CP238_MOUSE
ID CP238_MOUSE Reviewed; 490 AA.
AC P56655; B2RWV4; F8VPK7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cytochrome P450 2C38;
DE EC=1.14.14.1 {ECO:0000269|PubMed:9721182};
DE AltName: Full=CYPIIC38;
DE Flags: Precursor;
GN Name=Cyp2c38 {ECO:0000303|PubMed:9721182, ECO:0000312|MGI:MGI:1306819};
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, TISSUE
RP SPECIFICITY, AND PATHWAY.
RC STRAIN=CD-1;
RX PubMed=9721182; DOI=10.1006/abbi.1998.0806;
RA Luo G., Zeldin D.C., Blaisdell J.A., Hodgson E., Goldstein J.A.;
RT "Cloning and expression of murine CYP2Cs and their ability to metabolize
RT arachidonic acid.";
RL Arch. Biochem. Biophys. 357:45-57(1998).
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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: A cytochrome P450 monooxygenase that primarily catalyzes the
CC epoxidation of 11,12 double bond of (5Z,8Z,11Z,14Z)-eicosatetraenoic
CC acid (arachidonate) forming 11,12-epoxyeicosatrienoic acid (11,12-EET)
CC regioisomer. Mechanistically, uses molecular oxygen inserting one
CC oxygen atom into a substrate, and reducing the second into a water
CC molecule, with two electrons provided by NADPH via cytochrome P450
CC reductase (CPR; NADPH--hemoprotein reductase).
CC {ECO:0000269|PubMed:9721182}.
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:9721182};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC Evidence={ECO:0000305|PubMed:9721182};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:51480, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76625; Evidence={ECO:0000269|PubMed:9721182};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51481;
CC Evidence={ECO:0000305|PubMed:9721182};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000305|PubMed:9721182}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein. Microsome membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Liver, brain, kidney, and intestine, with trace
CC amounts in lung and heart. {ECO:0000269|PubMed:9721182}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF047725; AAD13720.1; -; mRNA.
DR EMBL; AC139233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150721; AAI50722.1; -; mRNA.
DR CCDS; CCDS29794.1; -.
DR RefSeq; NP_034132.2; NM_010002.3.
DR AlphaFoldDB; P56655; -.
DR SMR; P56655; -.
DR STRING; 10090.ENSMUSP00000044722; -.
DR SwissLipids; SLP:000001669; -.
DR iPTMnet; P56655; -.
DR PhosphoSitePlus; P56655; -.
DR jPOST; P56655; -.
DR MaxQB; P56655; -.
DR PaxDb; P56655; -.
DR PeptideAtlas; P56655; -.
DR PRIDE; P56655; -.
DR DNASU; 13097; -.
DR Ensembl; ENSMUST00000035488; ENSMUSP00000044722; ENSMUSG00000032808.
DR GeneID; 13097; -.
DR KEGG; mmu:13097; -.
DR UCSC; uc008hka.1; mouse.
DR CTD; 13097; -.
DR MGI; MGI:1306819; Cyp2c38.
DR VEuPathDB; HostDB:ENSMUSG00000032808; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000155736; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; P56655; -.
DR OMA; LLWFMNA; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P56655; -.
DR TreeFam; TF352043; -.
DR UniPathway; UPA00383; -.
DR BioGRID-ORCS; 13097; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cyp2c38; mouse.
DR PRO; PR:P56655; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P56655; protein.
DR Bgee; ENSMUSG00000032808; Expressed in liver and 8 other tissues.
DR Genevisible; P56655; 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:0008405; F:arachidonic acid 11,12-epoxygenase activity; IDA:UniProtKB.
DR GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; IDA:UniProtKB.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; ISO: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: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:UniProtKB.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
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 Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..490
FT /note="Cytochrome P450 2C38"
FT /evidence="ECO:0000255"
FT /id="PRO_0000051721"
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"
FT CONFLICT 60
FT /note="T -> A (in Ref. 1; AAD13720 and 3; AAI50722)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="E -> G (in Ref. 1; AAD13720 and 3; AAI50722)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="R -> H (in Ref. 1; AAD13720 and 3; AAI50722)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="D -> H (in Ref. 1; AAD13720 and 3; AAI50722)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="E -> A (in Ref. 1; AAD13720 and 3; AAI50722)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="V -> F (in Ref. 1; AAD13720 and 3; AAI50722)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="R -> H (in Ref. 1; AAD13720 and 3; AAI50722)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="I -> M (in Ref. 1; AAD13720 and 3; AAI50722)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="T -> A (in Ref. 1; AAD13720 and 3; AAI50722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 56229 MW; 876444B4A6C1343A CRC64;
MDLVTFLVLT LSSLILLSLW RQRSRRGRLP PGPTPFPIIG NFLQIDVKNF NQSLTNFSKT
YGPVFTLYLG SRPIVVLHGY EAVKEALIDH GEEFSGRENI PMSEKINNGL GITFSNGNSW
KETRRFTLMT LRNLGMGKRN IEDRVREEAQ CLVEELRKTK GSPCDPTFIL SCAPCNVICS
IIFQDRFDYK DKDFLMLMKK LNENVKILSS PWLQVCNNFP LLIDYCPGSH HKVLKNFKYI
RSYLLEKVKE HQESLDVTNP RDFIDYFLIK QKQANHIEQA EYSLENLVCT INNLFAAGTE
TTSTTLRYAL LLLMKYPDVT AKVQEEIDHV VGRHRSPCMQ DRSRMPYTDA MIHEVQRFIN
LVPNNLPHAV TCDIKFRNYI IPKGTTVVTS LTSVLHDSKE FPNPEMFDPG HFLDANGNFK
KSDYFMTFSA GKRVCAGEGL ARMELFLILT TILQNFKLKS LVHPKDIDMI PFVNGLITLP
PHYQLCFIPL
