Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Beta-1,3-N-acetylglucosaminyltransferase manic fringe

Gene

Mfng

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glycosyltransferase involved in the elongation of O-linked ligands to activate Notch signaling. Possesses fucose-specific beta-1,3-N-acetylglucosaminyltransferase activity.

Catalytic activityi

Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.

Cofactori

Mn2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701Substrate
Binding sitei143 – 1431Substrate
Metal bindingi144 – 1441Manganese
Active sitei232 – 23211 Publication
Metal bindingi256 – 2561Manganese

GO - Molecular functioni

GO - Biological processi

  • marginal zone B cell differentiation Source: UniProtKB
  • pattern specification process Source: InterPro
  • positive regulation of Notch signaling pathway Source: MGI
  • positive regulation of protein binding Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.222. 3474.
ReactomeiR-MMU-1912420. Pre-NOTCH Processing in Golgi.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1095404. Mfng.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence analysis
Transmembranei8 – 2720Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini28 – 321294LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321Beta-1,3-N-acetylglucosaminyltransferase manic fringePRO_0000219183Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence analysis
Disulfide bondi110 ↔ 1211 Publication
Disulfide bondi139 ↔ 2021 Publication
Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence analysis
Disulfide bondi306 ↔ 3151 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiO09008.
PaxDbiO09008.
PRIDEiO09008.

Expressioni

Gene expression databases

BgeeiO09008.
ExpressionAtlasiO09008. baseline and differential.
GenevisibleiO09008. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000018313.

Structurei

Secondary structure

1
321
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi53 – 553Combined sources
Beta strandi56 – 616Combined sources
Helixi64 – 663Combined sources
Turni67 – 704Combined sources
Helixi71 – 766Combined sources
Helixi78 – 814Combined sources
Helixi83 – 853Combined sources
Beta strandi86 – 927Combined sources
Helixi95 – 1017Combined sources
Helixi102 – 1043Combined sources
Beta strandi105 – 1073Combined sources
Helixi121 – 13313Combined sources
Beta strandi136 – 1427Combined sources
Beta strandi145 – 1473Combined sources
Helixi149 – 1568Combined sources
Beta strandi166 – 1683Combined sources
Helixi197 – 1993Combined sources
Beta strandi201 – 2044Combined sources
Helixi205 – 21511Combined sources
Turni224 – 2285Combined sources
Helixi231 – 24111Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi256 – 2583Combined sources
Helixi260 – 2623Combined sources
Turni265 – 2673Combined sources
Helixi268 – 2703Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi277 – 2793Combined sources
Beta strandi282 – 2843Combined sources
Turni294 – 2963Combined sources
Helixi301 – 3088Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0AX-ray1.80A45-321[»]
2J0BX-ray2.10A45-321[»]
ProteinModelPortaliO09008.
SMRiO09008. Positions 50-318.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO09008.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II9W. Eukaryota.
ENOG410XS8Y. LUCA.
HOGENOMiHOG000046678.
HOVERGENiHBG007986.
InParanoidiO09008.
KOiK05948.
OMAiCKMAAEL.
OrthoDBiEOG7ZSHTD.
PhylomeDBiO09008.
TreeFamiTF324207.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

O09008-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHCRLFRGMA GALFTLLCVG LLSLRYHSSL SQRMIQGALR LNQRNPGPLE
60 70 80 90 100
LQLGDIFIAV KTTWAFHRSR LDLLLDTWVS RIRQQTFIFT DSPDERLQER
110 120 130 140 150
LGPHLVVTNC SAEHSHPALS CKMAAEFDAF LVSGLRWFCH VDDDNYVNPK
160 170 180 190 200
ALLQLLKTFP QDRDVYVGKP SLNRPIHASE LQSKNRTKLV RFWFATGGAG
210 220 230 240 250
FCINRQLALK MVPWASGSHF VDTSALIRLP DDCTVGYIIE CKLGGRLQPS
260 270 280 290 300
PLFHSHLETL QLLGAAQLPE QVTLSYGVFE GKLNVIKLPG PFSHEEDPSR
310 320
FRSLHCLLYP DTPWCPLLAA P
Length:321
Mass (Da):36,200
Last modified:July 1, 1997 - v1
Checksum:i76EBCEC2314C50CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94349 mRNA. Translation: AAC53260.1.
AF015769 mRNA. Translation: AAB71669.1.
BC010983 mRNA. Translation: AAH10983.1.
CCDSiCCDS27622.1.
RefSeqiNP_032621.1. NM_008595.2.
UniGeneiMm.149235.

Genome annotation databases

EnsembliENSMUST00000018313; ENSMUSP00000018313; ENSMUSG00000018169.
GeneIDi17305.
KEGGimmu:17305.
UCSCiuc007wri.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

manic fringe homolog (mfng)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94349 mRNA. Translation: AAC53260.1.
AF015769 mRNA. Translation: AAB71669.1.
BC010983 mRNA. Translation: AAH10983.1.
CCDSiCCDS27622.1.
RefSeqiNP_032621.1. NM_008595.2.
UniGeneiMm.149235.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0AX-ray1.80A45-321[»]
2J0BX-ray2.10A45-321[»]
ProteinModelPortaliO09008.
SMRiO09008. Positions 50-318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000018313.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Proteomic databases

EPDiO09008.
PaxDbiO09008.
PRIDEiO09008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018313; ENSMUSP00000018313; ENSMUSG00000018169.
GeneIDi17305.
KEGGimmu:17305.
UCSCiuc007wri.1. mouse.

Organism-specific databases

CTDi4242.
MGIiMGI:1095404. Mfng.

Phylogenomic databases

eggNOGiENOG410II9W. Eukaryota.
ENOG410XS8Y. LUCA.
HOGENOMiHOG000046678.
HOVERGENiHBG007986.
InParanoidiO09008.
KOiK05948.
OMAiCKMAAEL.
OrthoDBiEOG7ZSHTD.
PhylomeDBiO09008.
TreeFamiTF324207.

Enzyme and pathway databases

BRENDAi2.4.1.222. 3474.
ReactomeiR-MMU-1912420. Pre-NOTCH Processing in Golgi.

Miscellaneous databases

EvolutionaryTraceiO09008.
PROiO09008.
SOURCEiSearch...

Gene expression databases

BgeeiO09008.
ExpressionAtlasiO09008. baseline and differential.
GenevisibleiO09008. MM.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A family of mammalian Fringe genes implicated in boundary determination and the Notch pathway."
    Johnston S.H., Rauskolb C., Wilson R., Prabhakaran B., Irvine K.D., Vogt T.F.
    Development 124:2245-2254(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Fringe boundaries coincide with Notch-dependent patterning centres in mammals and alter Notch-dependent development in Drosophila."
    Cohen B., Bashirullah A., Dagnino L., Campbell C., Fisher W.W., Leow C.C., Whiting E., Ryan D., Zinyk D., Boulianne G., Hui C.-C., Gallie B., Phillips R.A., Lipshitz H.D., Egan S.E.
    Nat. Genet. 16:283-288(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Structural insights into the Notch-modifying glycosyltransferase Fringe."
    Jinek M., Chen Y.W., Clausen H., Cohen S.M., Conti E.
    Nat. Struct. Mol. Biol. 13:945-946(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 45-321 IN COMPLEX WITH UDP, COFACTOR, MANGANESE-BINDING SITES, SUBSTRATE-BINDING SITES, ACTIVE SITE, DISULFIDE BONDS.

Entry informationi

Entry nameiMFNG_MOUSE
AccessioniPrimary (citable) accession number: O09008
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: July 1, 1997
Last modified: June 8, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.