF352043; -.
DR PRO; PR:P15149; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008395; F:steroid hydroxylase activity; IDA:RGD.
DR GO; GO:0009804; P:coumarin metabolic process; IBA:GO_Central.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..492
FT /note="Cytochrome P450 2A2"
FT /id="PRO_0000051664"
FT BINDING 437
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 CONFLICT 4
FT /note="T -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 56345 MW; 9AB94CB68D34D81E CRC64;
MLDTGLLLVV ILASLSVMFL VSLWQQKIRE RLPPGPTPLP FIGNYLQLNM KDVYSSITQL
SERYGPVFTI HLGPRRIVVL YGYDAVKEAL VDQAEEFSGR GELPTFNILF KGYGFSLSNV
EQAKRIRRFT IATLRDFGVG KRDVQECILE EAGYLIKTLQ GTCGAPIDPS IYLSKTVSNV
INSIVFGNRF DYEDKEFLSL LEMIDEMNIF AASATGQLYD MFHSVMKYLP GPQQQIIKVT
QKLEDFMIEK VRQNHSTLDP NSPRNFIDSF LIRMQEEKYV NSEFHMNNLV MSSLGLLFAG
TGSVSSTLYH GFLLLMKHPD VEAKVHEEIE RVIGRNRQPQ YEDHMKMPYT QAVINEIQRF
SNLAPLGIPR RIIKNTTFRG FFLPKGTDVF PIIGSLMTEP KFFPNHKDFN PQHFLDDKGQ
LKKNAAFLPF SIGKRFCLGD SLAKMELFLL LTTILQNFRF KFPMNLEDIN EYPSPIGFTR
IIPNYTMSFM PI
