RFNG_MOUSE
ID RFNG_MOUSE Reviewed; 332 AA.
AC O09009; B1ATU3;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9187150; DOI=10.1242/dev.124.11.2245;
RA Johnston S.H., Rauskolb C., Wilson R., Prabhakaran B., Irvine K.D.,
RA Vogt T.F.;
RT "A family of mammalian Fringe genes implicated in boundary determination
RT and the Notch pathway.";
RL Development 124:2245-2254(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9207795; DOI=10.1038/ng0797-283;
RA Cohen B., Bashirullah A., Dagnino L., Campbell C., Fisher W.W., Leow C.C.,
RA Whiting E., Ryan D., Zinyk D., Boulianne G., Hui C.-C., Gallie B.,
RA Phillips R.A., Lipshitz H.D., Egan S.E.;
RT "Fringe boundaries coincide with Notch-dependent patterning centres in
RT mammals and alter Notch-dependent development in Drosophila.";
RL Nat. Genet. 16:283-288(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=10341080; DOI=10.1007/s003359901039;
RA Moran J.L., Johnston S.H., Rauskolb C., Bhalerao J., Bowcock A.M.,
RA Vogt T.F.;
RT "Genomic structure, mapping, and expression analysis of the mammalian
RT Lunatic, Manic, and Radical fringe genes.";
RL Mamm. Genome 10:535-541(1999).
RN [6]
RP FUNCTION.
RX PubMed=28089369; DOI=10.1016/j.devcel.2016.12.013;
RA Kakuda S., Haltiwanger R.S.;
RT "Deciphering the fringe-mediated notch code: identification of activating
RT and inhibiting sites allowing discrimination between ligands.";
RL Dev. Cell 40:193-201(2017).
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 (PubMed:28089369). May be
CC involved in limb formation and in neurogenesis (By similarity).
CC {ECO:0000250|UniProtKB:O12972, ECO:0000250|UniProtKB:Q9R1U9,
CC ECO:0000269|PubMed:28089369}.
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: Detected in all the examined tissues (12.5 dpc).
CC High expression found in adult brain.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; U94350; AAC53261.1; -; mRNA.
DR EMBL; AF015770; AAB71670.1; -; mRNA.
DR EMBL; AL663090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066023; AAH66023.1; -; mRNA.
DR CCDS; CCDS25757.1; -.
DR RefSeq; NP_033079.1; NM_009053.2.
DR AlphaFoldDB; O09009; -.
DR SMR; O09009; -.
DR BioGRID; 202870; 1.
DR STRING; 10090.ENSMUSP00000026156; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; O09009; 1 site.
DR iPTMnet; O09009; -.
DR PhosphoSitePlus; O09009; -.
DR EPD; O09009; -.
DR PaxDb; O09009; -.
DR PRIDE; O09009; -.
DR ProteomicsDB; 255299; -.
DR Antibodypedia; 2622; 117 antibodies from 21 providers.
DR DNASU; 19719; -.
DR Ensembl; ENSMUST00000026156; ENSMUSP00000026156; ENSMUSG00000025158.
DR GeneID; 19719; -.
DR KEGG; mmu:19719; -.
DR UCSC; uc007mum.1; mouse.
DR CTD; 5986; -.
DR MGI; MGI:894275; Rfng.
DR VEuPathDB; HostDB:ENSMUSG00000025158; -.
DR eggNOG; ENOG502QV30; Eukaryota.
DR GeneTree; ENSGT00940000160801; -.
DR HOGENOM; CLU_056611_0_1_1; -.
DR InParanoid; O09009; -.
DR OMA; RKYHKTR; -.
DR OrthoDB; 826272at2759; -.
DR PhylomeDB; O09009; -.
DR TreeFam; TF324207; -.
DR BioGRID-ORCS; 19719; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Rfng; mouse.
DR PRO; PR:O09009; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O09009; protein.
DR Bgee; ENSMUSG00000025158; Expressed in ileal epithelium and 262 other tissues.
DR Genevisible; O09009; MM.
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; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IMP: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..332
FT /note="Beta-1,3-N-acetylglucosaminyltransferase radical
FT fringe"
FT /id="PRO_0000219186"
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..332
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 238
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..126
FT /evidence="ECO:0000250"
FT DISULFID 144..208
FT /evidence="ECO:0000250"
FT DISULFID 312..321
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 36926 MW; 4152A7547D917CA4 CRC64;
MSRARRVLCR ACLALAAVLA VLLLLPLPLP LPLPRAPAPD PDRVPTRSLT LEGDRLQPDD
VFIAVKTTRK NHGPRLRLLL RTWISRAPRQ TFIFTDGDDP ELQMLAGGRM INTNCSAVRT
RQALCCKMSV EYDKFLESGR KWFCHVDDDN YVNPKSLLHL LSTFSSNQDI YLGRPSLDHP
IEATERVQGG GTSNTVKFWF ATGGAGFCLS RGLALKMSPW ASLGSFMSTA ERVRLPDDCT
VGYIVEGLLG ARLLHSPLFH SHLENLQRLP SGAILQQVTL SYGGPENPHN VVNVAGSFNI
QQDPTRFQSV HCLLYPDTHW CPMKNRVEGA FQ
