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Protein

Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe

Gene

lfng

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (By similarity). Involved in the correct formation of boundaries in the somites and hindbrain. Required for Delta-Notch-mediated induction of hypochord cells at the lateral borders of the midline precursor domain.By similarity2 Publications

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
Binding sitei123 – 1231SubstrateBy similarity
Binding sitei196 – 1961SubstrateBy similarity
Metal bindingi197 – 1971ManganeseBy similarity
Active sitei285 – 2851By similarity
Metal bindingi309 – 3091ManganeseBy similarity

GO - Molecular functioni

GO - Biological processi

  • fin regeneration Source: ZFIN
  • hypochord development Source: ZFIN
  • negative regulation of neuron differentiation Source: ZFIN
  • Notch signaling pathway Source: UniProtKB-KW
  • pattern specification process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Biological processi

Differentiation, Neurogenesis, Notch signaling pathway

Keywords - Ligandi

Manganese, Metal-binding

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
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 3

Organism-specific databases

ZFINiZDB-GENE-980605-16. 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 – 374345LumenalSequence 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 – 374374Beta-1,3-N-acetylglucosaminyltransferase lunatic fringePRO_0000219180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...)Sequence analysis
Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence analysis
Disulfide bondi163 ↔ 174By similarity
Disulfide bondi192 ↔ 255By similarity
Disulfide bondi359 ↔ 368By similarity

Post-translational modificationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei83 – 842Cleavage; by furin-like proteaseSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8JHF2.

Expressioni

Tissue specificityi

In the embryo, expressed along the A-P axis of the neural tube, within the lateral plate mesoderm, in the presomitic mesoderm and the somites, in specific rhombomeres of the hindbrain (even-numbered rhombomeres) and in the otic vesicles.2 Publications

Developmental stagei

Expressed both maternally and throughout the zygotic stages, with highest expression at the bud stage. No evidence for a cyclic pattern of expression in the presomitic mesoderm during somitogenesis. Expressed weakly at the epiboly stage (4.5 hours) throughout the blastoderm. Expression clears from marginal region and localizes to the epiblast cells of the animal pole. As gastrulation proceeds, expressed in hypoblast cells that migrate towards the animal pole, in the prechordal plate and in forerunner cells. At 90% epiboly, expressed in the neural plate. At the three somite stage (11 hours), expressed in a small cluster of cells within the tailbud region and in future spinal cord. From the 8-14 somite stages, expressed in alternating pre-rhombomeres of the hindbrain, and more broadly in mid- and forebrain. Also expressed weakly in the anterior margins of the formed somites and in the anterior presomitic mesoderm. At the end of somitogenesis (22 hours), expressed strongly in the telencephalon and anterior midbrain, weakly in other parts of the midbrain and variably in the hindbrain.4 Publications

Gene expression databases

BgeeiQ8JHF2.
ExpressionAtlasiQ8JHF2. differential.

Interactioni

Protein-protein interaction databases

STRINGi7955.ENSDARP00000031031.

Structurei

3D structure databases

ProteinModelPortaliQ8JHF2.
SMRiQ8JHF2. Positions 103-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II9W. Eukaryota.
ENOG410XS8Y. LUCA.
GeneTreeiENSGT00390000009913.
HOGENOMiHOG000046678.
HOVERGENiHBG007986.
InParanoidiQ8JHF2.
KOiK05948.
OMAiFENKRNI.
OrthoDBiEOG7ZSHTD.
PhylomeDBiQ8JHF2.
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.

Q8JHF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKTYRGKVV VSLAGATVTC LGFLLFLSQH QRIQADGMQN ESEVGLRSLQ
60 70 80 90 100
SLGDSETDDG AQPEQNAKKG FSAYFSKLTR SRREADKPSE APGAATDAPP
110 120 130 140 150
AEDISADDIF IAVKTTKKFH RSRLDLLLDT WISRNMRQTY IFTDGEDEEL
160 170 180 190 200
KKKIGSHAIN TNCSAAHSRQ ALSCKMAVEY DKFIESGKKW FCHVDDDNYV
210 220 230 240 250
NTKTLVKLLS NYPHTQDMYI GKPSLDRPIE ATERLGDNKM RPVNFWFATG
260 270 280 290 300
GAGFCISRGL ALKMSPWASG GHFMNTAEKI RLPDDCTIGY IIESVLGVSL
310 320 330 340 350
TRSSLFHSHL ENLQQVSKSE VHKQITLSYG MFENKRNIIN MKGAFSVEED
360 370
PSRFKSVHCL LYPDTPWCPP QVAY
Length:374
Mass (Da):41,882
Last modified:February 1, 2005 - v2
Checksum:i082F1FD0705B9A8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161A → T (PubMed:11429294).Curated
Sequence conflicti46 – 461L → LL (PubMed:11429294).Curated
Sequence conflicti64 – 674EQNA → DQENT (PubMed:11429294).Curated
Sequence conflicti109 – 1091I → M (PubMed:11429294).Curated
Sequence conflicti137 – 1371R → Q in AAM44059 (PubMed:15376327).Curated
Sequence conflicti344 – 3441A → V (PubMed:11429294).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007434 mRNA. Translation: AAG12160.1.
AF510992 mRNA. Translation: AAM44059.1.
BC044339 mRNA. Translation: AAH44339.1.
RefSeqiNP_571046.1. NM_130971.1.
UniGeneiDr.1831.

Genome annotation databases

EnsembliENSDART00000028673; ENSDARP00000031031; ENSDARG00000037879.
GeneIDi30158.
KEGGidre:30158.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY007434 mRNA. Translation: AAG12160.1.
AF510992 mRNA. Translation: AAM44059.1.
BC044339 mRNA. Translation: AAH44339.1.
RefSeqiNP_571046.1. NM_130971.1.
UniGeneiDr.1831.

3D structure databases

ProteinModelPortaliQ8JHF2.
SMRiQ8JHF2. Positions 103-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000031031.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Proteomic databases

PaxDbiQ8JHF2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000028673; ENSDARP00000031031; ENSDARG00000037879.
GeneIDi30158.
KEGGidre:30158.

Organism-specific databases

CTDi3955.
ZFINiZDB-GENE-980605-16. lfng.

Phylogenomic databases

eggNOGiENOG410II9W. Eukaryota.
ENOG410XS8Y. LUCA.
GeneTreeiENSGT00390000009913.
HOGENOMiHOG000046678.
HOVERGENiHBG007986.
InParanoidiQ8JHF2.
KOiK05948.
OMAiFENKRNI.
OrthoDBiEOG7ZSHTD.
PhylomeDBiQ8JHF2.
TreeFamiTF324207.

Miscellaneous databases

PROiQ8JHF2.

Gene expression databases

BgeeiQ8JHF2.
ExpressionAtlasiQ8JHF2. differential.

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. "Homologues of c-hairy1 (her9) and lunatic fringe in zebrafish are expressed in the developing central nervous system, but not in the presomitic mesoderm."
    Leve C., Gajewski M., Rohr K.B., Tautz D.
    Dev. Genes Evol. 211:493-500(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  3. "Lunatic fringe regulates Delta-Notch induction of hypochord in zebrafish."
    Appel B., Marasco P., McClung L.E., Latimer A.J.
    Dev. Dyn. 228:281-286(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  4. "Sequence and embryonic expression of three zebrafish fringe genes: lunatic fringe, radical fringe, and manic fringe."
    Qiu X., Xu H., Haddon C., Lewis J., Jiang Y.-J.
    Dev. Dyn. 231:621-630(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Embryo.
  5. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: AB.
  6. "Upstream regulatory region of zebrafish lunatic fringe: isolation and promoter analysis."
    Liu J., Sun Y.-H., Wang N., Wang Y.-P., Zhu Z.-Y.
    Mar. Biotechnol. 8:357-365(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiLFNG_DANRE
AccessioniPrimary (citable) accession number: Q8JHF2
Secondary accession number(s): Q9DEV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: February 1, 2005
Last modified: June 8, 2016
This is version 89 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.