LFNG_CHICK
ID LFNG_CHICK Reviewed; 363 AA.
AC O12971; O13130;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe;
DE EC=2.4.1.222;
DE AltName: Full=O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase;
GN Name=LFNG;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Leghorn;
RX PubMed=9175788; DOI=10.1006/bbrc.1997.6652;
RA Sakamoto K., Yan L., Imai H., Takagi M., Nabeshima Y., Takeda S.,
RA Katsube K.;
RT "Identification of a chick homologue of Fringe and C-Fringe 1: involvement
RT in the neurogenesis and the somitogenesis.";
RL Biochem. Biophys. Res. Commun. 234:754-759(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. Essential mediator of somite segmentation
CC and patterning. {ECO:0000250|UniProtKB:O09010}.
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:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: At stage 13 it is detected in the presomitic
CC mesoderm, transiently observed before segmentation, and in the rostral
CC part of the neural tube. Up-regulated in the neural tube, the retina
CC and the otic vesicle from this stage on. At stage 17 a distinct stripe
CC pattern was clear in the hindbrain and the spinal chord. Also found in
CC the neuroepithelium of the midbrain and forebrain. The expression was
CC down-regulated with the termination of neurogenesis at stage 36.
CC -!- PTM: A soluble form may be derived from the membrane form by
CC proteolytic processing. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; U91849; AAC60099.1; -; mRNA.
DR EMBL; U97157; AAB60860.1; -; mRNA.
DR PIR; JC5536; JC5536.
DR RefSeq; NP_990279.1; NM_204948.1.
DR AlphaFoldDB; O12971; -.
DR SMR; O12971; -.
DR STRING; 9031.ENSGALP00000006798; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; O12971; -.
DR Ensembl; ENSGALT00000073543; ENSGALP00000045107; ENSGALG00000038515.
DR GeneID; 395790; -.
DR KEGG; gga:395790; -.
DR CTD; 3955; -.
DR VEuPathDB; HostDB:geneid_395790; -.
DR eggNOG; ENOG502QV30; Eukaryota.
DR GeneTree; ENSGT00940000158717; -.
DR InParanoid; O12971; -.
DR OMA; SENKMRP; -.
DR OrthoDB; 826272at2759; -.
DR PhylomeDB; O12971; -.
DR PRO; PR:O12971; -.
DR Proteomes; UP000000539; Chromosome 14.
DR Bgee; ENSGALG00000038515; Expressed in lung and 10 other tissues.
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:0007386; P:compartment pattern specification; IEA:Ensembl.
DR GO; GO:0002315; P:marginal zone B cell differentiation; IEA:Ensembl.
DR GO; GO:1902367; P:negative regulation of Notch signaling pathway involved in somitogenesis; IEA:Ensembl.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0014807; P:regulation of somitogenesis; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR GO; GO:0030217; P:T cell differentiation; IEA:Ensembl.
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; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..363
FT /note="Beta-1,3-N-acetylglucosaminyltransferase lunatic
FT fringe"
FT /id="PRO_0000219179"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..363
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 274
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT SITE 77..78
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 152..163
FT /evidence="ECO:0000250"
FT DISULFID 181..244
FT /evidence="ECO:0000250"
FT DISULFID 348..357
FT /evidence="ECO:0000250"
FT CONFLICT 161
FT /note="L -> C (in Ref. 2; AAB60860)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="E -> Q (in Ref. 2; AAB60860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40658 MW; 433579BDA394F999 CRC64;
MLKSCGRKLL LSLVGSMFTC LLVLMVEPPG RPGLARGEAG GAQRALQSLG AARAAGQGAP
GLRSFADYFG RLSRARRELP AAPPSPPRPP AEDITPRDVF IAVKTTKKFH KARLELLLDT
WISRNRDMTF IFTDGEDEEL KKQARNVINT NCSAAHSRQA LSCKMAVEYD KFIESGRKWF
CHVDDDNYVN VRTLVKLLSS YPHTQDIYIG KPSLDRPIQA TERISENKMH PVHFWFATGG
AGFCISRGLA LKMSPWASGG HFMSTAEKIR LPDDCTIGYI IESVLGVKLI RSNLFHSHLE
NLHQVPKTEI HKQVTLSYGM FENKRNSIHM KGAFSVEEDP SRFRSVHCLL YPDTPWCPSN
VVY
