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Protein

Beta-1,3-N-acetylglucosaminyltransferase manic fringe

Gene

MFNG

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed-Annotation score: -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. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1.By similarity

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)DescriptionActionsGraphical viewLength
Binding sitei70SubstrateBy similarity1
Binding sitei143SubstrateBy similarity1
Metal bindingi144ManganeseBy similarity1
Active sitei232By similarity1
Metal bindingi256ManganeseBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, Glycosyltransferase, Transferase
LigandManganese, Metal-binding

Protein family/group databases

CAZyiGT31 Glycosyltransferase Family 31

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-N-acetylglucosaminyltransferase manic fringe (EC:2.4.1.222)
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene namesi
Name:MFNG
OrganismiPan troglodytes (Chimpanzee)
Taxonomic identifieri9598 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
Proteomesi
  • UP000002277 Componenti: Chromosome 22

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 7CytoplasmicSequence analysis7
Transmembranei8 – 27Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini28 – 321LumenalSequence analysisAdd BLAST294

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002191841 – 321Beta-1,3-N-acetylglucosaminyltransferase manic fringeAdd BLAST321

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi109N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi110 ↔ 121By similarity
Disulfide bondi139 ↔ 202By similarity
Glycosylationi185N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi306 ↔ 315By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5IS64
SMRiQ5IS64
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000009913
HOVERGENiHBG007986
InParanoidiQ5IS64
KOiK05948

Family and domain databases

InterProiView protein in InterPro
IPR017374 Fringe
IPR003378 Fringe-like
PfamiView protein in Pfam
PF02434 Fringe, 1 hit
PIRSFiPIRSF038073 B-acetylgalactosaminyltfrase, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.iShow all

Q5IS64-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQCRLPRGLA GALLTLLCMG LLCLRYHLNL SPQRVQETPE LRQPNPGPPE
60 70 80 90 100
LQLHDVFIAV KTTRAFHRLR LELLLDTWVS RTREQTFVFT DSPDKGLQER
110 120 130 140 150
LGSHLVVTNC SAEHSHPALS CKMAAEFDTF LASGLRWFCH VDDDNYVNPR
160 170 180 190 200
ALLQLLRAFP LAHDVYVGRP SLNRPIHASE PQPHNRTRLV QFWFATGGAG
210 220 230 240 250
FCINRRLALK MAPWASGSRF MDTSALIRLP DDCTMGYIIE CKLGGRLQPS
260 270 280 290 300
PLFHSHLETL QLLRTAQLPE QVTLSYGVFE GKLNVIKLQG PFSPEEDPSR
310 320
FRSLHCLLYP DTPWCPQLGA R
Length:321
Mass (Da):36,353
Last modified:February 15, 2005 - v1
Checksum:i62A68643836EE1DD
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H2R9C9H2R9C9_PANTR
Beta-1,3-N-acetylglucosaminyltransf...
MFNG CK820_G0027689
307Annotation score:
A0A2I3TMG4A0A2I3TMG4_PANTR
Beta-1,3-N-acetylglucosaminyltransf...
MFNG
130Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY665264 mRNA Translation: AAV74302.1
RefSeqiNP_001012433.1, NM_001012431.1
XP_016794235.1, XM_016938746.1
UniGeneiPtr.6369

Genome annotation databases

EnsembliENSPTRT00000095465; ENSPTRP00000071868; ENSPTRG00000014335
GeneIDi458811
KEGGiptr:458811

Similar proteinsi

Entry informationi

Entry nameiMFNG_PANTR
AccessioniPrimary (citable) accession number: Q5IS64
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: February 15, 2005
Last modified: March 28, 2018
This is version 67 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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