CY250_MOUSE
ID CY250_MOUSE Reviewed; 490 AA.
AC Q91X77; E9QPJ0; Q6XVG3; Q80X43;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cytochrome P450 2C50;
DE EC=1.14.14.1 {ECO:0000269|PubMed:15102943};
DE AltName: Full=CYPIIC50;
GN Name=Cyp2c50 {ECO:0000312|EMBL:AAH11222.1};
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 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO52736.1};
RC TISSUE=Heart {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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH51050.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH51050.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAH51050.1};
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 PROTEIN SEQUENCE OF 100-116, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
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 to several midchain and omega-
CC terminal hydroxyeicosatetraenoic acids (HETE).
CC {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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15102943};
CC IsoId=Q91X77-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q91X77-2; Sequence=VSP_052374;
CC -!- TISSUE SPECIFICITY: Expressed in heart and liver.
CC {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; AY206873; AAO52736.1; -; mRNA.
DR EMBL; AC148014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011222; AAH11222.1; -; mRNA.
DR EMBL; BC051050; AAH51050.1; -; mRNA.
DR CCDS; CCDS29801.1; -. [Q91X77-1]
DR CCDS; CCDS50433.1; -. [Q91X77-2]
DR RefSeq; NP_001161347.1; NM_001167875.1. [Q91X77-2]
DR RefSeq; NP_598905.2; NM_134144.2. [Q91X77-1]
DR AlphaFoldDB; Q91X77; -.
DR SMR; Q91X77; -.
DR STRING; 10090.ENSMUSP00000079065; -.
DR iPTMnet; Q91X77; -.
DR PhosphoSitePlus; Q91X77; -.
DR SwissPalm; Q91X77; -.
DR jPOST; Q91X77; -.
DR MaxQB; Q91X77; -.
DR PaxDb; Q91X77; -.
DR PeptideAtlas; Q91X77; -.
DR PRIDE; Q91X77; -.
DR ProteomicsDB; 279248; -. [Q91X77-1]
DR ProteomicsDB; 279249; -. [Q91X77-2]
DR DNASU; 107141; -.
DR Ensembl; ENSMUST00000068094; ENSMUSP00000068039; ENSMUSG00000054827. [Q91X77-2]
DR Ensembl; ENSMUST00000080171; ENSMUSP00000079065; ENSMUSG00000054827. [Q91X77-1]
DR GeneID; 107141; -.
DR KEGG; mmu:107141; -.
DR UCSC; uc008hki.2; mouse. [Q91X77-1]
DR UCSC; uc012blo.1; mouse. [Q91X77-2]
DR CTD; 107141; -.
DR MGI; MGI:2147497; Cyp2c50.
DR VEuPathDB; HostDB:ENSMUSG00000054827; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000155736; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; Q91X77; -.
DR OMA; PTCENHS; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q91X77; -.
DR TreeFam; TF352043; -.
DR BioGRID-ORCS; 107141; 0 hits in 41 CRISPR screens.
DR PRO; PR:Q91X77; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91X77; protein.
DR Bgee; ENSMUSG00000054827; Expressed in left lobe of liver and 13 other tissues.
DR Genevisible; Q91X77; 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; Alternative splicing; Direct protein sequencing;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..490
FT /note="Cytochrome P450 2C50"
FT /id="PRO_0000282957"
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 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
FT VAR_SEQ 215..273
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052374"
FT CONFLICT 71
FT /note="R -> N (in Ref. 3; AAH51050/AAH11222)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="N -> D (in Ref. 3; AAH11222)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="R -> S (in Ref. 3; AAH51050/AAH11222)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="H -> R (in Ref. 3; AAH51050/AAH11222)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="L -> Q (in Ref. 1; AAO52736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 55765 MW; 6C66FA7482AB3F78 CRC64;
MDPILVLVFT LSCLFLLSLW RQSSERGKLP PGPTPLPIIG NILQINVKDI CQSFTNLSKV
YGPVYTLYLG RKPTVVLHGY EAVKEALVDH GEEFAGRGRL PVFDKATNGM GIIFSKGNVW
KNTRRFSLTT LRNLGMGKRS IEDRVQEEAR CLVEELRKTN GSPCDPTFIL GCAPCNVICS
IIFQDRFDYK DRDFLNLMEK LNEITKIMST PWLQVCNTFP VLLDYCPGSH NKVFKNYACI
KNFLLEKIKE HEESLDVTIP RDFIDYFLIN GGQENGNYPL KNRLEHLAIT VTDLFSAGTE
TTSTTLRYAL LLLLKYPHVT AKVQEEIEHV IGKHRRPCMQ DRSHMPYTDA MIHEVQRFID
LVPNSLPHEV TCDIKFRNYF IPKGTNVITS LSSVLRDSKE FPNPEKFDPG HFLDENGKFK
KSDYFMPFST GKRICAGEGL ARMELFLFLT SILQNFNLKP LVHPKDIDVT PMLIGLASVP
PAFQLCFIPS
