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   02-SEP-2026, entry version 152.
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 + reduced [NADPH--hemoprotein reductase] +
CC         O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O +
CC         H(+); 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U39943; AAB48545.1; -; mRNA.
DR   EMBL; BC089766; AAH89766.1; -; mRNA.
DR   RefSeq; NP_786942.1; NM_175766.4.
DR   AlphaFoldDB; P51590; -.
DR   SMR; P51590; -.
DR   FunCoup; P51590; 95.
DR   STRING; 10116.ENSRNOP00000054968; -.
DR   PhosphoSitePlus; P51590; -.
DR   PaxDb; 10116-ENSRNOP00000054968; -.
DR   Ensembl; ENSRNOT00000058163.6; ENSRNOP00000054968.4; ENSRNOG00000077186.1.
DR   GeneID; 313375; -.
DR   KEGG; rno:313375; -.
DR   UCSC; RGD:631442; rat.
DR   AGR; RGD:631442; -.
DR   CTD; 313375; -.
DR   RGD; 631442; Cyp2j3.
DR   GeneTree; ENSGT00940000155417; -.
DR   InParanoid; P51590; -.
DR   OMA; RPMIPNL; -.
DR   OrthoDB; 83594at9989; -.
DR   PhylomeDB; P51590; -.
DR   BRENDA; 1.14.14.24; 5301.
DR   Reactome; R-RNO-211935; Fatty acids.
DR   Reactome; R-RNO-211981; Xenobiotics.
DR   Reactome; R-RNO-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
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:0008405; F:arachidonate 11,12-epoxygenase activity; IEA:Ensembl.
DR   GO; GO:0008404; F:arachidonate 14,15-epoxygenase activity; IEA:Ensembl.
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:0019373; P:epoxygenase P450 pathway; IEA:Ensembl.
DR   GO; GO:0043651; P:linoleic acid metabolic process; IEA:Ensembl.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20662; CYP2J; 1.
DR   FunFam; 1.10.630.10:FF:000004; cytochrome P450 2D15 isoform X1; 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; IPR008071; Cyt_P450_E_grp-I_CYP2J-like.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR050182; Cytochrome_P450_fam2.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   PANTHER; PTHR24300:SF108; CYTOCHROME P450 CYP2J9-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01688; EP450ICYP2J.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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
//