Q8VHI3 · OFUT2_MOUSE
- ProteinGDP-fucose protein O-fucosyltransferase 2
- GenePofut2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids429 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-L-seryl-[protein] + GDP + H+This reaction proceeds in the forward direction.
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 53-57 | GDP-beta-L-fucose (UniProtKB | ChEBI) | ||||
Sequence: PEGFN | ||||||
Active site | 54 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 292-294 | GDP-beta-L-fucose (UniProtKB | ChEBI) | ||||
Sequence: HLR | ||||||
Binding site | 371 | GDP-beta-L-fucose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 388-389 | GDP-beta-L-fucose (UniProtKB | ChEBI) | ||||
Sequence: TF | ||||||
Site | 396 | Required for enzyme activity | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | Golgi apparatus | |
Molecular Function | fucosyltransferase activity | |
Molecular Function | peptide-O-fucosyltransferase activity | |
Biological Process | fucose metabolic process | |
Biological Process | fucosylation | |
Biological Process | mesoderm formation | |
Biological Process | positive regulation of protein folding | |
Biological Process | protein O-linked fucosylation | |
Biological Process | regulation of epithelial to mesenchymal transition | |
Biological Process | regulation of gene expression | |
Biological Process | regulation of secretion |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGDP-fucose protein O-fucosyltransferase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8VHI3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Mainly located in the endoplasmic reticulum.
Keywords
- Cellular component
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 396 | Abolishes in vitro enzyme activity. | ||||
Sequence: E → A |
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.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MAALSVVCLLLAAASWRPVSA | ||||||
Chain | PRO_0000012155 | 22-429 | GDP-fucose protein O-fucosyltransferase 2 | |||
Sequence: SGEEFWPGQSAADILSGAASRRRYLLYDVNPPEGFNLRRDVYIRVASLLKTLLKTEEWVLVLPPWGRLYHWQSPDIHQVRIPWSEFFDLPSLNKNIPVIEYEQFIAESGGPFIDQVYVLQGYAEGWKEGTWEEKVDARPCIDPLLYSQDKHEYYRGWFWGYEETRGLNVSCLSVQGSASIVAPVLLKNTSARSVMLDRAENLLHDHYGGREYWDTRRSMVFAKHLRAVGDEFRSQHLNSTDAADKMAPEEDWTKMKVKLGSALGGPYLGVHLRRKDFIWGHREDVPSLEGAVKKIRSLMKTHQLDKVFVATDAIRKEQEELRKLLPEMVRFEPTWEELELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREILGLDPKTTYNRFCGDQEKACEQPTHWKIAY | ||||||
Disulfide bond | 161↔192 | |||||
Sequence: CIDPLLYSQDKHEYYRGWFWGYEETRGLNVSC | ||||||
Glycosylation | 189 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 209 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 259 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 412↔419 | |||||
Sequence: CGDQEKAC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length429
- Mass (Da)49,429
- Last updated2002-03-01 v1
- Checksum0E7AFF5F1CD33560
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1W2P6H4 | A0A1W2P6H4_MOUSE | Pofut2 | 170 | ||
A0A1W2P7Z1 | A0A1W2P7Z1_MOUSE | Pofut2 | 209 | ||
A0A1W2P844 | A0A1W2P844_MOUSE | Pofut2 | 164 |
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |