CP254_MOUSE
ID CP254_MOUSE Reviewed; 490 AA.
AC Q6XVG2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cytochrome P450 2C54;
DE EC=1.14.14.1 {ECO:0000269|PubMed:15102943};
DE AltName: Full=CYPIIC54;
GN Name=Cyp2c54 {ECO:0000312|EMBL:AAO52737.1};
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, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO52737.1};
RC TISSUE=Liver {ECO:0000269|PubMed:15102943};
RX PubMed=15102943; DOI=10.1124/mol.65.5.1148;
RA Wang H., Zhao Y., Bradbury J.A., Graves J.P., Foley J., Blaisdell J.A.,
RA Goldstein J.A., Zeldin D.C.;
RT "Cloning, expression, and characterization of three new mouse cytochrome
RT p450 enzymes and partial characterization of their fatty acid oxidation
RT activities.";
RL Mol. Pharmacol. 65:1148-1158(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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: Metabolizes arachidonic acid mainly to 12-
CC hydroxyeicosatetraenoic acid (HETE). {ECO:0000269|PubMed:15102943}.
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 Evidence={ECO:0000269|PubMed:15102943};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15102943}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15102943}. Microsome membrane
CC {ECO:0000269|PubMed:15102943}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15102943}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. {ECO:0000269|PubMed:15102943}.
CC -!- INDUCTION: P450 can be induced to high levels in liver and other
CC tissues by various foreign compounds, including drugs, pesticides, and
CC carcinogens. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000255}.
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DR EMBL; AY206874; AAO52737.1; -; mRNA.
DR CCDS; CCDS29800.1; -.
DR RefSeq; NP_996260.1; NM_206537.2.
DR AlphaFoldDB; Q6XVG2; -.
DR SMR; Q6XVG2; -.
DR BioGRID; 240101; 36.
DR STRING; 10090.ENSMUSP00000048284; -.
DR iPTMnet; Q6XVG2; -.
DR PhosphoSitePlus; Q6XVG2; -.
DR SwissPalm; Q6XVG2; -.
DR jPOST; Q6XVG2; -.
DR MaxQB; Q6XVG2; -.
DR PaxDb; Q6XVG2; -.
DR PeptideAtlas; Q6XVG2; -.
DR PRIDE; Q6XVG2; -.
DR ProteomicsDB; 285275; -.
DR DNASU; 404195; -.
DR Ensembl; ENSMUST00000048959; ENSMUSP00000048284; ENSMUSG00000067225.
DR GeneID; 404195; -.
DR KEGG; mmu:404195; -.
DR UCSC; uc012bln.1; mouse.
DR CTD; 404195; -.
DR MGI; MGI:3642960; Cyp2c54.
DR VEuPathDB; HostDB:ENSMUSG00000067225; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000155736; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; Q6XVG2; -.
DR OMA; WKIKGGD; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q6XVG2; -.
DR TreeFam; TF352043; -.
DR BioGRID-ORCS; 404195; 3 hits in 40 CRISPR screens.
DR PRO; PR:Q6XVG2; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6XVG2; protein.
DR Bgee; ENSMUSG00000067225; Expressed in left lobe of liver and 26 other tissues.
DR Genevisible; Q6XVG2; 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:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; IDA:MGI.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034875; F:caffeine oxidase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0071614; F:linoleic acid epoxygenase activity; IDA:MGI.
DR GO; GO:0120319; F:long-chain fatty acid omega-1 hydroxylase activity; ISO:MGI.
DR GO; GO:0004497; F:monooxygenase activity; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase 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; IBA:GO_Central.
DR GO; GO:0008395; F:steroid hydroxylase activity; ISO:MGI.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:MGI.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR GO; GO:0043651; P:linoleic acid metabolic process; IDA:MGI.
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; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Acetylation; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW Microsome; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..490
FT /note="Cytochrome P450 2C54"
FT /id="PRO_0000282958"
FT BINDING 435
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|UniProtKB:P10632"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00176"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
SQ SEQUENCE 490 AA; 55858 MW; C226BBBB734DE29D CRC64;
MDPILVLVLT LSCLFLLSLW RQSYERGKLP PGPTPLPIIG NILQIDVKDI CQSFTNLSRV
YGPVYTLYLG RKPTVVLHGY EAVKEALVDH GDVFAGRGRL PVFDKATNGM GIGFSNGSVW
KNTRHFSLMT LRNLGMGKRS IEDRVQEEAR CLVEELRKTN GSPCDPTFIL GCAPCNVICS
IIFQDRFDYK DRDFLNLLEK LDEISKILST PWLQVCNTFP ALLDYCPGSH NQFFKNYAYI
KNFLLEKIRE HKESLDVTIP RDFIDYFLIK GAQEDDNHPL KNNFEHLAIT VTDLFIGGTE
SMSTTLRYAL LLLLKYPHVT AKVQEEIEHV IGKHRRPCMQ DRSHMPYTNA MIHEVQRFID
LVPNNLPHEV TCDIKFRNYF IPKGTTVITS LSSVLRDSKE FPNPEKFDPG HFLDENGKFK
KSDYFMPFST GKRICAGEGL ARMELFLFLT SILQNFNLKP LVHPKDIDIT PMLIGLGSVP
PAFQLCFIPS
