RFNG_XENLA
ID RFNG_XENLA Reviewed; 340 AA.
AC P79949;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Beta-1,3-N-acetylglucosaminyltransferase radical fringe;
DE EC=2.4.1.222;
DE AltName: Full=O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase;
GN Name=rfng;
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].
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. {ECO:0000250|UniProtKB:O09009}.
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:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; U77641; AAB19226.1; -; mRNA.
DR RefSeq; NP_001080939.1; NM_001087470.1.
DR AlphaFoldDB; P79949; -.
DR SMR; P79949; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GeneID; 394282; -.
DR KEGG; xla:394282; -.
DR CTD; 394282; -.
DR Xenbase; XB-GENE-864975; rfng.L.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 394282; Expressed in testis and 19 other tissues.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR InterPro; IPR003378; Fringe-like.
DR Pfam; PF02434; Fringe; 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..340
FT /note="Beta-1,3-N-acetylglucosaminyltransferase radical
FT fringe"
FT /id="PRO_0000219190"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..340
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..161
FT /evidence="ECO:0000250"
FT DISULFID 179..242
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 38679 MW; DF6C8BEAAAFB6715 CRC64;
MKITYVGLIK VCFLVFLLLC ATVLLNISWR QRDSSQSLQH CNSTCSAKYL ETKLKEAHLT
GRHKKWETYR LDAKPTSATG QGHQHFAKEP LQIKDLFIAV KTTKKYHGNR LNLLMQTWIS
RAKEQTFIFT DWEDQELRQK AGDQMVNTNC SAVHTRQALC CKMAVEYDKF VLSDKKWFCH
LDDDNYLNLH ALLDLLSTFS HSTDVYVGRP SLDHPVETVD RMKGDGSGSL KFWFATGGAG
FCISRGLALK MSPWASMGNF ISTAEKVRLP DDCTIGYIIE GMLDVKMQHS NLFHSHLEHL
QRLPTESLLK QVTLSYGGPD NKWNVVRVNG AFSLAEDPTR
