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Reviewed, UniProtKB/Swiss-Prot Q9EP75 (CP4FE_MOUSE)

Last modified June 16, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Leukotriene-B4 omega-hydroxylase 3
    EC=1.14.13.30
Alternative name(s):
    Cytochrome P450 4F14
    Leukotriene-B4 20-monooxygenase 3
    Cytochrome P450-LTB-omega
    Cyp4f-14
Gene names
Name: Cyp4f14
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length524 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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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 By similarity.

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.

Cofactor

Heme group By similarity.

Pathway

Lipid metabolism; leukotriene B4 degradation.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein By similarity. Microsome membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the cytochrome P450 family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 524524Leukotriene-B4 omega-hydroxylase 3
PRO_0000051858

Sites

Metal binding4681Iron (heme axial ligand) By similarity
Binding site3281Heme (covalent; via 1 link) By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9EP75-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: A89F80E10925E9F4

FASTA52459,800
        10         20         30         40         50         60 
MSQLSLSWLG LGPEVAFPWK TLLLLGASWI LARILIQIYA AYRNYRHLHG FPQPPKRNWL 

        70         80         90        100        110        120 
MGHVGMVTPT EQGLKELTRL VGTYPQGFLM WIGPMVPVIT LCHSDIVRSI LNASAAVALK 

       130        140        150        160        170        180 
DVIFYSILKP WLGDGLLVSA GDKWSRHRRM LTPAFHFNIL KPYVKIFNDS TNIMHAKWQR 

       190        200        210        220        230        240 
LISDGSARLD MFEHVSLMTL DSLQKCVFSF DSNCQEKSSE YIAAILELSA LVAKRHQQPL 

       250        260        270        280        290        300 
MFMDLLYNLT PDGMRFRKAC NVVHEFTDAV IRERHRTLPD QGLDDFLKSK AKSKTLDFID 

       310        320        330        340        350        360 
VLLLSKDEDG KELSDEDIRA EADTFMFEGH DTTASGLSWI LYNLARHPEY QERCRQEVQE 

       370        380        390        400        410        420 
LLRGREPEEI EWDDLAQLPF LTMCIKESLR LHPPVTVISR CCTQDILLPD GRTIPKGIIC 

       430        440        450        460        470        480 
LISIFGIHHN PSVWPDPEVY DPFRFDPENI KDSSPLAFIP FSAGPRNCIG QTFAMSEMKV 

       490        500        510        520 
ALALTLLRFR LLPDDKEPRR QPELILRAEG GLWLRVEPLS AGAH

« Hide

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References

« Hide 'large scale' references
[1]"Mouse liver leukotriene B4 omega-hydroxylase."
Kikuta Y., Kasyu H., Kusunose E., Kusunose M.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Liver.
[2]"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].
Strain: 129/Sv.
Tissue: Brain.
[3]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cecum and Liver.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AB037541 mRNA. Translation: BAB12564.1.
AB037540 mRNA. Translation: BAB12563.1.
AF233644 mRNA. Translation: AAK15010.1.
AK005007 mRNA. Translation: BAB23740.1.
AK018676 mRNA. Translation: BAB31338.1.
BC011228 mRNA. Translation: AAH11228.1.
BC094016 mRNA. Translation: AAH94016.1.
IPIIPI00109257.
RefSeqNP_071879.1.
UniGeneMm.426027

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ9EP75.

Genome annotation databases

EnsemblENSMUSG00000024292. Mus musculus. [Contig view]
GeneID64385.
KEGGmmu:64385.

Organism-specific databases

MGIMGI:1927669. Cyp4f14.

Phylogenomic databases

HOGENOMQ9EP75.
HOVERGENQ9EP75.
OMAQ9EP75. ERHRTLP.

Enzyme and pathway databases

BRENDA1.14.13.30. 244.

Gene expression databases

ArrayExpressQ9EP75.
BgeeQ9EP75.
GermOnlineENSMUSG00000024292. Mus musculus.

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHERPTHR19383. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio320067.
SOURCESearch...

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Entry information

Entry nameCP4FE_MOUSE
AccessionPrimary (citable) accession number: Q9EP75
Secondary accession number(s): Q52L93
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2001
Last modified: June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents