CP2J3_RAT
ID CP2J3_RAT Reviewed; 502 AA.
AC P51590; Q5EBD7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cytochrome P450 2J3;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIJ3;
GN Name=Cyp2j3; Synonyms=Cyp2j9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Fischer 344;
RX PubMed=9139707; DOI=10.1074/jbc.272.19.12551;
RA Wu S., Chen W., Murphy E., Gabel S., Tomer K.B., Foley J., Steenbergen C.,
RA Falck J.R., Moomaw C.R., Zeldin D.C.;
RT "Molecular cloning, expression, and functional significance of a cytochrome
RT P450 highly expressed in rat heart myocytes.";
RL J. Biol. Chem. 272:12551-12559(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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: This enzyme metabolizes arachidonic acid predominantly via a
CC NADPH-dependent olefin epoxidation mainly to 14,15-, 11,12-, and 8,9-
CC epoxyeicosatrienoic acids (EET). It also acts as an omega-1-hydroxylase
CC by metabolizing arachidonic acid to 19-hydroxyeicosatetraenoic acid
CC (19-OH-AA).
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 -!- TISSUE SPECIFICITY: Abundantly expressed in heart and liver.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U39943; AAB48545.1; -; mRNA.
DR EMBL; BC089766; AAH89766.1; -; mRNA.
DR RefSeq; NP_786942.1; NM_175766.3.
DR AlphaFoldDB; P51590; -.
DR SMR; P51590; -.
DR PhosphoSitePlus; P51590; -.
DR PRIDE; P51590; -.
DR Ensembl; ENSRNOT00000058163; ENSRNOP00000054968; ENSRNOG00000031004.
DR GeneID; 313375; -.
DR KEGG; rno:313375; -.
DR UCSC; RGD:631442; rat.
DR CTD; 313375; -.
DR RGD; 631442; Cyp2j3.
DR GeneTree; ENSGT00940000155417; -.
DR InParanoid; P51590; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P51590; -.
DR BRENDA; 1.14.14.24; 5301.
DR PRO; PR:P51590; -.
DR Proteomes; UP000002494; Chromosome 5.
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; IEA:Ensembl.
DR GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0071614; F:linoleic acid epoxygenase activity; IEA:Ensembl.
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:0019373; P:epoxygenase P450 pathway; IEA:Ensembl.
DR GO; GO:0043651; P:linoleic acid metabolic process; IEA:Ensembl.
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; 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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..502
FT /note="Cytochrome P450 2J3"
FT /id="PRO_0000051770"
FT BINDING 448
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 502 AA; 57969 MW; CCC0AE67977FFF31 CRC64;
MLVTAGSLLG AIWTVLHLRI LLLAAVTFLF LADFLKHRRP KNYPPGPWRL PLVGCLFHLD
PKQPHLSLQQ FVKKYGNVLS LDFANIPSVV VTGMPLIKEI FTQMEHNFLN RPVTLLRKHL
FNKNGLIFSS GQTWKEQRRF ALMTLRNFGL GKKSLEQRIQ EEAYHLVEAI KDEGGLPFDP
HFNINKAVSN IICSVTFGER FEYHDSQFQE MLRLLDEAMC LESSMMCQLY NIFPRILQYL
PGSHQTLFSN WRKLKLFISD IIKNHRRDWD PDEPRDFIDA FLKEMAKYPD KTTTSFNEEN
LICSTLDLFF AGTETTSTTL RWALLCMALY PEVQEKMQAE IDRVIGQGRQ PNLADRDSMP
YTNAVIHEVQ RIGNIIPFNV PREVAVDTYL AGFNLPKGTM ILTNLTALHR DPKEWATPDT
FNPEHFLENG QFKKRESFLP FSMGKRACLG EQLARSELFI FITSLIQKFT FKPPVNEKLS
LQFRMSVTIS PVSHRLCAIP RL
