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O09008 (MFNG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Beta-1,3-N-acetylglucosaminyltransferase manic fringe
EC=2.4.1.222
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene names
Name:Mfng
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 31 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 321321Beta-1,3-N-acetylglucosaminyltransferase manic fringe
PRO_0000219183

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2720Helical; Signal-anchor for type II membrane protein; Potential
Topological domain28 – 321294Lumenal Potential

Amino acid modifications

Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential

Secondary structure

1 ....................................................... 321
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O09008 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 76EBCEC2314C50CD

FASTA32136,200
        10         20         30         40         50         60 
MHCRLFRGMA GALFTLLCVG LLSLRYHSSL SQRMIQGALR LNQRNPGPLE LQLGDIFIAV 

        70         80         90        100        110        120 
KTTWAFHRSR LDLLLDTWVS RIRQQTFIFT DSPDERLQER LGPHLVVTNC SAEHSHPALS 

       130        140        150        160        170        180 
CKMAAEFDAF LVSGLRWFCH VDDDNYVNPK ALLQLLKTFP QDRDVYVGKP SLNRPIHASE 

       190        200        210        220        230        240 
LQSKNRTKLV RFWFATGGAG FCINRQLALK MVPWASGSHF VDTSALIRLP DDCTVGYIIE 

       250        260        270        280        290        300 
CKLGGRLQPS PLFHSHLETL QLLGAAQLPE QVTLSYGVFE GKLNVIKLPG PFSHEEDPSR 

       310        320 
FRSLHCLLYP DTPWCPLLAA P

« Hide

References

« Hide 'large scale' references
[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: 9187150] [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: 9207795] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

manic fringe homolog (mfng)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U94349 mRNA. Translation: AAC53260.1.
AF015769 mRNA. Translation: AAB71669.1.
BC010983 mRNA. Translation: AAH10983.1.
IPIIPI00113736.
RefSeqNP_032621.1. NM_008595.2.
UniGeneMm.149235.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0AX-ray1.80A45-321[»]
2J0BX-ray2.10A45-321[»]
ProteinModelPortalO09008.
SMRO09008. Positions 50-318.
ModBaseSearch...

Protein-protein interaction databases

STRINGO09008.

Protein family/group databases

CAZyGT31. Glycosyltransferase Family 31.

Proteomic databases

PRIDEO09008.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018313; ENSMUSP00000018313; ENSMUSG00000018169.
GeneID17305.
KEGGmmu:17305.

Organism-specific databases

CTD4242.
MGIMGI:1095404. Mfng.

Phylogenomic databases

eggNOGroNOG14994.
HOGENOMHBG714286.
HOVERGENHBG007986.
InParanoidO09008.
OMALRWFCHV.
OrthoDBEOG4GQQ57.
PhylomeDBO09008.

Gene expression databases

ArrayExpressO09008.
BgeeO09008.
GenevestigatorO09008.
GermOnlineENSMUSG00000018169. Mus musculus.

Family and domain databases

InterProIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
KOK05948.
PfamPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
ProtoNetSearch...

Other

NextBio291848.
SOURCESearch...

Entry information

Entry nameMFNG_MOUSE
AccessionPrimary (citable) accession number: O09008
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: July 1, 1997
Last modified: November 16, 2011
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents