CP4F3_RAT
ID CP4F3_RAT Reviewed; 524 AA.
AC Q3MID2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome P450 4F3 {ECO:0000250|UniProtKB:Q08477};
DE AltName: Full=CYPIVF3;
DE AltName: Full=Leukotriene-B(4) omega-1/omega-2 hydroxylase {ECO:0000250|UniProtKB:Q99N16};
GN Name=Cyp4f3 {ECO:0000250|UniProtKB:Q08477};
GN Synonyms=Cyp4f18 {ECO:0000312|RGD:1305261};
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 [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 involved in the metabolism of
CC the pro-inflammatory lipid mediator leukotriene B4 (LTB4). Hydroxylates
CC at the omega-1 and omega-2 positions LTB4. This oxidation step leads to
CC LTB4 inactivation, which is postulated to be a crucial part of the
CC resolution of inflammation. Mechanistically, uses molecular oxygen
CC inserting one oxygen atom into a substrate, and reducing the second
CC into a water molecule, with two electrons provided by NADPH via
CC cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
CC {ECO:0000250|UniProtKB:Q99N16}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] =
CC 18-hydroxy-leukotriene B4 + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53440, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57461, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:137391; Evidence={ECO:0000250|UniProtKB:Q99N16};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53441;
CC Evidence={ECO:0000250|UniProtKB:Q99N16};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] =
CC 19-hydroxy-leukotriene B4 + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53436, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57461, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:137390; Evidence={ECO:0000250|UniProtKB:Q99N16};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53437;
CC Evidence={ECO:0000250|UniProtKB:Q99N16};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P51869};
CC -!- PATHWAY: Lipid metabolism; leukotriene B4 degradation.
CC {ECO:0000250|UniProtKB:Q99N16}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q99N16}; Single-pass membrane protein
CC {ECO:0000305}. Microsome membrane {ECO:0000250|UniProtKB:Q99N16};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000255}.
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DR EMBL; BC101918; AAI01919.1; -; mRNA.
DR RefSeq; NP_001028858.1; NM_001033686.1.
DR AlphaFoldDB; Q3MID2; -.
DR SMR; Q3MID2; -.
DR STRING; 10116.ENSRNOP00000021609; -.
DR iPTMnet; Q3MID2; -.
DR PhosphoSitePlus; Q3MID2; -.
DR PaxDb; Q3MID2; -.
DR PRIDE; Q3MID2; -.
DR GeneID; 290623; -.
DR KEGG; rno:290623; -.
DR UCSC; RGD:1305261; rat.
DR CTD; 72054; -.
DR RGD; 1305261; Cyp4f18.
DR eggNOG; KOG0157; Eukaryota.
DR InParanoid; Q3MID2; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q3MID2; -.
DR Reactome; R-RNO-211935; Fatty acids.
DR Reactome; R-RNO-211958; Miscellaneous substrates.
DR Reactome; R-RNO-211979; Eicosanoids.
DR Reactome; R-RNO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-RNO-2142816; Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
DR SABIO-RK; Q3MID2; -.
DR UniPathway; UPA00883; -.
DR PRO; PR:Q3MID2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; IBA:GO_Central.
DR GO; GO:0102207; F:docosanoate omega-hydroxylase activity; ISO:RGD.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050051; F:leukotriene-B4 20-monooxygenase activity; IBA:GO_Central.
DR GO; GO:0120319; F:long-chain fatty acid omega-1 hydroxylase activity; ISS:UniProtKB.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; ISO:RGD.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IBA:GO_Central.
DR GO; GO:0010430; P:fatty acid omega-oxidation; ISO:RGD.
DR GO; GO:0036101; P:leukotriene B4 catabolic process; IBA:GO_Central.
DR GO; GO:0036102; P:leukotriene B4 metabolic process; ISS:UniProtKB.
DR GO; GO:0042361; P:menaquinone catabolic process; IBA:GO_Central.
DR GO; GO:0097267; P:omega-hydroxylase P450 pathway; ISO:RGD.
DR GO; GO:0042376; P:phylloquinone catabolic 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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..524
FT /note="Cytochrome P450 4F3"
FT /id="PRO_0000238925"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 468
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:P33274"
SQ SEQUENCE 524 AA; 59906 MW; 8DC9033E01F1A1E8 CRC64;
MPLLSLSWLG LGHTAASPWL LLLLVGASCL LAYILPQVYA VFENSRRLRR FPQPPPRNWL
FGHLGLIQSS EEGLLYIQSL SRTFRDVCCW WVGPWHPVIR IFHPAFIKPV ILAPASVAPK
DRVFYRFLRP WLGDGLLLST GDKWSRHRRM LTPAFHFNIL KPYVKIFNDS TNIMHAKWQR
LASQGSARLD MFEHISLMTL DSLQKCVFSF DSNCQEKPSE YITAILELSA LVARRHQSLL
LHVDLFYHLT RDGMRFRKAC RLVHDFTDAV IRERRCTLPD QGGDDALKAK AKAKTLDFID
VLLLSKDEHG EALSDEDIRA EADTFMFGGH DTTASGLSWI LYNLAKHPEY QERCRQEVRE
LLRDREPEEI EWDDLAQLPF LTMCIKESLR LHPPATAISR CCTQDIMLPD GRVIPKGVIC
RISIFGTHHN PAVWPDPEVY NPFRFDADNG KGRSPLAFIP FSAGPRNCIG QTFAMSEMKV
ALALTLLRFR VLPDDKEPRR KPELILRAEG GLWLRVEPLS AGAH
