CP2A3_RAT
ID CP2A3_RAT Reviewed; 494 AA.
AC P20812;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cytochrome P450 2A3;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIA3;
DE AltName: Full=Coumarin 7-hydroxylase;
GN Name=Cyp2a3; Synonyms=Cyp2a-3, Cyp2a3a;
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 [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=2388852; DOI=10.1093/nar/18.15.4623;
RA Ueno T., Gonzalez F.;
RT "Complete sequence of the rat CYP2A3 gene specifically transcribed in
RT lung.";
RL Nucleic Acids Res. 18:4623-4624(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-494.
RC TISSUE=Lung;
RX PubMed=2751996; DOI=10.1021/bi00435a026;
RA Kimura S., Kozak C.A., Gonzalez F.J.;
RT "Identification of a novel P450 expressed in rat lung: cDNA cloning and
RT sequence, chromosome mapping, and induction by 3-methylcholanthrene.";
RL Biochemistry 28:3798-3803(1989).
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: Lung.
CC -!- INDUCTION: By 3-methylcholanthrene (3MC).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M33190; AAA41022.1; -; Genomic_DNA.
DR EMBL; J02852; AAA88511.1; -; mRNA.
DR PIR; S15056; A32030.
DR RefSeq; NP_036674.1; NM_012542.2.
DR AlphaFoldDB; P20812; -.
DR SMR; P20812; -.
DR STRING; 10116.ENSRNOP00000028231; -.
DR PhosphoSitePlus; P20812; -.
DR GeneID; 24299; -.
DR KEGG; rno:24299; -.
DR UCSC; RGD:2465; rat.
DR CTD; 24299; -.
DR RGD; 2465; Cyp2a3.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; P20812; -.
DR OrthoDB; 702827at2759; -.
DR Reactome; R-RNO-211935; Fatty acids.
DR Reactome; R-RNO-211981; Xenobiotics.
DR Reactome; R-RNO-211999; CYP2E1 reactions.
DR PRO; PR:P20812; -.
DR Proteomes; UP000002494; Unplaced.
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:0004497; F:monooxygenase activity; TAS:RGD.
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:0019825; F:oxygen binding; TAS:RGD.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISO: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:0042168; P:heme metabolic process; ISO:RGD.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0035634; P:response to stilbenoid; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW Microsome; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..494
FT /note="Cytochrome P450 2A3"
FT /id="PRO_0000051665"
FT BINDING 439
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 MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00176"
FT MOD_RES 379
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
FT CONFLICT 109
FT /note="W -> G (in Ref. 2; AAA88511)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="I -> N (in Ref. 2; AAA88511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56510 MW; F71855CBE602672F CRC64;
MLASGLLLVA SVAFLSVLVL MSVWKQRKLS GKLPPGPTPL PFIGNYLQLN TEKMYSSLMK
ISQRYGPVFT IHLGPRRVVV LCGQEAVKEA LVDQAEEFSG RGEQATFDWL FKGYGVAFSS
GERAKQLRRF SIATLRDFGV GKRGIEERIQ EEAGFLIESF RKTNGALIDP TFYLSRTVSN
VISSIVFGDR FDYEDKEFLS LLRMMLGSFQ FTATSTGQLY EMFSSVMKHL PGPQQQAFKE
LQGLEDFITK KVEQNQRTLD PNSPRDFIDS FLIRMLEEKK NPNTEFYMKN LVLTTLNLFF
AGTETVSTTL RYGFLLLMKH PDIEAKVHEE IDRVIGRNRQ AKYEDRMKMP YTEAVIHEIQ
RFADMIPMGL ARRVTKDTKF REFLLPKGTE VFPMLGSVLK DPKFFSNPND FNPKHFLDDK
GQFKKSDAFV PFSIGKRYCF GEGLARMELF LFLTNIMQNF CFKSPQAPQD IDVSPRLVGF
ATIPPNYTMS FLSR
