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O09010 (LFNG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe

EC=2.4.1.222
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene names
Name:Lfng
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules inhibiting Jagged mediated Notch signaling. Essential mediator of somite segmentation and patterning. During somite boundary formation, it restricts Notch activity in the presomitic mesoderm to a boundary-formig territory in the posterior half of the prospective somite. In this region, Notch function activates a set of genes that are involved in boundary formation and in anterior-posterior somite identity. Ectopically expressed in the thymus, Lfgn inhibits Notch signaling which results in inhibition of T-cell commitment and promotes B-cell development in lymphoid progenitors. May play a role in boundary formation of the enamel knot.

Catalytic activity

Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.

Cofactor

Manganese By similarity.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Detected at 12.5 dpc in all tissues examined with the highest level observed in adult brain and spleen. Detected in the dental epithelium.

Developmental stage

Developmental protein. During segmentation it shows a cyclic transcription pattern which is under the control of Notch. Expressed in the caudal region of the presomitic mesoderm with each cycle corresponding to the formation time of one somite. In the dental epithelium it is detected at stage E13.5. The pattern of expression corresponds exactly to the formation of the enamel knot between late bud and early cap stages. Ref.3 Ref.7 Ref.8 Ref.10

Post-translational modification

A soluble form may be derived from the membrane form by proteolytic processing.

Sequence similarities

Belongs to the glycosyltransferase 31 family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandManganese
Metal-binding
   Molecular functionDevelopmental protein
Glycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcompartment pattern specification

Inferred from mutant phenotype PubMed 12001066. Source: MGI

female meiotic division

Inferred from mutant phenotype PubMed 15659488. Source: MGI

metabolic process

Inferred from direct assay PubMed 16385447. Source: GOC

ovarian follicle development

Inferred from mutant phenotype PubMed 15659488. Source: MGI

positive regulation of Notch signaling pathway

Inferred from direct assay PubMed 15574878. Source: MGI

positive regulation of protein binding

Inferred from direct assay PubMed 15574878. Source: MGI

regulation of Notch signaling pathway

Inferred from direct assay PubMed 16385447. Source: UniProt

regulation of somitogenesis

Inferred from mutant phenotype PubMed 19779553. Source: MGI

somitogenesis

Inferred from mutant phenotype PubMed 18234727. Source: MGI

   Cellular_componentGolgi membrane

Traceable author statement. Source: Reactome

integral component of Golgi membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionO-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity

Inferred from direct assay PubMed 16385447. Source: UniProt

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
PRO_0000219177

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 378349Lumenal Potential

Sites

Active site2891 By similarity
Metal binding2011Manganese By similarity
Metal binding3131Manganese By similarity
Binding site1281Substrate By similarity
Binding site2001Substrate By similarity
Site85 – 862Cleavage; by furin-like protease Potential

Amino acid modifications

Glycosylation1661N-linked (GlcNAc...) Potential
Disulfide bond167 ↔ 178 By similarity
Disulfide bond196 ↔ 259 By similarity
Disulfide bond363 ↔ 372 By similarity

Experimental info

Sequence conflict3431V → M in AK004642. Ref.4
Sequence conflict3611V → I in AK004642. Ref.4

Sequences

Sequence LengthMass (Da)Tools
O09010 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: FD0A02597BF9AFED

FASTA37841,952
        10         20         30         40         50         60 
MLQRCGRRLL LALVGALLAC LLVLTADPPP TPMPAERGRR ALRSLAGSSG GAPASGSRAA 

        70         80         90        100        110        120 
VDPGVLTREV HSLSEYFSLL TRARRDADPP PGVASRQGDG HPRPPAEVLS PRDVFIAVKT 

       130        140        150        160        170        180 
TRKFHRARLD LLFETWISRH KEMTFIFTDG EDEALAKLTG NVVLTNCSSA HSRQALSCKM 

       190        200        210        220        230        240 
AVEYDRFIES GKKWFCHVDD DNYVNLRALL RLLASYPHTQ DVYIGKPSLD RPIQATERIS 

       250        260        270        280        290        300 
EHKVRPVHFW FATGGAGFCI SRGLALKMGP WASGGHFMST AERIRLPDDC TIGYIVEALL 

       310        320        330        340        350        360 
GVPLIRSGLF HSHLENLQQV PTTELHEQVT LSYGMFENKR NAVHIKGPFS VEADPSRFRS 

       370 
VHCHLYPDTP WCPRSAIF 

« Hide

References

« Hide 'large scale' references
[1]"A family of mammalian Fringe genes implicated in boundary determination and the Notch pathway."
Johnston S.H., Rauskolb C., Wilson R., Prabhakaran B., Irvine K.D., Vogt T.F.
Development 124:2245-2254(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Fringe boundaries coincide with Notch-dependent patterning centres in mammals and alter Notch-dependent development in Drosophila."
Cohen B., Bashirullah A., Dagnino L., Campbell C., Fisher W.W., Leow C.C., Whiting E., Ryan D., Zinyk D., Boulianne G., Hui C.-C., Gallie B., Phillips R.A., Lipshitz H.D., Egan S.E.
Nat. Genet. 16:283-288(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Clock regulatory elements control cyclic expression of Lunatic fringe during somitogenesis."
Cole S.E., Levorse J.M., Tilghman S.M., Vogt T.F.
Dev. Cell 3:75-84(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-143, DEVELOPMENTAL STAGE.
Strain: 129S6/SvEvTac.
[4]"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: Bone marrow and Lung.
[5]"Interaction between Notch signalling and Lunatic fringe during somite boundary formation in the mouse."
del Barco Barrantes I., Elia A.J., Wuensch K., De Angelis M.H., Mak T.W., Rossant J., Conlon R.A., Gossler A., de la Pompa J.L.
Curr. Biol. 9:470-480(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Lunatic fringe, FGF, and BMP regulate the Notch pathway during epithelial morphogenesis of teeth."
Mustonen T., Tuemmers M., Mikami T., Itoh N., Zhang N., Gridley T., Thesleff I.
Dev. Biol. 248:281-293(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Lunatic fringe is an essential mediator of somite segmentation and patterning."
Evrard Y.A., Lun Y., Aulehla A., Gan L., Johnson R.L.
Nature 394:377-381(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[8]"Genomic structure, mapping, and expression analysis of the mammalian Lunatic, Manic, and Radical fringe genes."
Moran J.L., Johnston S.H., Rauskolb C., Bhalerao J., Bowcock A.M., Vogt T.F.
Mamm. Genome 10:535-541(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[9]"Subversion of the T/B lineage decision in the thymus by lunatic fringe-mediated inhibition of Notch-1."
Koch U., Lacombe T.A., Holland D., Bowman J.L., Cohen B.L., Egan S.E., Guidos C.J.
Immunity 15:225-236(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"Periodic Lunatic fringe expression is controlled during segmentation by a cyclic transcriptional enhancer responsive to notch signaling."
Morales A.V., Yasuda Y., Ish-Horowicz D.
Dev. Cell 3:63-74(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

lunatic fringe gene homolog (lfng)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U94351 mRNA. Translation: AAC53262.1.
AF015768 mRNA. Translation: AAB71668.1.
AY124581 Genomic DNA. Translation: AAM93541.1.
AK004642 mRNA. No translation available.
AK153283 mRNA. Translation: BAE31866.1.
CCDSCCDS19821.1.
RefSeqNP_032520.1. NM_008494.3.
UniGeneMm.12834.

3D structure databases

ProteinModelPortalO09010.
SMRO09010. Positions 113-373.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSiteO09010.

Proteomic databases

PRIDEO09010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031555; ENSMUSP00000031555; ENSMUSG00000029570.
GeneID16848.
KEGGmmu:16848.
UCSCuc009ahu.1. mouse.

Organism-specific databases

CTD3955.
MGIMGI:1095413. Lfng.

Phylogenomic databases

eggNOGNOG70217.
GeneTreeENSGT00390000009913.
HOGENOMHOG000046678.
HOVERGENHBG007986.
InParanoidO09010.
KOK05948.
OMAFRSVHCH.
OrthoDBEOG7ZSHTD.
PhylomeDBO09010.
TreeFamTF324207.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

ArrayExpressO09010.
BgeeO09010.
GenevestigatorO09010.

Family and domain databases

InterProIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
ProtoNetSearch...

Other

NextBio290782.
PROO09010.
SOURCESearch...

Entry information

Entry nameLFNG_MOUSE
AccessionPrimary (citable) accession number: O09010
Secondary accession number(s): Q3U659, Q8K3F1, Q9DC10
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 115 of the entry and version 1 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

MGD cross-references

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