Reviewed, UniProtKB/Swiss-Prot Q99N16 (CP4F3_MOUSE)

Names and origin

Protein names

Recommended name:
    Leukotriene-B(4) omega-hydroxylase 2
    EC=1.14.13.30
Alternative name(s):
    Cytochrome P450 4F3
    CYPIVF3
    Leukotriene-B(4) 20-monooxygenase 2
    Cytochrome P450-LTB-omega

Gene names

Name:	Cyp4f3
Synonyms:	Cyp4f18

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	524 AA.
Sequence status	Complete.
Protein existence	Evidence 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.4 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.4
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.4
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Transmembrane
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro leukotriene-B4 20-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 524	524	Leukotriene-B(4) omega-hydroxylase 2		PRO_0000238924
Regions
	Transmembrane	15 – 35	21	Potential
Sites
	Metal binding	468	1	Iron (heme axial ligand) By similarity UniProtKB P33274
Experimental info
	Sequence conflict	6	1	L → M in BAB25315. Ref.2
	Sequence conflict	37	1	Q → P in BAB25315. Ref.2
	Sequence conflict	142	1	D → G in BAB25315. Ref.2
	Sequence conflict	230	1	A → T in BAB25315. Ref.2
	Sequence conflict	284	1	D → V in BAB25315. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q99N16-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 728F21423CA8864D	FASTA	524	59,842
	10 20 30 40 50 60 MSQLSLSWMG LGHTAASPWL LLLLAGASCL LAYILTQIYG 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 YITAILELSA LVARRHQRLL 250 260 270 280 290 300 LHVDLFYYLT HDGMRFRKAC RLVHDFTDAV IRERRRTLLD QGGDDVLKAK 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

References

	« Hide 'large scale' referencesShow '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. , 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: Pancreas.
[3]	"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: Colon.
[4]	"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: 16380383] [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. BC013494 mRNA. Translation: AAH13494.1.
IPI	IPI00117991.
RefSeq	NP_077764.2.
UniGene	Mm.160020
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q99N16.
Proteomic databases
PRIDE	Q99N16.
Genome annotation databases
Ensembl	ENSMUST00000003574; ENSMUSP00000003574; ENSMUSG00000003484; Mus musculus. [Genome view]
GeneID	72054.
KEGG	mmu:72054.
UCSC	uc009mfe.1. mouse.
Organism-specific databases
CTD	72054.
MGI	MGI:1919304. Cyp4f18.
Phylogenomic databases
eggNOG	maNOG13304.
HOGENOM	HBG505954.
HOVERGEN	Q99N16.
InParanoid	Q99N16.
PhylomeDB	Q99N16.
Enzyme and pathway databases
BRENDA	1.14.13.30. 244.
Gene expression databases
ArrayExpress	Q99N16.
Bgee	Q99N16.
Genevestigator	Q99N16.
GermOnline	ENSMUSG00000003484. Mus musculus.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017973. Cyt_P450_C. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
PANTHER	PTHR19383. Cyt_P450. 1 hit.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	335324.
SOURCE	Search...

Entry information

Entry name

CP4F3_MOUSE

Accession

Primary (citable) accession number: Q99N16
Secondary accession number(s): Q9D8N4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	June 1, 2001
Last modified:	February 9, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)