LFNG_DANRE
ID LFNG_DANRE Reviewed; 374 AA.
AC Q8JHF2; Q9DEV1;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 118.
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 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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=11702199; DOI=10.1007/s00427-001-0181-4;
RA Leve C., Gajewski M., Rohr K.B., Tautz D.;
RT "Homologues of c-hairy1 (her9) and lunatic fringe in zebrafish are
RT expressed in the developing central nervous system, but not in the
RT presomitic mesoderm.";
RL Dev. Genes Evol. 211:493-500(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryo;
RX PubMed=11429294; DOI=10.1016/s0925-4773(01)00398-7;
RA Prince V.E., Holley S.A., Bally-Cuif L., Prabhakaran B., Oates A.C.,
RA Ho R.K., Vogt T.F.;
RT "Zebrafish lunatic fringe demarcates segmental boundaries.";
RL Mech. Dev. 105:175-180(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=14518000; DOI=10.1002/dvdy.10375;
RA Appel B., Marasco P., McClung L.E., Latimer A.J.;
RT "Lunatic fringe regulates Delta-Notch induction of hypochord in
RT zebrafish.";
RL Dev. Dyn. 228:281-286(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=16729214; DOI=10.1007/s10126-005-5125-y;
RA Liu J., Sun Y.-H., Wang N., Wang Y.-P., Zhu Z.-Y.;
RT "Upstream regulatory region of zebrafish lunatic fringe: isolation and
RT promoter analysis.";
RL Mar. Biotechnol. 8:357-365(2006).
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. Involved in the correct formation of
CC boundaries in the somites and hindbrain (By similarity). Required for
CC Delta-Notch-mediated induction of hypochord cells at the lateral
CC borders of the midline precursor domain (PubMed:11429294,
CC PubMed:14518000). {ECO:0000250|UniProtKB:O09010,
CC ECO:0000269|PubMed:11429294, ECO:0000269|PubMed:14518000}.
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 -!- TISSUE SPECIFICITY: In the embryo, expressed along the A-P axis of the
CC neural tube, within the lateral plate mesoderm, in the presomitic
CC mesoderm and the somites, in specific rhombomeres of the hindbrain
CC (even-numbered rhombomeres) and in the otic vesicles.
CC {ECO:0000269|PubMed:11429294, ECO:0000269|PubMed:15376327}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and throughout the
CC zygotic stages, with highest expression at the bud stage. No evidence
CC for a cyclic pattern of expression in the presomitic mesoderm during
CC somitogenesis. Expressed weakly at the epiboly stage (4.5 hours)
CC throughout the blastoderm. Expression clears from marginal region and
CC localizes to the epiblast cells of the animal pole. As gastrulation
CC proceeds, expressed in hypoblast cells that migrate towards the animal
CC pole, in the prechordal plate and in forerunner cells. At 90% epiboly,
CC expressed in the neural plate. At the three somite stage (11 hours),
CC expressed in a small cluster of cells within the tailbud region and in
CC future spinal cord. From the 8-14 somite stages, expressed in
CC alternating pre-rhombomeres of the hindbrain, and more broadly in
CC mid- and forebrain. Also expressed weakly in the anterior margins of
CC the formed somites and in the anterior presomitic mesoderm. At the end
CC of somitogenesis (22 hours), expressed strongly in the telencephalon
CC and anterior midbrain, weakly in other parts of the midbrain and
CC variably in the hindbrain. {ECO:0000269|PubMed:11429294,
CC ECO:0000269|PubMed:11702199, ECO:0000269|PubMed:14518000,
CC ECO:0000269|PubMed:16729214}.
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; AY007434; AAG12160.1; -; mRNA.
DR EMBL; AF510992; AAM44059.1; -; mRNA.
DR EMBL; BC044339; AAH44339.1; -; mRNA.
DR RefSeq; NP_571046.1; NM_130971.1.
DR AlphaFoldDB; Q8JHF2; -.
DR SMR; Q8JHF2; -.
DR STRING; 7955.ENSDARP00000031031; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q8JHF2; -.
DR Ensembl; ENSDART00000028673; ENSDARP00000031031; ENSDARG00000037879.
DR GeneID; 30158; -.
DR KEGG; dre:30158; -.
DR CTD; 3955; -.
DR ZFIN; ZDB-GENE-980605-16; lfng.
DR eggNOG; ENOG502QV30; Eukaryota.
DR GeneTree; ENSGT00940000158717; -.
DR HOGENOM; CLU_056611_0_1_1; -.
DR InParanoid; Q8JHF2; -.
DR OMA; SENKMRP; -.
DR OrthoDB; 826272at2759; -.
DR PhylomeDB; Q8JHF2; -.
DR TreeFam; TF324207; -.
DR PRO; PR:Q8JHF2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000037879; Expressed in somite and 55 other tissues.
DR ExpressionAtlas; Q8JHF2; baseline and differential.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR GO; GO:0055016; P:hypochord development; IMP:ZFIN.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:ZFIN.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; 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; Notch signaling pathway; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..374
FT /note="Beta-1,3-N-acetylglucosaminyltransferase lunatic
FT fringe"
FT /id="PRO_0000219180"
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..374
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 80..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 285
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT SITE 83..84
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 163..174
FT /evidence="ECO:0000250"
FT DISULFID 192..255
FT /evidence="ECO:0000250"
FT DISULFID 359..368
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="A -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="L -> LL (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 64..67
FT /note="EQNA -> DQENT (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="I -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="R -> Q (in Ref. 4; AAM44059)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 41882 MW; 082F1FD0705B9A8B CRC64;
MLKTYRGKVV VSLAGATVTC LGFLLFLSQH QRIQADGMQN ESEVGLRSLQ SLGDSETDDG
AQPEQNAKKG FSAYFSKLTR SRREADKPSE APGAATDAPP AEDISADDIF IAVKTTKKFH
RSRLDLLLDT WISRNMRQTY IFTDGEDEEL KKKIGSHAIN TNCSAAHSRQ ALSCKMAVEY
DKFIESGKKW FCHVDDDNYV NTKTLVKLLS NYPHTQDMYI GKPSLDRPIE ATERLGDNKM
RPVNFWFATG GAGFCISRGL ALKMSPWASG GHFMNTAEKI RLPDDCTIGY IIESVLGVSL
TRSSLFHSHL ENLQQVSKSE VHKQITLSYG MFENKRNIIN MKGAFSVEED PSRFKSVHCL
LYPDTPWCPP QVAY
