CP4FE_MOUSE
ID CP4FE_MOUSE Reviewed; 524 AA.
AC Q9EP75; Q52L93;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Leukotriene-B4 omega-hydroxylase 3;
DE EC=1.14.14.94;
DE AltName: Full=Cyp4f-14;
DE AltName: Full=Cytochrome P450 4F14;
DE AltName: Full=Cytochrome P450-LTB-omega;
DE AltName: Full=Leukotriene-B4 20-monooxygenase 3;
GN Name=Cyp4f14;
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/6J; TISSUE=Liver;
RA Kikuta Y., Kasyu H., Kusunose E., Kusunose M.;
RT "Mouse liver leukotriene B4 omega-hydroxylase.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv; TISSUE=Brain;
RA Antonovic L., Kawashima H., Strobel H.;
RT "Protein expression and catalytic activity assessment of mouse 4F clones.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC Catalyzes the omega-hydroxylation of LTB4 (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] =
CC 20-hydroxy-leukotriene B4 + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:22176, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57460, ChEBI:CHEBI:57461, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.94; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P51869};
CC -!- PATHWAY: Lipid metabolism; leukotriene B4 degradation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Microsome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AB037541; BAB12564.1; -; mRNA.
DR EMBL; AB037540; BAB12563.1; -; mRNA.
DR EMBL; AF233644; AAK15010.1; -; mRNA.
DR EMBL; AK005007; BAB23740.1; -; mRNA.
DR EMBL; AK018676; BAB31338.1; -; mRNA.
DR EMBL; BC011228; AAH11228.1; -; mRNA.
DR EMBL; BC094016; AAH94016.1; -; mRNA.
DR CCDS; CCDS28621.1; -.
DR RefSeq; NP_001191262.1; NM_001204333.1.
DR RefSeq; NP_001191263.1; NM_001204334.1.
DR RefSeq; NP_001191264.1; NM_001204335.1.
DR RefSeq; NP_001191265.1; NM_001204336.1.
DR RefSeq; NP_071879.1; NM_022434.2.
DR RefSeq; XP_006524845.1; XM_006524782.3.
DR AlphaFoldDB; Q9EP75; -.
DR SMR; Q9EP75; -.
DR STRING; 10090.ENSMUSP00000050478; -.
DR iPTMnet; Q9EP75; -.
DR PhosphoSitePlus; Q9EP75; -.
DR SwissPalm; Q9EP75; -.
DR jPOST; Q9EP75; -.
DR MaxQB; Q9EP75; -.
DR PaxDb; Q9EP75; -.
DR PeptideAtlas; Q9EP75; -.
DR PRIDE; Q9EP75; -.
DR ProteomicsDB; 284155; -.
DR DNASU; 64385; -.
DR Ensembl; ENSMUST00000054174; ENSMUSP00000050478; ENSMUSG00000024292.
DR Ensembl; ENSMUST00000179434; ENSMUSP00000136139; ENSMUSG00000024292.
DR Ensembl; ENSMUST00000234759; ENSMUSP00000157036; ENSMUSG00000024292.
DR Ensembl; ENSMUST00000235058; ENSMUSP00000157006; ENSMUSG00000024292.
DR GeneID; 64385; -.
DR KEGG; mmu:64385; -.
DR UCSC; uc008bxq.2; mouse.
DR CTD; 64385; -.
DR MGI; MGI:1927669; Cyp4f14.
DR VEuPathDB; HostDB:ENSMUSG00000024292; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000154646; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; Q9EP75; -.
DR OMA; IVHECNR; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q9EP75; -.
DR TreeFam; TF105088; -.
DR BRENDA; 1.14.14.94; 3474.
DR Reactome; R-MMU-211935; Fatty acids.
DR Reactome; R-MMU-211979; Eicosanoids.
DR UniPathway; UPA00883; -.
DR BioGRID-ORCS; 64385; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Cyp4f14; mouse.
DR PRO; PR:Q9EP75; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9EP75; protein.
DR Bgee; ENSMUSG00000024292; Expressed in small intestine Peyer's patch and 47 other tissues.
DR ExpressionAtlas; Q9EP75; baseline and differential.
DR Genevisible; Q9EP75; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:0018685; F:alkane 1-monooxygenase activity; ISO:MGI.
DR GO; GO:0052871; F:alpha-tocopherol omega-hydroxylase activity; ISO:MGI.
DR GO; GO:0050544; F:arachidonic acid binding; ISO:MGI.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; ISO:MGI.
DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; ISO:MGI.
DR GO; GO:0052869; F:arachidonic acid omega-hydroxylase activity; ISO:MGI.
DR GO; GO:0005504; F:fatty acid 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:0050051; F:leukotriene-B4 20-monooxygenase activity; ISO:MGI.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; ISO:MGI.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; ISO:MGI.
DR GO; GO:0052872; F:tocotrienol omega-hydroxylase activity; ISO:MGI.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISO:MGI.
DR GO; GO:0006690; P:icosanoid metabolic process; ISO:MGI.
DR GO; GO:0036101; P:leukotriene B4 catabolic process; ISO:MGI.
DR GO; GO:0042361; P:menaquinone catabolic process; IBA:GO_Central.
DR GO; GO:0097267; P:omega-hydroxylase P450 pathway; ISO:MGI.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..524
FT /note="Leukotriene-B4 omega-hydroxylase 3"
FT /id="PRO_0000051858"
FT BINDING 328
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P51869"
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:P51869"
SQ SEQUENCE 524 AA; 59800 MW; A89F80E10925E9F4 CRC64;
MSQLSLSWLG LGPEVAFPWK TLLLLGASWI LARILIQIYA AYRNYRHLHG FPQPPKRNWL
MGHVGMVTPT EQGLKELTRL VGTYPQGFLM WIGPMVPVIT LCHSDIVRSI LNASAAVALK
DVIFYSILKP WLGDGLLVSA GDKWSRHRRM LTPAFHFNIL KPYVKIFNDS TNIMHAKWQR
LISDGSARLD MFEHVSLMTL DSLQKCVFSF DSNCQEKSSE YIAAILELSA LVAKRHQQPL
MFMDLLYNLT PDGMRFRKAC NVVHEFTDAV IRERHRTLPD QGLDDFLKSK AKSKTLDFID
VLLLSKDEDG KELSDEDIRA EADTFMFEGH DTTASGLSWI LYNLARHPEY QERCRQEVQE
LLRGREPEEI EWDDLAQLPF LTMCIKESLR LHPPVTVISR CCTQDILLPD GRTIPKGIIC
LISIFGIHHN PSVWPDPEVY DPFRFDPENI KDSSPLAFIP FSAGPRNCIG QTFAMSEMKV
ALALTLLRFR LLPDDKEPRR QPELILRAEG GLWLRVEPLS AGAH
