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   27-MAR-2024, entry version 143.
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; 10090-ENSMUSP00000048284; -.
DR   PeptideAtlas; Q6XVG2; -.
DR   ProteomicsDB; 285275; -.
DR   DNASU; 404195; -.
DR   Ensembl; ENSMUST00000048959.5; ENSMUSP00000048284.4; ENSMUSG00000067225.3.
DR   GeneID; 404195; -.
DR   KEGG; mmu:404195; -.
DR   UCSC; uc012bln.1; mouse.
DR   AGR; MGI:3642960; -.
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; HIHESEF; -.
DR   OrthoDB; 2900138at2759; -.
DR   PhylomeDB; Q6XVG2; -.
DR   TreeFam; TF352043; -.
DR   BioGRID-ORCS; 404195; 3 hits in 45 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 cell types or tissues.
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; IDA:MGI.
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:0071614; F:linoleic acid epoxygenase activity; IDA: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: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:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20665; CYP2C-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24300:SF374; CYTOCHROME P450 2C18; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   Genevisible; Q6XVG2; MM.
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
//