Q8VHI3 · OFUT2_MOUSE

  • Protein
    GDP-fucose protein O-fucosyltransferase 2
  • Gene
    Pofut2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively (PubMed:20637190).
O-fucosylates members of several protein families including the ADAMTS, the thrombospondin (TSP) and spondin families (PubMed:20637190).
Required for the proper secretion of ADAMTS family members such as ADAMTSL1 and ADAMTS13 (By similarity).
The O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm (PubMed:20637190).

Catalytic activity

Pathway

Protein modification; protein glycosylation.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site53-57GDP-beta-L-fucose (UniProtKB | ChEBI)
Active site54Proton acceptor
Binding site292-294GDP-beta-L-fucose (UniProtKB | ChEBI)
Binding site371GDP-beta-L-fucose (UniProtKB | ChEBI)
Binding site388-389GDP-beta-L-fucose (UniProtKB | ChEBI)
Site396Required for enzyme activity

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular ComponentGolgi apparatus
Molecular Functionfucosyltransferase activity
Molecular Functionpeptide-O-fucosyltransferase activity
Biological Processfucose metabolic process
Biological Processfucosylation
Biological Processmesoderm formation
Biological Processpositive regulation of protein folding
Biological Processprotein O-linked fucosylation
Biological Processregulation of epithelial to mesenchymal transition
Biological Processregulation of gene expression
Biological Processregulation of secretion

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    GDP-fucose protein O-fucosyltransferase 2
  • EC number
  • Alternative names
    • Peptide-O-fucosyltransferase 2 (O-FucT-2)

Gene names

    • Name
      Pofut2

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8VHI3
  • Secondary accessions
    • Q8VEM2
    • Q9CV66

Proteomes

Organism-specific databases

Subcellular Location

Endoplasmic reticulum
Golgi apparatus
Note: Mainly located in the endoplasmic reticulum.

Keywords

Phenotypes & Variants

Disruption phenotype

Null mice embryos die before 10.5 dpc. At the onset of gastrulation at 6.5 dpc, embryos are rounder and the embryonic and extra-embryonic ectoderm appears thickened and disorganized. Expression of NODAL and WNT3 is significantly expanded and/or displaced in the primitive streak as is BMP4 in the extra-embryonic ectoderm. By 7.5 dpc, embryos are unusually dense and shorter characterized by a dumb-bell appearance. There is unrestricted epithelial to mesenchymal transition (EMT) producing an abundance of mesenchymal cells. SNAIL1 expression is expanded and E-cadherin expression decreased. There is distal expansion of the proximal visceral endoderm.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis396Abolishes in vitro enzyme activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 17 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_000001215522-429GDP-fucose protein O-fucosyltransferase 2
Disulfide bond161↔192
Glycosylation189N-linked (GlcNAc...) asparagine
Glycosylation209N-linked (GlcNAc...) asparagine
Glycosylation259N-linked (GlcNAc...) asparagine
Disulfide bond412↔419

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    429
  • Mass (Da)
    49,429
  • Last updated
    2002-03-01 v1
  • Checksum
    0E7AFF5F1CD33560
MAALSVVCLLLAAASWRPVSASGEEFWPGQSAADILSGAASRRRYLLYDVNPPEGFNLRRDVYIRVASLLKTLLKTEEWVLVLPPWGRLYHWQSPDIHQVRIPWSEFFDLPSLNKNIPVIEYEQFIAESGGPFIDQVYVLQGYAEGWKEGTWEEKVDARPCIDPLLYSQDKHEYYRGWFWGYEETRGLNVSCLSVQGSASIVAPVLLKNTSARSVMLDRAENLLHDHYGGREYWDTRRSMVFAKHLRAVGDEFRSQHLNSTDAADKMAPEEDWTKMKVKLGSALGGPYLGVHLRRKDFIWGHREDVPSLEGAVKKIRSLMKTHQLDKVFVATDAIRKEQEELRKLLPEMVRFEPTWEELELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREILGLDPKTTYNRFCGDQEKACEQPTHWKIAY

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1W2P6H4A0A1W2P6H4_MOUSEPofut2170
A0A1W2P7Z1A0A1W2P7Z1_MOUSEPofut2209
A0A1W2P844A0A1W2P844_MOUSEPofut2164

Sequence caution

The sequence BC018194 differs from that shown. Reason: Frameshift

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF455270
EMBL· GenBank· DDBJ
AAL65192.1
EMBL· GenBank· DDBJ
mRNA
BC018194
EMBL· GenBank· DDBJ
-mRNA No translation available.
AK009301
EMBL· GenBank· DDBJ
BAB26202.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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