RFNG_NOTVI
ID RFNG_NOTVI Reviewed; 396 AA.
AC Q9YHB3;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Beta-1,3-N-acetylglucosaminyltransferase radical fringe;
DE Short=nrFng;
DE EC=2.4.1.222;
DE AltName: Full=O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase;
GN Name=RFNG;
OS Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae;
OC Notophthalmus.
OX NCBI_TaxID=8316;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10090152;
RX DOI=10.1002/(sici)1097-0177(199903)214:3<259::aid-aja9>3.0.co;2-g;
RA Cadinouche M.Z., Liversage R.A., Muller W., Tsilfidis C.;
RT "Molecular cloning of the Notophthalmus viridescens radical fringe cDNA and
RT characterization of its expression during forelimb development and adult
RT forelimb regeneration.";
RL Dev. Dyn. 214:259-268(1999).
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 (By similarity). Involved in forelimb
CC development and in adult forelimb regeneration. {ECO:0000250}.
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 the mesanchymal region of the
CC developing limb. Expressed in mesoderm but not in ectoderm with no
CC evident boundary of expression.
CC -!- DEVELOPMENTAL STAGE: First detected in the presumptive limb field. As
CC the limb develops from a limb bud into a cone, a stron homogeneous
CC signal is evident. Strong expression persists as the cone flattens into
CC a palette and digits begin to appear and is down-regulated as limb
CC development advances. At the three digit stage there is a faint
CC mesenchymal expression which disappears at the appearance of the fourth
CC digit.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AF115388; AAD10827.1; -; mRNA.
DR AlphaFoldDB; Q9YHB3; -.
DR SMR; Q9YHB3; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
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 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; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..396
FT /note="Beta-1,3-N-acetylglucosaminyltransferase radical
FT fringe"
FT /id="PRO_0000219189"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..396
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 307
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 185..196
FT /evidence="ECO:0000250"
FT DISULFID 214..277
FT /evidence="ECO:0000250"
FT DISULFID 381..390
FT /evidence="ECO:0000250"
SQ SEQUENCE 396 AA; 45048 MW; 09370E3E44AFC4D4 CRC64;
MNFSCLGLSK ICFLVSVIFC TFLLLFIPKT KTPWRPRTYP QPRPPPLFNA TCGKQFALPG
IEHAQQKLPT HTTDITHFED PGNVEDWRAY ILGRENPDEK HEGPTDNPGE HKSVLASSIN
SSKDALEFED LFIAVKTTRK YHKTRLDLLL QTWISRAKQQ TFIFTDGEDQ DLRQRAGIQV
INTNCSAMHT RQALCCKMAV EYDKFIESER KWFCHVDDDN YVNLFSLRHL LASFSHSQDV
YLGRPSLDHP IEAIERVKSD GSASVRFWFA TGGAGFCISR GLALKMSPWA SMGNFITTAE
LVRLPDDCTI GYIIEGLLGV KMHHTPLFHS HLENLQRLPL QSVLKQVTLS YGGPDNKRNV
VSVGGIFSLE NDPTRFRTVH CLLYPDTHWC PPRKTR
