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Protein

Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe

Gene

Lfng

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

Functioni

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 activityi

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

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei85 – 862Cleavage; by furin-like proteaseSequence Analysis
Binding sitei128 – 1281SubstrateBy similarity
Binding sitei200 – 2001SubstrateBy similarity
Metal bindingi201 – 2011ManganeseBy similarity
Active sitei289 – 2891By similarity
Metal bindingi313 – 3131ManganeseBy similarity

GO - Molecular functioni

GO - Biological processi

  • compartment pattern specification Source: MGI
  • female meiotic division Source: MGI
  • metabolic process Source: GOC
  • ovarian follicle development Source: MGI
  • positive regulation of Notch signaling pathway Source: MGI
  • positive regulation of protein binding Source: MGI
  • regulation of Notch signaling pathway Source: UniProtKB
  • regulation of somitogenesis Source: MGI
  • somitogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.222. 3474.
ReactomeiREACT_321348. Pre-NOTCH Processing in Golgi.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (EC:2.4.1.222)
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene namesi
Name:Lfng
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1095413. Lfng.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence Analysis
Transmembranei9 – 2921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 378349LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 378378Beta-1,3-N-acetylglucosaminyltransferase lunatic fringePRO_0000219177Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi167 ↔ 178By similarity
Disulfide bondi196 ↔ 259By similarity
Disulfide bondi363 ↔ 372By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiO09010.

PTM databases

PhosphoSiteiO09010.

Expressioni

Tissue specificityi

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 stagei

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.4 Publications

Gene expression databases

BgeeiO09010.
ExpressionAtlasiO09010. baseline and differential.
GenevisibleiO09010. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031555.

Structurei

3D structure databases

ProteinModelPortaliO09010.
SMRiO09010. Positions 113-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG70217.
GeneTreeiENSGT00390000009913.
HOGENOMiHOG000046678.
HOVERGENiHBG007986.
InParanoidiO09010.
KOiK05948.
OMAiWISRNAQ.
OrthoDBiEOG7ZSHTD.
PhylomeDBiO09010.
TreeFamiTF324207.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.

Sequencei

Sequence statusi: Complete.

O09010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQRCGRRLL LALVGALLAC LLVLTADPPP TPMPAERGRR ALRSLAGSSG
60 70 80 90 100
GAPASGSRAA VDPGVLTREV HSLSEYFSLL TRARRDADPP PGVASRQGDG
110 120 130 140 150
HPRPPAEVLS PRDVFIAVKT TRKFHRARLD LLFETWISRH KEMTFIFTDG
160 170 180 190 200
EDEALAKLTG NVVLTNCSSA HSRQALSCKM AVEYDRFIES GKKWFCHVDD
210 220 230 240 250
DNYVNLRALL RLLASYPHTQ DVYIGKPSLD RPIQATERIS EHKVRPVHFW
260 270 280 290 300
FATGGAGFCI SRGLALKMGP WASGGHFMST AERIRLPDDC TIGYIVEALL
310 320 330 340 350
GVPLIRSGLF HSHLENLQQV PTTELHEQVT LSYGMFENKR NAVHIKGPFS
360 370
VEADPSRFRS VHCHLYPDTP WCPRSAIF
Length:378
Mass (Da):41,952
Last modified:July 1, 1997 - v1
Checksum:iFD0A02597BF9AFED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti343 – 3431V → M in AK004642 (PubMed:16141072).Curated
Sequence conflicti361 – 3611V → I in AK004642 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19821.1.
RefSeqiNP_032520.1. NM_008494.3.
UniGeneiMm.12834.

Genome annotation databases

EnsembliENSMUST00000031555; ENSMUSP00000031555; ENSMUSG00000029570.
GeneIDi16848.
KEGGimmu:16848.
UCSCiuc009ahu.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

lunatic fringe gene homolog (lfng)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19821.1.
RefSeqiNP_032520.1. NM_008494.3.
UniGeneiMm.12834.

3D structure databases

ProteinModelPortaliO09010.
SMRiO09010. Positions 113-373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031555.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

PTM databases

PhosphoSiteiO09010.

Proteomic databases

PRIDEiO09010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031555; ENSMUSP00000031555; ENSMUSG00000029570.
GeneIDi16848.
KEGGimmu:16848.
UCSCiuc009ahu.1. mouse.

Organism-specific databases

CTDi3955.
MGIiMGI:1095413. Lfng.

Phylogenomic databases

eggNOGiNOG70217.
GeneTreeiENSGT00390000009913.
HOGENOMiHOG000046678.
HOVERGENiHBG007986.
InParanoidiO09010.
KOiK05948.
OMAiWISRNAQ.
OrthoDBiEOG7ZSHTD.
PhylomeDBiO09010.
TreeFamiTF324207.

Enzyme and pathway databases

BRENDAi2.4.1.222. 3474.
ReactomeiREACT_321348. Pre-NOTCH Processing in Golgi.

Miscellaneous databases

NextBioi290782.
PROiO09010.
SOURCEiSearch...

Gene expression databases

BgeeiO09010.
ExpressionAtlasiO09010. baseline and differential.
GenevisibleiO09010. MM.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiLFNG_MOUSE
AccessioniPrimary (citable) accession number: O09010
Secondary accession number(s): Q3U659, Q8K3F1, Q9DC10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: July 1, 1997
Last modified: July 22, 2015
This is version 124 of the entry and version 1 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. 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.