LFNG_BOVIN
ID LFNG_BOVIN Reviewed; 380 AA.
AC Q2KJ92;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; BC105463; AAI05464.1; -; mRNA.
DR RefSeq; NP_001039687.1; NM_001046222.2.
DR AlphaFoldDB; Q2KJ92; -.
DR SMR; Q2KJ92; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q2KJ92; -.
DR PRIDE; Q2KJ92; -.
DR Ensembl; ENSBTAT00000083095; ENSBTAP00000057504; ENSBTAG00000040361.
DR GeneID; 516209; -.
DR KEGG; bta:516209; -.
DR CTD; 3955; -.
DR VEuPathDB; HostDB:ENSBTAG00000040361; -.
DR VGNC; VGNC:30849; LFNG.
DR eggNOG; ENOG502QV30; Eukaryota.
DR GeneTree; ENSGT00940000158717; -.
DR HOGENOM; CLU_056611_0_1_1; -.
DR InParanoid; Q2KJ92; -.
DR OMA; SENKMRP; -.
DR OrthoDB; 826272at2759; -.
DR TreeFam; TF324207; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000040361; Expressed in neutrophil and 102 other tissues.
DR ExpressionAtlas; Q2KJ92; baseline and differential.
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; IBA:GO_Central.
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:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
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..380
FT /note="Beta-1,3-N-acetylglucosaminyltransferase lunatic
FT fringe"
FT /id="PRO_0000250424"
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..380
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 85..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 291
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 315
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 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 169..180
FT /evidence="ECO:0000250"
FT DISULFID 198..261
FT /evidence="ECO:0000250"
FT DISULFID 365..374
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 41847 MW; 6C5720A3B180E682 CRC64;
MLKRCGRRLL LALAGALLAC LLVLTADPPP PPVPAERGRR ALRSLAGPSG VATAPGLEAA
AAAAPGAPVR EVHSLSEYFS LLTRSRRDVG PPPGGAPRPA DGPPRPLAEP LAPRDVFIAV
KTTKKFHRAR LDLLLETWIS RHEEMTFIFT DGEDEALARR TGHVVNTNCS AAHSRQALSC
KMAVEYDRFI ESGRKWFCHV DDDNYVNVRA LLRLLGSYPH TQDVYLGKPS LDRPIQATER
VSENKVRPVH FWFATGGAGF CISRGLALKM SPWASGGHFM STAERIRLPD DCTIGYIVEA
LLGVPLVRCG LFHSHLENLQ QVPASELHEQ VTLSYGMFEN KRNSVHIKGP FSVEADPSRF
RSVHCHLYPD TSWCPRSAIF
