RFNG_RAT
ID RFNG_RAT Reviewed; 334 AA.
AC Q9R1U9;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar;
RX PubMed=11165380; DOI=10.1016/s0169-328x(00)00278-3;
RA Mikami T., Ohnaka Y., Nakamura A., Kurosaka A., Itoh N.;
RT "Radical fringe negatively modulates Notch signaling in postmitotic neurons
RT of the rat brain.";
RL Brain Res. Mol. Brain Res. 86:138-144(2001).
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 enhancement
CC of NOTCH1 activation by DLL1 and JAG1 (By similarity). Inhibits Notch
CC signaling in postmitotic neurons of the brain. It may play a role in
CC adult brain and in neurogenesis (PubMed:11165380). It may play a role
CC in limb development (By similarity). {ECO:0000250|UniProtKB:O09009,
CC ECO:0000250|UniProtKB:O12972, ECO:0000269|PubMed:11165380}.
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 -!- TISSUE SPECIFICITY: Most abundantly expressed in adult brain. Expressed
CC in most neurons of the brain but not in glial cells. Also detected to a
CC lower extent in adult lung and kidney. {ECO:0000269|PubMed:11165380}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AB016486; BAA82742.1; -; mRNA.
DR RefSeq; NP_068621.1; NM_021849.1.
DR AlphaFoldDB; Q9R1U9; -.
DR SMR; Q9R1U9; -.
DR STRING; 10116.ENSRNOP00000067562; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q9R1U9; 1 site.
DR PaxDb; Q9R1U9; -.
DR GeneID; 60433; -.
DR KEGG; rno:60433; -.
DR CTD; 5986; -.
DR RGD; 621322; Rfng.
DR eggNOG; ENOG502QV30; Eukaryota.
DR InParanoid; Q9R1U9; -.
DR OrthoDB; 826272at2759; -.
DR PhylomeDB; Q9R1U9; -.
DR PRO; PR:Q9R1U9; -.
DR Proteomes; UP000002494; Unplaced.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:RGD.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007389; P:pattern specification process; IEA:InterPro.
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 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; Differentiation; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Neurogenesis; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..334
FT /note="Beta-1,3-N-acetylglucosaminyltransferase radical
FT fringe"
FT /id="PRO_0000219187"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..334
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 240
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..128
FT /evidence="ECO:0000250"
FT DISULFID 146..210
FT /evidence="ECO:0000250"
FT DISULFID 314..323
FT /evidence="ECO:0000250"
SQ SEQUENCE 334 AA; 36993 MW; ED0D21CFD5BFB40A CRC64;
MSRVRRVLCR ACLALAAVLA VLLLLPLPLP LPLPLPRAPA PDPGRVPTGS LTLEVSRLQP
DDVFIAVKTT RKNHGPRLRL LLRTWISRAP RQTFIFTDGD DPELQLLAGS QMINTNCSAV
RTRQALCCKM SVEYDKFIES GRKWFCHVDD DNYVNPKSLL HLLSTFSSNQ DIYLGRPSLD
HPIEATERVQ GGGTSNTVKF WFATGGAGFC LSRGLALKMS PWASLGSFMS TAERVRLPDD
CTVGYIVEGL LGARLLHSPL FHSHLENLQK LPSGAVLQQV TLSYGGPENP HNVVNVAGSF
SIRQDPTRFQ SVHCLLYPDT HWCPMKNRGK EAFQ
