CP2J5_MOUSE
ID CP2J5_MOUSE Reviewed; 501 AA.
AC O54749;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cytochrome P450 2J5;
DE EC=1.14.14.1;
DE AltName: Full=Arachidonic acid epoxygenase;
DE AltName: Full=CYPIIJ5;
GN Name=Cyp2j5;
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].
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=9570962; DOI=10.1006/geno.1998.5235;
RA Ma J., Ramachandran S., Fiedorek F.T. Jr., Zeldin D.C.;
RT "Mapping of the CYP2J cytochrome P450 genes to human chromosome 1 and mouse
RT chromosome 4.";
RL Genomics 49:152-155(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and 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 -!- 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 -!- 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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U62294; AAB87635.1; -; mRNA.
DR EMBL; BC021624; AAH21624.1; -; mRNA.
DR CCDS; CCDS18371.1; -.
DR RefSeq; NP_034137.1; NM_010007.4.
DR AlphaFoldDB; O54749; -.
DR SMR; O54749; -.
DR BioGRID; 199026; 25.
DR STRING; 10090.ENSMUSP00000030299; -.
DR iPTMnet; O54749; -.
DR PhosphoSitePlus; O54749; -.
DR SwissPalm; O54749; -.
DR jPOST; O54749; -.
DR PaxDb; O54749; -.
DR PeptideAtlas; O54749; -.
DR PRIDE; O54749; -.
DR ProteomicsDB; 278006; -.
DR Ensembl; ENSMUST00000030299; ENSMUSP00000030299; ENSMUSG00000052520.
DR GeneID; 13109; -.
DR KEGG; mmu:13109; -.
DR UCSC; uc008ttl.1; mouse.
DR CTD; 13109; -.
DR MGI; MGI:1270149; Cyp2j5.
DR VEuPathDB; HostDB:ENSMUSG00000052520; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00950000182879; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; O54749; -.
DR OMA; HIRHHIA; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; O54749; -.
DR TreeFam; TF352043; -.
DR BioGRID-ORCS; 13109; 5 hits in 75 CRISPR screens.
DR PRO; PR:O54749; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O54749; protein.
DR Bgee; ENSMUSG00000052520; Expressed in right kidney and 27 other tissues.
DR ExpressionAtlas; O54749; baseline and differential.
DR Genevisible; O54749; 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; IBA:GO_Central.
DR GO; GO:0008405; F:arachidonic acid 11,12-epoxygenase activity; ISO:MGI.
DR GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; ISO:MGI.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; ISO: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:0016853; F:isomerase activity; ISO:MGI.
DR GO; GO:0071614; F:linoleic acid epoxygenase 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; IBA:GO_Central.
DR GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0019373; P:epoxygenase P450 pathway; ISO:MGI.
DR GO; GO:0006690; P:icosanoid metabolic process; ISO:MGI.
DR GO; GO:0043651; P:linoleic acid metabolic process; ISO:MGI.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:2000863; P:positive regulation of estrogen secretion; IMP:MGI.
DR GO; GO:0001990; P:regulation of systemic arterial blood pressure by hormone; IMP:MGI.
DR GO; GO:0097254; P:renal tubular secretion; IMP: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; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR008071; Cyt_P450_E_grp-I_CYP2J-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01688; EP450ICYP2J.
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..501
FT /note="Cytochrome P450 2J5"
FT /id="PRO_0000051771"
FT BINDING 447
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 501 AA; 57784 MW; C67F2E79DD64AF99 CRC64;
MIMFLSSLVT TFWEALHLKT LVLAVVTFLF LINILRSRHP KNYPPGPWRL PFVGNFFQID
TKQTHLVLQQ FVKKYGNVFS LELGQSPVVV VSGLPLIKEM FTHLDQNFVN RFMTPVRERI
TGKNGLVVSN GQTWKEQRRL ALMALRNFGL GKKSLEERIQ EETHHLVEAI REEGGQPFNP
HLKLINAVSN IICSVTFGER FDYEDCQFQE LLQLLDETMH LMGSSAGQLY NGFPCIMKYL
PGPHQKIFRN WGKLKLFVSH IVKKHEKDWN PDEPRDFIDA FLIEMQKDPD RTTSFNEENL
ISTTLDLFLG GTETTSSTLR WALLYMSSYP EIQENVQAEI DRVIGHKRQV SLSDRESMPY
TNAVIHEVQR MGNIVPLNSS REVTVDTKFN GFHLPKGTMI LTNLTALHRD PKEWATPEVF
NPEHFLENGQ FKKRESFLPF SMGKRACLGE QLAKSELFIF FSALMQKFTF KPPINEKLSL
KFRMGLILSP ASYRICAIPR V