CP2F2_RAT
ID CP2F2_RAT Reviewed; 491 AA.
AC O35293;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cytochrome P450 2F2;
DE EC=1.14.14.-;
DE AltName: Full=CYPIIF2;
DE AltName: Full=Cytochrome P450-NAH-2;
DE AltName: Full=Naphthalene dehydrogenase;
DE AltName: Full=Naphthalene hydroxylase;
GN Name=Cyp2f2; Synonyms=Cyp2f4;
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], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=15509722; DOI=10.1124/jpet.104.075440;
RA Baldwin R.M., Shultz M.A., Buckpitt A.R.;
RT "Bioactivation of the pulmonary toxicants naphthalene and 1-
RT nitronaphthalene by rat CYP2F4.";
RL J. Pharmacol. Exp. Ther. 312:857-865(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
CC -!- FUNCTION: Involved in the regio- and stereoselective transformation of
CC naphthalene to trans-1R-hydroxy-2R-glutathionyl-1,2-dihydronaphthalene
CC in the presence of glutathione and glutathione S-transferases. It
CC specifically catalyzes the production of a very reactive and
CC potentially toxic intermediate, the 2R,2S arene oxide, that is
CC associated with necrosis of the unciliated bronchiolar epithelial cells
CC or Clara cells in lung. {ECO:0000269|PubMed:15509722}.
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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF017393; AAB70259.1; -; mRNA.
DR EMBL; BC070939; AAH70939.1; -; mRNA.
DR RefSeq; NP_062176.1; NM_019303.1.
DR RefSeq; XP_006228647.1; XM_006228585.2.
DR AlphaFoldDB; O35293; -.
DR SMR; O35293; -.
DR STRING; 10116.ENSRNOP00000058858; -.
DR PaxDb; O35293; -.
DR Ensembl; ENSRNOT00000068690; ENSRNOP00000058858; ENSRNOG00000032805.
DR GeneID; 54246; -.
DR KEGG; rno:54246; -.
DR UCSC; RGD:2476; rat.
DR CTD; 54246; -.
DR RGD; 2476; Cyp2f4.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000162522; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; O35293; -.
DR OMA; NTVHHDP; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; O35293; -.
DR Reactome; R-RNO-211935; Fatty acids.
DR Reactome; R-RNO-211981; Xenobiotics.
DR Reactome; R-RNO-211999; CYP2E1 reactions.
DR PRO; PR:O35293; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000032805; Expressed in esophagus and 14 other tissues.
DR Genevisible; O35293; RN.
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; ISO:RGD.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
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; IDA: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; ISO:RGD.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:1901170; P:naphthalene catabolic process; ISO:RGD.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:1901360; P:organic cyclic compound metabolic process; IDA:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0018979; P:trichloroethylene metabolic process; IDA: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; IPR020469; Cyt_P450_CYP2_fam.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01957; EP450ICYP2F.
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..491
FT /note="Cytochrome P450 2F2"
FT /id="PRO_0000051761"
FT BINDING 436
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 491 AA; 55946 MW; 31482F3588279567 CRC64;
MDGVSTAILL LLLAVISLSL TFTSWGKGQL PPGPKPLPIL GNLLQLRSQD LLTSLTKLSK
DYGSVFTVYL GPRRVIVLSG YQTVKEALVD KGEEFSGRGS YPIFFNFTKG NGIAFSDGER
WKILRRFSVQ ILRNFGMGKR SIEERILEEG SFLLDVLRKT EGKPFDPVFI LSRSVSNIIC
SVIFGSRFDY DDERLLTIIH FINDNFQIMS SPWGEMYNIF PSLLDWVPGP HRRVFRNFGG
MKDLIARSVR EHQDSLDPNS PRDFIDCFLT KMVQEKQDPL SHFNMDTLLM TTHNLLFGGT
ETVGTTLRHA FLILMKYPKV QARVQEEIDC VVGRSRMPTL EDRASMPYTD AVIHEVQRFA
DVIPMNLPHR VIRDTPFRGF LIPKGTDVIT LLNTVHYDSD QFKTPQEFNP EHFLDANQSF
KKSPAFMPFS AGRRLCLGEP LARMELFIYL TSILQNFTLH PLVEPEDIDL TPLSSGLGNL
PRPFQLCMRI R
