LFNG_XENLA
ID LFNG_XENLA Reviewed; 375 AA.
AC P79948;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe;
DE EC=2.4.1.222;
DE AltName: Full=O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase;
GN Name=lfng;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=8662522; DOI=10.1126/science.273.5273.355;
RA Wu J.Y., Wen L., Zhang W.-J., Rao Y.;
RT "The secreted product of Xenopus gene lunatic Fringe, a vertebrate
RT signaling molecule.";
RL Science 273:355-358(1996).
CC -!- FUNCTION: Glycosyltransferase that initiates the elongation of O-linked
CC fucose residues attached to EGF-like repeats in the extracellular
CC domain of Notch molecules. Essential mediator of somite segmentation
CC and patterning (By similarity). May be involved in mesoderm development
CC (PubMed:8662522). {ECO:0000250|UniProtKB:O09010,
CC ECO:0000269|PubMed:8662522}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] +
CC UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-
CC (1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-
CC COMP:17923, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:189631, ChEBI:CHEBI:189634; EC=2.4.1.222;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP-
CC N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-
CC (1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:70511, Rhea:RHEA-COMP:17919, Rhea:RHEA-
CC COMP:17920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:189632, ChEBI:CHEBI:189633; EC=2.4.1.222;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in the neural tube, the eye and the otic
CC vesicle, expression coincides with the region that produces the medial,
CC intermediate and lateral neurons. {ECO:0000269|PubMed:8662522}.
CC -!- DEVELOPMENTAL STAGE: Developmental protein. Present as a maternal
CC component before zygotic transcription begins. Detected in animal,
CC marginal and vegetal regions in late blastula and gastrula embryos.
CC Later expressed in the neural tube, in the medial intermediate, and
CC later neurons. Detected in the eyes at stage 25 until stage 28. At
CC stage 35 not detected in the eyes but in the otic vesicles.
CC {ECO:0000269|PubMed:8662522}.
CC -!- PTM: A soluble form may be derived from the membrane form by
CC proteolytic processing. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; U77640; AAB19225.1; -; mRNA.
DR RefSeq; NP_001081471.1; NM_001088002.1.
DR AlphaFoldDB; P79948; -.
DR SMR; P79948; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GeneID; 397855; -.
DR KEGG; xla:397855; -.
DR CTD; 397855; -.
DR Xenbase; XB-GENE-17334134; lfng.S.
DR OrthoDB; 826272at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 397855; Expressed in internal ear and 19 other tissues.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033829; F:O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007389; P:pattern specification process; IEA:InterPro.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR InterPro; IPR017374; Fringe.
DR InterPro; IPR003378; Fringe-like.
DR Pfam; PF02434; Fringe; 1.
DR PIRSF; PIRSF038073; B-acetylgalactosaminyltfrase; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..375
FT /note="Beta-1,3-N-acetylglucosaminyltransferase lunatic
FT fringe"
FT /id="PRO_0000219181"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..375
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 53..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT SITE 87..88
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 164..175
FT /evidence="ECO:0000250"
FT DISULFID 193..256
FT /evidence="ECO:0000250"
FT DISULFID 360..369
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 42134 MW; 9430EFAAA3DAF55E CRC64;
MLKNWGKKLL LSIVGATLTC LLVLVVDQQS RHMLETQSDH EPGSAAAVHL RADLDPANPG
DGGDPANSAQ DSGTFSAYFN KLTRVRRDVE QVAAPSKDSA APEEDITAND VFIAVKTTKK
FHRSRMDLLM DTWISRNKEQ TFIFTDGEDE ELQKKTGNVI STNCSAAHSR QALSCKMAVE
YDKFIESDKK WFCHVDDDNY VNVRTLVKLL SRYSHTNDIY IGKPSLDRPI QATERISESN
MRPVNFWFAT GGAGFCISRG LALKMSPWAS GGHFMNTAEK IRLPDDCTIG YIIESVLGVK
LIRSNLFHSH LENLHQVPQS EIHNQVTLSY GMFENKRNAI LMKGAFSVEE DPSRFRSVHC
LLYPDTPWCP WKAAY
