RFNG_DANRE
ID RFNG_DANRE Reviewed; 362 AA.
AC Q6KFX9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 {ECO:0000312|EMBL:AAQ08017.1,
GN ECO:0000312|ZFIN:ZDB-GENE-030131-5418};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAQ08017.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:15376327};
RX PubMed=15376327; DOI=10.1002/dvdy.20155;
RA Qiu X., Xu H., Haddon C., Lewis J., Jiang Y.-J.;
RT "Sequence and embryonic expression of three zebrafish fringe genes: lunatic
RT fringe, radical fringe, and manic fringe.";
RL Dev. Dyn. 231:621-630(2004).
RN [2] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15068793; DOI=10.1016/s1534-5807(04)00097-8;
RA Cheng Y.-C., Amoyel M., Qiu X., Jiang Y.-J., Xu Q., Wilkinson D.G.;
RT "Notch activation regulates the segregation and differentiation of
RT rhombomere boundary cells in the zebrafish hindbrain.";
RL Dev. Cell 6:539-550(2004).
RN [3] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15659486; DOI=10.1242/dev.01616;
RA Amoyel M., Cheng Y.-C., Jiang Y.-J., Wilkinson D.G.;
RT "Wnt1 regulates neurogenesis and mediates lateral inhibition of boundary
RT cell specification in the zebrafish hindbrain.";
RL Development 132:775-785(2005).
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). Regulates neurogenesis in
CC the hindbrain; involved in boundary cell specification via Notch-
CC mediated activation of wnt1 expression (PubMed:15068793,
CC PubMed:15659486). {ECO:0000250|UniProtKB:O09009,
CC ECO:0000269|PubMed:15068793, ECO:0000269|PubMed:15659486}.
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 Evidence={ECO:0000250|UniProtKB:Q9Y644};
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 Evidence={ECO:0000250|UniProtKB:Q9Y644};
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 -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. At the
CC tailbud stage, expressed weakly in the adaxial cells and the future
CC brain. From the 3-somite stage, strong expression in the adaxial cells
CC and weak expression in the somites and tailbud. During somitogenesis,
CC expression in the brain is gradually restricted to and up-regulated in
CC the tectum and rhombomere boundary cells. {ECO:0000269|PubMed:15068793,
CC ECO:0000269|PubMed:15376327, ECO:0000269|PubMed:15659486}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000255}.
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DR EMBL; AF510993; AAQ08017.1; -; mRNA.
DR AlphaFoldDB; Q6KFX9; -.
DR SMR; Q6KFX9; -.
DR STRING; 7955.ENSDARP00000022107; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q6KFX9; -.
DR ZFIN; ZDB-GENE-030131-5418; rfng.
DR eggNOG; ENOG502QV30; Eukaryota.
DR InParanoid; Q6KFX9; -.
DR PhylomeDB; Q6KFX9; -.
DR PRO; PR:Q6KFX9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0035284; P:brain segmentation; IMP:ZFIN.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0021592; P:fourth ventricle development; IMP:ZFIN.
DR GO; GO:0030902; P:hindbrain development; IMP:ZFIN.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0021654; P:rhombomere boundary formation; IMP:ZFIN.
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; Notch signaling pathway; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..362
FT /note="Beta-1,3-N-acetylglucosaminyltransferase radical
FT fringe"
FT /id="PRO_0000250423"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..362
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 33..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 273
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..162
FT /evidence="ECO:0000250"
FT DISULFID 180..243
FT /evidence="ECO:0000250"
FT DISULFID 347..356
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 41019 MW; A6CDCBFBC84C69C7 CRC64;
MHLSHVASNK TCFLLSLAFC ALLVLLIPSL QPPQRQADLP QPRPHAKPAK HPLKNSLYRP
NEDTRGGGFT QTPPPDNLEK MDDLNSHYRD FLDLRDIFIA VKTTRKYHKS RLQLLSQTWV
SRAKEQTFIF TDGEDKELRL KAGLNIINTN CSAAHTRQAL CCKMSVEYDK FIESQKKWFC
HVDDDNYVIL PSLLELLSSY SHTQDVYLGR PSLDHPIEAA ERVKSDGSVS VKFWFATGGA
GFCISRGLAL KMSPWASLGN FITTAEKIRL PDDCTIGYII EALLEVPLTH TGLFHSHLEN
LQRLPAENIL RQVTLSYGGF ENRRNVVSVG GAFSLAEDPT RFKTVHCKLY PDTEWCPRKT
RH
