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Q99N16 (CP4F3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Cyp4f3
Synonyms:Cyp4f18
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.5 UniProtKB Q08477

Catalytic activity

(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. UniProtKB Q08477

Cofactor

Heme group By similarity.

Enzyme regulation

Inhibited by carbon monoxide (CO) By similarity. UniProtKB Q08477

Pathway

Lipid metabolism; leukotriene B4 degradation.

Subcellular location

Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Microsome membrane; Single-pass membrane protein By similarity.

Tissue specificity

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. Ref.5

Induction

Up-regulated in myeloid dendritic cells upon induction with LPS in vitro. Down-regulated upon migration of induced cells to the lymph node. Ref.5

Sequence similarities

Belongs to the cytochrome P450 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 524524Leukotriene-B(4) omega-hydroxylase 2
PRO_0000238924

Regions

Transmembrane15 – 3521Helical; Potential

Sites

Metal binding4681Iron (heme axial ligand) By similarity UniProtKB P33274

Experimental info

Sequence conflict61M → L in AAK15013. Ref.1
Sequence conflict61M → L in AAH13494. Ref.4
Sequence conflict371P → Q in AAK15013. Ref.1
Sequence conflict371P → Q in AAH13494. Ref.4
Sequence conflict1421D → G in BAB25315. Ref.2
Sequence conflict2301T → A in AAK15013. Ref.1
Sequence conflict2301T → A in AAH13494. Ref.4
Sequence conflict2841V → D in AAK15013. Ref.1
Sequence conflict2841V → D in AAH13494. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q99N16 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: E97FACEB00CFD7CB

FASTA52459,843
        10         20         30         40         50         60 
MSQLSMSWMG LGHTAASPWL LLLLAGASCL LAYILTPIYG VFENSLRLRC FPQPPKRNWI 

        70         80         90        100        110        120 
LGHLGLIQSS EEGLLYIQSL VRTFRDACCW WVGPLHPVIR IFHPAFIKPV VLAPALVAPK 

       130        140        150        160        170        180 
DTVFYRFLKP WLGDGLLMST GDKWSRHRRM LTPAFHFNIL KPYVKVFNDS TNIMHAKWQR 

       190        200        210        220        230        240 
LASKGSAYLN MFEHISLMTL DSLQKCVFSF DSNCQEKPSE YITAILELST LVARRHQRLL 

       250        260        270        280        290        300 
LHVDLFYYLT HDGMRFRKAC RLVHDFTDAV IRERRRTLLD QGGVDVLKAK AKAKTLDFID 

       310        320        330        340        350        360 
VLLLSKDEHG KALSDEDIRA EADTFMFGGH DTTASGLSWI LYNLARHPEY QERCRQEVRE 

       370        380        390        400        410        420 
LLRDREPEEI EWDDLAQLPF LTMCIKESLR LHPPVTAISR CCTQDIVLPD GRVIPKGVIS 

       430        440        450        460        470        480 
RISIFGTHHN PAVWPDPEVY DPFRFDADNV KGRSPLAFIP FSAGPRNCIG QTFAMSEMKV 

       490        500        510        520 
ALALTLLRFR VLPDDKEPRR KPELILRAEG GLWLKVEPLS AGAQ 

« Hide

References

« Hide 'large scale' references
[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: Kidney.
[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. expand/collapse author list , 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/6J.
Tissue: Pancreas.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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/N.
Tissue: Colon.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF233647 mRNA. Translation: AAK15013.1.
AK007863 mRNA. Translation: BAB25315.1.
AC162522 Genomic DNA. No translation available.
BC013494 mRNA. Translation: AAH13494.1.
RefSeqNP_077764.2. NM_024444.2.
XP_006509811.1. XM_006509748.1.
UniGeneMm.160020.

3D structure databases

ProteinModelPortalQ99N16.
SMRQ99N16. Positions 96-524.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000003574.

PTM databases

PhosphoSiteQ99N16.

Proteomic databases

PaxDbQ99N16.
PRIDEQ99N16.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003574; ENSMUSP00000003574; ENSMUSG00000003484.
GeneID72054.
KEGGmmu:72054.
UCSCuc009mfe.2. mouse.

Organism-specific databases

CTD72054.
MGIMGI:1919304. Cyp4f18.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00730000110562.
HOGENOMHOG000233833.
HOVERGENHBG000182.
InParanoidQ99N16.
KOK17726.
OMARISIFGT.
OrthoDBEOG7CNZFK.
TreeFamTF105088.

Enzyme and pathway databases

UniPathwayUPA00883.

Gene expression databases

BgeeQ99N16.
GenevestigatorQ99N16.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio335324.
PROQ99N16.
SOURCESearch...

Entry information

Entry nameCP4F3_MOUSE
AccessionPrimary (citable) accession number: Q99N16
Secondary accession number(s): E9QLZ3, Q9D8N4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot