LFNG_RAT
ID LFNG_RAT Reviewed; 378 AA.
AC Q924T4;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Itoh N.;
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. Modulates NOTCH1 activity by modifying O-
CC fucose residues at specific EGF-like domains resulting in inhibition of
CC NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1
CC via an increase in its binding to DLL1. Decreases the binding of JAG1
CC to NOTCH2 but not that of DLL1. Essential mediator of somite
CC segmentation and patterning. {ECO:0000250|UniProtKB:O09010,
CC ECO:0000250|UniProtKB:Q8NES3}.
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 -!- 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; AB054539; BAB63256.1; -; mRNA.
DR EMBL; BC070933; AAH70933.1; -; mRNA.
DR RefSeq; NP_596884.1; NM_133393.2.
DR AlphaFoldDB; Q924T4; -.
DR SMR; Q924T4; -.
DR STRING; 10116.ENSRNOP00000001682; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q924T4; 1 site.
DR PhosphoSitePlus; Q924T4; -.
DR PaxDb; Q924T4; -.
DR Ensembl; ENSRNOT00000101623; ENSRNOP00000086737; ENSRNOG00000001250.
DR GeneID; 170905; -.
DR KEGG; rno:170905; -.
DR UCSC; RGD:620587; rat.
DR CTD; 3955; -.
DR RGD; 620587; Lfng.
DR eggNOG; ENOG502QV30; Eukaryota.
DR GeneTree; ENSGT00940000158717; -.
DR HOGENOM; CLU_056611_0_1_1; -.
DR InParanoid; Q924T4; -.
DR OMA; SENKMRP; -.
DR OrthoDB; 826272at2759; -.
DR PhylomeDB; Q924T4; -.
DR TreeFam; TF324207; -.
DR PRO; PR:Q924T4; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001250; Expressed in spleen and 18 other tissues.
DR Genevisible; Q924T4; RN.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033829; F:O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity; ISO:RGD.
DR GO; GO:0007386; P:compartment pattern specification; ISO:RGD.
DR GO; GO:0002315; P:marginal zone B cell differentiation; ISS:UniProtKB.
DR GO; GO:1902367; P:negative regulation of Notch signaling pathway involved in somitogenesis; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISO:RGD.
DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; ISO:RGD.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0014807; P:regulation of somitogenesis; ISO:RGD.
DR GO; GO:0001756; P:somitogenesis; ISS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; 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..378
FT /note="Beta-1,3-N-acetylglucosaminyltransferase lunatic
FT fringe"
FT /id="PRO_0000219178"
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..378
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 85..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 289
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT SITE 85..86
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 167..178
FT /evidence="ECO:0000250"
FT DISULFID 196..259
FT /evidence="ECO:0000250"
FT DISULFID 363..372
FT /evidence="ECO:0000250"
SQ SEQUENCE 378 AA; 41958 MW; 482A68ED60499066 CRC64;
MLQRCGRRLL LALVGALLAC LLVLTADPPP TPVPAERGRR ALRSLAGSSG AAPGPGSRAA
VDPGVLVREV HSLSEYFSLL TRARRDADPP PGVASRQGDG HPRPPAEVLS PRDVFIAVKT
TRKFHRARLD LLFETWISRH KEMTFIFTDG EDEALAKHTG NVVLTNCSAA HSRQALSCKM
AVEYDRFIES GKKWFCHVDD DNYVNLRALL RLLASYPHTQ DVYIGKPSLD RPIQATERIS
EHRVRPVHFW FATGGAGFCI SRGLALKMGP WASGGHFMST AERIRLPDDC TIGYIVEALL
GVPLIRSGLF HSHLENLQQV PTTELHEQVT LSYGMFENKR NAVHIKGPFS VEADPSRFRS
IHCHLYPDTP WCPRTAIL
