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Protein

Leukotriene-B(4) omega-hydroxylase 2

Gene

Cyp4f3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Cytochromes P450 are a group of heme-thiolate monooxygenases. This enzyme requires molecular oxygen and NADPH for the omega-hydroxylation of LTB4, a potent chemoattractant for polymorphonuclear leukocytes.By similarity1 Publication

Catalytic activityi

(6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + NADPH + O2 = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa-6,8,10,14-tetraenoate + NADP+ + H2O.By similarity

Cofactori

hemeBy similarity

Enzyme regulationi

Inhibited by carbon monoxide (CO).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi468 – 4681Iron (heme axial ligand)By similarity

GO - Molecular functioni

  1. alkane 1-monooxygenase activity Source: MGI
  2. alpha-tocopherol omega-hydroxylase activity Source: MGI
  3. arachidonic acid epoxygenase activity Source: MGI
  4. arachidonic acid omega-hydroxylase activity Source: MGI
  5. heme binding Source: InterPro
  6. iron ion binding Source: InterPro
  7. leukotriene-B4 20-monooxygenase activity Source: MGI
  8. 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 Source: MGI
  9. tocotrienol omega-hydroxylase activity Source: MGI
  10. vitamin-K-epoxide reductase (warfarin-sensitive) activity Source: MGI

GO - Biological processi

  1. arachidonic acid metabolic process Source: MGI
  2. drug metabolic process Source: MGI
  3. epoxygenase P450 pathway Source: MGI
  4. leukotriene B4 catabolic process Source: MGI
  5. long-chain fatty acid metabolic process Source: MGI
  6. menaquinone catabolic process Source: MGI
  7. negative regulation of blood coagulation Source: MGI
  8. negative regulation of icosanoid secretion Source: MGI
  9. oxidation-reduction process Source: MGI
  10. phylloquinone catabolic process Source: MGI
  11. positive regulation of icosanoid secretion Source: MGI
  12. regulation of blood pressure Source: MGI
  13. very long-chain fatty acid metabolic process Source: MGI
  14. vitamin E metabolic process Source: MGI
  15. vitamin K biosynthetic process Source: MGI
  16. vitamin K catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

ReactomeiREACT_281747. Eicosanoids.
REACT_300263. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
REACT_314116. Miscellaneous substrates.
REACT_321024. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_331519. Fatty acids.
UniPathwayiUPA00883.

Names & Taxonomyi

Protein namesi
Recommended name:
Leukotriene-B(4) omega-hydroxylase 2 (EC:1.14.13.30)
Alternative name(s):
CYPIVF3
Cytochrome P450 4F3
Cytochrome P450-LTB-omega
Leukotriene-B(4) 20-monooxygenase 2
Gene namesi
Name:Cyp4f3By similarity
Synonyms:Cyp4f18Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1919304. Cyp4f18.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei15 – 3521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: MGI
  2. cytoplasm Source: MGI
  3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
  5. intracellular membrane-bounded organelle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 524524Leukotriene-B(4) omega-hydroxylase 2PRO_0000238924Add
BLAST

Proteomic databases

PaxDbiQ99N16.
PRIDEiQ99N16.

PTM databases

PhosphoSiteiQ99N16.

Expressioni

Tissue specificityi

Highest level in polymorphonuclear leukocytes and dendritic cells. Detectable in lymph nodes, spleen, bone marrow and peripheral blood. Highly expressed in ovary. Very low level in liver, kidney, and smooth muscle.1 Publication

Inductioni

Up-regulated in myeloid dendritic cells upon induction with LPS in vitro. Down-regulated upon migration of induced cells to the lymph node.1 Publication

Gene expression databases

BgeeiQ99N16.
GenevestigatoriQ99N16.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003574.

Structurei

3D structure databases

ProteinModelPortaliQ99N16.
SMRiQ99N16. Positions 96-524.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Sequence Analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000118816.
HOGENOMiHOG000233833.
HOVERGENiHBG000182.
InParanoidiQ99N16.
KOiK17726.
OMAiRISIFGT.
OrthoDBiEOG7CNZFK.
TreeFamiTF105088.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99N16-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQLSMSWMG LGHTAASPWL LLLLAGASCL LAYILTPIYG VFENSLRLRC
60 70 80 90 100
FPQPPKRNWI LGHLGLIQSS EEGLLYIQSL VRTFRDACCW WVGPLHPVIR
110 120 130 140 150
IFHPAFIKPV VLAPALVAPK DTVFYRFLKP WLGDGLLMST GDKWSRHRRM
160 170 180 190 200
LTPAFHFNIL KPYVKVFNDS TNIMHAKWQR LASKGSAYLN MFEHISLMTL
210 220 230 240 250
DSLQKCVFSF DSNCQEKPSE YITAILELST LVARRHQRLL LHVDLFYYLT
260 270 280 290 300
HDGMRFRKAC RLVHDFTDAV IRERRRTLLD QGGVDVLKAK AKAKTLDFID
310 320 330 340 350
VLLLSKDEHG KALSDEDIRA EADTFMFGGH DTTASGLSWI LYNLARHPEY
360 370 380 390 400
QERCRQEVRE LLRDREPEEI EWDDLAQLPF LTMCIKESLR LHPPVTAISR
410 420 430 440 450
CCTQDIVLPD GRVIPKGVIS RISIFGTHHN PAVWPDPEVY DPFRFDADNV
460 470 480 490 500
KGRSPLAFIP FSAGPRNCIG QTFAMSEMKV ALALTLLRFR VLPDDKEPRR
510 520
KPELILRAEG GLWLKVEPLS AGAQ
Length:524
Mass (Da):59,843
Last modified:July 27, 2011 - v2
Checksum:iE97FACEB00CFD7CB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61M → L in AAK15013 (Ref. 1) Curated
Sequence conflicti6 – 61M → L in AAH13494 (PubMed:15489334).Curated
Sequence conflicti37 – 371P → Q in AAK15013 (Ref. 1) Curated
Sequence conflicti37 – 371P → Q in AAH13494 (PubMed:15489334).Curated
Sequence conflicti142 – 1421D → G in BAB25315 (PubMed:16141072).Curated
Sequence conflicti230 – 2301T → A in AAK15013 (Ref. 1) Curated
Sequence conflicti230 – 2301T → A in AAH13494 (PubMed:15489334).Curated
Sequence conflicti284 – 2841V → D in AAK15013 (Ref. 1) Curated
Sequence conflicti284 – 2841V → D in AAH13494 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF233647 mRNA. Translation: AAK15013.1.
AK007863 mRNA. Translation: BAB25315.1.
AC162522 Genomic DNA. No translation available.
BC013494 mRNA. Translation: AAH13494.1.
CCDSiCCDS22406.1.
RefSeqiNP_077764.2. NM_024444.2.
XP_006509811.1. XM_006509748.1.
UniGeneiMm.160020.

Genome annotation databases

EnsembliENSMUST00000003574; ENSMUSP00000003574; ENSMUSG00000003484.
GeneIDi72054.
KEGGimmu:72054.
UCSCiuc009mfe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF233647 mRNA. Translation: AAK15013.1.
AK007863 mRNA. Translation: BAB25315.1.
AC162522 Genomic DNA. No translation available.
BC013494 mRNA. Translation: AAH13494.1.
CCDSiCCDS22406.1.
RefSeqiNP_077764.2. NM_024444.2.
XP_006509811.1. XM_006509748.1.
UniGeneiMm.160020.

3D structure databases

ProteinModelPortaliQ99N16.
SMRiQ99N16. Positions 96-524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000003574.

PTM databases

PhosphoSiteiQ99N16.

Proteomic databases

PaxDbiQ99N16.
PRIDEiQ99N16.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003574; ENSMUSP00000003574; ENSMUSG00000003484.
GeneIDi72054.
KEGGimmu:72054.
UCSCiuc009mfe.2. mouse.

Organism-specific databases

CTDi72054.
MGIiMGI:1919304. Cyp4f18.

Phylogenomic databases

eggNOGiCOG2124.
GeneTreeiENSGT00760000118816.
HOGENOMiHOG000233833.
HOVERGENiHBG000182.
InParanoidiQ99N16.
KOiK17726.
OMAiRISIFGT.
OrthoDBiEOG7CNZFK.
TreeFamiTF105088.

Enzyme and pathway databases

UniPathwayiUPA00883.
ReactomeiREACT_281747. Eicosanoids.
REACT_300263. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
REACT_314116. Miscellaneous substrates.
REACT_321024. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_331519. Fatty acids.

Miscellaneous databases

NextBioi335324.
PROiQ99N16.
SOURCEiSearch...

Gene expression databases

BgeeiQ99N16.
GenevestigatoriQ99N16.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Protein expression and catalytic activity assessment of mouse 4F clones."
    Antonovic L., Kawashima H., Strobel H.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: KidneyImported.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
    Tissue: PancreasImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/NImported.
    Tissue: ColonImported.
  5. "Cytochrome P-450 4F18 is the leukotriene B4 omega-1/omega-2 hydroxylase in mouse polymorphonuclear leukocytes: identification as the functional orthologue of human polymorphonuclear leukocyte CYP4F3A in the down-regulation of responses to LTB4."
    Christmas P., Tolentino K., Primo V., Berry K.Z., Murphy R.C., Chen M., Lee D.M., Soberman R.J.
    J. Biol. Chem. 281:7189-7196(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.

Entry informationi

Entry nameiCP4F3_MOUSE
AccessioniPrimary (citable) accession number: Q99N16
Secondary accession number(s): E9QLZ3, Q9D8N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.