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Protein

Beta-1,3-N-acetylglucosaminyltransferase radical fringe

Gene

rfng

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules.

Catalytic activityi

Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101SubstrateBy similarity
Binding sitei183 – 1831SubstrateBy similarity
Metal bindingi184 – 1841ManganeseBy similarity
Active sitei272 – 2721By similarity
Metal bindingi296 – 2961ManganeseBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-N-acetylglucosaminyltransferase radical fringe (EC:2.4.1.222)
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene namesi
Name:rfng
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-864975. rfng.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence analysis
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini26 – 340315LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Beta-1,3-N-acetylglucosaminyltransferase radical fringePRO_0000219190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence analysis
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence analysis
Disulfide bondi150 ↔ 161By similarity
Disulfide bondi179 ↔ 242By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP79949.
SMRiP79949. Positions 91-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG007986.
KOiK05948.

Family and domain databases

InterProiIPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P79949-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKITYVGLIK VCFLVFLLLC ATVLLNISWR QRDSSQSLQH CNSTCSAKYL
60 70 80 90 100
ETKLKEAHLT GRHKKWETYR LDAKPTSATG QGHQHFAKEP LQIKDLFIAV
110 120 130 140 150
KTTKKYHGNR LNLLMQTWIS RAKEQTFIFT DWEDQELRQK AGDQMVNTNC
160 170 180 190 200
SAVHTRQALC CKMAVEYDKF VLSDKKWFCH LDDDNYLNLH ALLDLLSTFS
210 220 230 240 250
HSTDVYVGRP SLDHPVETVD RMKGDGSGSL KFWFATGGAG FCISRGLALK
260 270 280 290 300
MSPWASMGNF ISTAEKVRLP DDCTIGYIIE GMLDVKMQHS NLFHSHLEHL
310 320 330 340
QRLPTESLLK QVTLSYGGPD NKWNVVRVNG AFSLAEDPTR
Length:340
Mass (Da):38,679
Last modified:May 1, 1997 - v1
Checksum:iDF6C8BEAAAFB6715
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77641 mRNA. Translation: AAB19226.1.
RefSeqiNP_001080939.1. NM_001087470.1.
UniGeneiXl.83.

Genome annotation databases

GeneIDi394282.
KEGGixla:394282.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77641 mRNA. Translation: AAB19226.1.
RefSeqiNP_001080939.1. NM_001087470.1.
UniGeneiXl.83.

3D structure databases

ProteinModelPortaliP79949.
SMRiP79949. Positions 91-340.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi394282.
KEGGixla:394282.

Organism-specific databases

CTDi5986.
XenbaseiXB-GENE-864975. rfng.

Phylogenomic databases

HOVERGENiHBG007986.
KOiK05948.

Family and domain databases

InterProiIPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRFNG_XENLA
AccessioniPrimary (citable) accession number: P79949
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: May 1, 1997
Last modified: May 11, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.