CP2F2_MOUSE
ID CP2F2_MOUSE Reviewed; 491 AA.
AC P33267;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 171.
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=Cyp2f-2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=1981702;
RA Nagata K., Martin B.M., Gillette J.R., Sasame H.A.;
RT "Isozymes of cytochrome P-450 that metabolize naphthalene in liver and lung
RT of untreated mice.";
RL Drug Metab. Dispos. 18:557-564(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=SWR/J; TISSUE=Lung;
RX PubMed=1742282; DOI=10.1021/bi00112a009;
RA Ritter J.K., Owens I.S., Negishi M., Nagata K., Sheen Y.Y., Gillette J.R.,
RA Sasame H.A.;
RT "Mouse pulmonary cytochrome P-450 naphthalene hydroxylase: cDNA cloning,
RT sequence, and expression in Saccharomyces cerevisiae.";
RL Biochemistry 30:11430-11437(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:1742282,
CC ECO:0000269|PubMed:1981702}.
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: Clara cells in lung and liver.
CC {ECO:0000269|PubMed:1742282, ECO:0000269|PubMed:1981702}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M77497; AAA37517.1; ALT_SEQ; mRNA.
DR EMBL; BC011089; AAH11089.1; -; mRNA.
DR EMBL; BC024742; AAH24742.1; -; mRNA.
DR CCDS; CCDS21010.1; -.
DR PIR; A39302; A39302.
DR RefSeq; NP_031843.2; NM_007817.2.
DR AlphaFoldDB; P33267; -.
DR SMR; P33267; -.
DR BioGRID; 199024; 24.
DR STRING; 10090.ENSMUSP00000003100; -.
DR iPTMnet; P33267; -.
DR PhosphoSitePlus; P33267; -.
DR SwissPalm; P33267; -.
DR jPOST; P33267; -.
DR MaxQB; P33267; -.
DR PaxDb; P33267; -.
DR PeptideAtlas; P33267; -.
DR PRIDE; P33267; -.
DR ProteomicsDB; 284151; -.
DR Antibodypedia; 30699; 119 antibodies from 26 providers.
DR Ensembl; ENSMUST00000003100; ENSMUSP00000003100; ENSMUSG00000052974.
DR GeneID; 13107; -.
DR KEGG; mmu:13107; -.
DR UCSC; uc009fuy.1; mouse.
DR CTD; 13107; -.
DR MGI; MGI:88608; Cyp2f2.
DR VEuPathDB; HostDB:ENSMUSG00000052974; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000162522; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; P33267; -.
DR OMA; NTVHHDP; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P33267; -.
DR TreeFam; TF352043; -.
DR Reactome; R-MMU-211935; Fatty acids.
DR Reactome; R-MMU-211981; Xenobiotics.
DR Reactome; R-MMU-211999; CYP2E1 reactions.
DR BioGRID-ORCS; 13107; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cyp2f2; mouse.
DR PRO; PR:P33267; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P33267; protein.
DR Bgee; ENSMUSG00000052974; Expressed in right lung and 125 other tissues.
DR ExpressionAtlas; P33267; baseline and differential.
DR Genevisible; P33267; MM.
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:MGI.
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; ISO:MGI.
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:MGI.
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; IMP:MGI.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:1901360; P:organic cyclic compound metabolic process; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; IMP:MGI.
DR GO; GO:0018979; P:trichloroethylene metabolic process; ISO:MGI.
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 1: Evidence at protein 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_0000051760"
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; 55949 MW; F56AEB956E7EBD25 CRC64;
MDGVSTAILL LLLAVISLSL TFSSRGKGQL PPGPKPLPIL GNLLQLRSQD LLTSLTKLSK
EYGSVFTVYL GSRPVIVLSG YQTVKEALVD KGEEFSGRGA YPVFFNFTRG NGIAFSDGER
WKILRRFSVQ ILRNFGMGKR SIEERILEEG SFLLEVLRKM EGKPFDPVFI LSRSVSNIIC
SVVFGSRFDY DDERLLTIIH FINDNFKIMS SPWGEMYNIF PSVLDWIPGP HKRLFRNFGG
MKDLIARSVR EHQDSLDPNS PRDFIDCFLT KMAQEKQDPL SHFNMDTLLM TTHNLLFGGT
ETVGTTLRHA FLILMKYPKV QARVQEEIDR VVGRSRMPTL EDRTSMPYTD AVIHEVQRFA
DVIPMNLPHR VTRDTPFRGF LIPKGTDVIT LLNTVHYDSD QFKTPQEFNP EHFLDDNHSF
KKSPAFMPFS AGRRLCLGEP LARMELFIYF TSILQNFTLQ PLVDPEDIDL TPLSSGLGNL
PRPFQLCMHI R
