RFNG_CHICK
ID RFNG_CHICK Reviewed; 372 AA.
AC O12972; O12970;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 126.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Limb;
RX PubMed=9121551; DOI=10.1038/386360a0;
RA Rodriguez-Esteban C., Schwabe J.W.R., De La Pena J., Foys B., Eshelman B.,
RA Izpisua-Belmonte J.-C.;
RT "Radical fringe positions the apical ectodermal ridge at the dorsoventral
RT boundary of the vertebrate limb.";
RL Nature 386:360-366(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9121552; DOI=10.1038/386366a0;
RA Laufer E., Dahn R., Orozco O.E., Yeo C.-Y., Pisenti J., Henrique D.,
RA Abbott U.K., Fallon J.F., Tabin C.;
RT "Expression of Radical fringe in limb-bud ectoderm regulates apical
RT ectodermal ridge formation.";
RL Nature 386:366-373(1997).
RN [3]
RP ERRATUM OF PUBMED:9121552.
RA Laufer E., Dahn R., Orozco O.E., Yeo C.-Y., Pisenti J., Henrique D.,
RA Abbott U.K., Fallon J.F., Tabin C.;
RL Nature 388:908-908(1997).
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). Plays an important role in
CC limb outgrowth, it directs the formation and positioning of the apical
CC ectodermal ridge (AER), one of the key organizer centers of vertebrate
CC limb development (PubMed:9121551, PubMed:9121552).
CC {ECO:0000250|UniProtKB:O09009, ECO:0000269|PubMed:9121551,
CC ECO:0000269|PubMed:9121552}.
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 -!- DEVELOPMENTAL STAGE: Detected at stage 15 in the presumptive dorsal-
CC limb ectoderm. At stages 16-18 expression is restricted to the dorsal
CC side with higher concentration at the dorsoventral boundary and later
CC in the AER. Expression remains restricted to the dorsal ectoderm and
CC the AER until stages 22-24 when it starts to fade in the dorsal
CC ectoderm, but remains in the AER until the last stage examined (27).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U82088; AAC60107.1; -; mRNA.
DR EMBL; U91850; AAC60100.1; -; mRNA.
DR RefSeq; NP_990278.1; NM_204947.1.
DR AlphaFoldDB; O12972; -.
DR SMR; O12972; -.
DR STRING; 9031.ENSGALP00000004473; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; O12972; -.
DR GeneID; 395789; -.
DR KEGG; gga:395789; -.
DR CTD; 5986; -.
DR VEuPathDB; HostDB:geneid_395789; -.
DR eggNOG; ENOG502QV30; Eukaryota.
DR HOGENOM; CLU_056611_0_1_1; -.
DR InParanoid; O12972; -.
DR OrthoDB; 826272at2759; -.
DR PhylomeDB; O12972; -.
DR PRO; PR:O12972; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
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 GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007389; P:pattern specification process; IEA:InterPro.
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..372
FT /note="Beta-1,3-N-acetylglucosaminyltransferase radical
FT fringe"
FT /id="PRO_0000219188"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..372
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 30..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..49
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 283
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..171
FT /evidence="ECO:0000250"
FT DISULFID 189..253
FT /evidence="ECO:0000250"
FT DISULFID 357..366
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="N -> S (in Ref. 2; AAC60100)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="T -> A (in Ref. 2; AAC60100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 40962 MW; 84CB7B74A4B81C6D CRC64;
MNSSCLGLRR TCFLLSVTAA AVLLLLLPRG QPPAAPRRRP PPAGPSRPSP KREARPAGSD
VPGDRGGGSG AAGGGRGVAG SPWPSRRVRM GPPGGSAKES LELKDIFIAV KTTRKYHKTR
LELLFQTWIS RARGQTFIFT DWEDRELRLK AGDHMINTNC SAVHTRQALC CKMSVEYDKF
LESGQKWFCH VDDDNYVNPR TLLRLLSAFS PSQDVYVGRP SLDHPIEAAD HVQSDGSKTS
VKFWFATGGA GFCISRGLAL KMSPWASLGN FISTAERVRL PDDCTIGYII EGLLEVKLLH
SPLFHSHLEN LQRLQGESVL QQVTLSYGDP ENKHNVVSVG GVFGLQQDPT RFKSVHCLLY
PDTIWCPNKK MS
