MFNG_DANRE
ID MFNG_DANRE Reviewed; 360 AA.
AC Q5YB40; A0JMI3; Q1RLZ4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Beta-1,3-N-acetylglucosaminyltransferase manic fringe;
DE EC=2.4.1.222 {ECO:0000250|UniProtKB:O00587};
DE AltName: Full=O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase;
GN Name=mfng {ECO:0000312|EMBL:AAT46070.1,
GN ECO:0000312|ZFIN:ZDB-GENE-041130-1};
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:AAT46070.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
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:0000312|EMBL:AAI15219.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:O00587}.
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:O00587};
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:O00587};
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: First detected at the 12-somite stage. From the
CC 20-somite stage, expressed in the otic vesicle.
CC {ECO:0000269|PubMed:15376327}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000255}.
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DR EMBL; AY608926; AAT46070.1; -; mRNA.
DR EMBL; BC115218; AAI15219.1; -; mRNA.
DR EMBL; BC125890; AAI25891.1; -; mRNA.
DR RefSeq; NP_001007789.1; NM_001007788.1.
DR AlphaFoldDB; Q5YB40; -.
DR SMR; Q5YB40; -.
DR STRING; 7955.ENSDARP00000063007; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q5YB40; -.
DR Ensembl; ENSDART00000063008; ENSDARP00000063007; ENSDARG00000042925.
DR GeneID; 493633; -.
DR KEGG; dre:493633; -.
DR CTD; 4242; -.
DR ZFIN; ZDB-GENE-041130-1; mfng.
DR eggNOG; ENOG502QUF4; Eukaryota.
DR GeneTree; ENSGT00940000159564; -.
DR HOGENOM; CLU_056611_0_1_1; -.
DR InParanoid; Q5YB40; -.
DR OMA; SHFVDTS; -.
DR OrthoDB; 826272at2759; -.
DR PhylomeDB; Q5YB40; -.
DR TreeFam; TF324207; -.
DR PRO; PR:Q5YB40; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 22.
DR Bgee; ENSDARG00000042925; Expressed in spleen and 16 other tissues.
DR ExpressionAtlas; Q5YB40; baseline.
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: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; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..360
FT /note="Beta-1,3-N-acetylglucosaminyltransferase manic
FT fringe"
FT /id="PRO_0000250422"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..360
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 51..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 261
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 139..150
FT /evidence="ECO:0000250"
FT DISULFID 168..231
FT /evidence="ECO:0000250"
FT DISULFID 335..344
FT /evidence="ECO:0000250"
FT CONFLICT 40
FT /note="D -> N (in Ref. 2; AAI15219)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="A -> V (in Ref. 2; AAI15219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 40964 MW; 8A78F3524D7ED093 CRC64;
MILRRLFHVL PAFAFTLFIL VLLDLQLRTR SDQKPQNAHD GHQRTTFISE TTAENQHRDG
AHEKEKAEGQ KWTEVRSTPP LELSDIFIAV KTTGRFHKSR LALLLETWIS ETKEHTYIFT
DSPDADISSE GFNVVVTNCS PEHSHQALSC KMAAEYDYFM ASYKKWLCHV DDDNYLNPGA
LLSLLMAFPA DGDIYVGKPS LDRPMRAQEL LEGNKTRDVH FWFATGGAGF CLSRNLAERM
APWASGPRFE QTSAVIMLPD DCTVGFIVER RLGISMIHSN MFHSHLENLL LLSPSDIPKQ
VTLSYGWFES KMNSVELKGV FTKDEDPSRF RTVHCLLYPT TSWCPVALKS ALSWNQHVMH
