S7WCF5 · OFUT2_TOXGG
- ProteinGDP-fucose protein O-fucosyltransferase 2
- GenePOFUT2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids858 (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:30514763, PubMed:30538131).
O-fucosylates microneme protein MIC2 and may play a role in its stabilization (PubMed:30514763, PubMed:30538131).
Probably by regulating protein O-fucosylation, may play a role in tachyzoite adhesion to and/or invasion of host cells; however, POFUT2 involvement in adhesion/invasion is controversial (PubMed:30514763, PubMed:30538131).
O-fucosylates microneme protein MIC2 and may play a role in its stabilization (PubMed:30514763, PubMed:30538131).
Probably by regulating protein O-fucosylation, may play a role in tachyzoite adhesion to and/or invasion of host cells; however, POFUT2 involvement in adhesion/invasion is controversial (PubMed:30514763, PubMed:30538131).
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 | 237-241 | GDP-beta-L-fucose (UniProtKB | ChEBI) | ||||
Sequence: GEGFH | ||||||
Active site | 238 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 646-648 | GDP-beta-L-fucose (UniProtKB | ChEBI) | ||||
Sequence: HLR | ||||||
Binding site | 787-788 | GDP-beta-L-fucose (UniProtKB | ChEBI) | ||||
Sequence: RF | ||||||
Site | 795 | Essential for catalytic activity | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | peptide-O-fucosyltransferase activity | |
Biological Process | fucose metabolic process | |
Biological Process | protein O-linked fucosylation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGDP-fucose protein O-fucosyltransferase 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Conoidasida > Coccidia > Eucoccidiorida > Eimeriorina > Sarcocystidae > Toxoplasma
Accessions
- Primary accessionS7WCF5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-150 | Cytoplasmic | ||||
Sequence: MHCQLGGQARALIFLMFESCRNSWHVSPWSSVPFLPSPCLFFSFSALPFLHPLSQLIACRGSSATWLFPVSSGTLVLRYALAASPPRGTMRPSTNPRTAEEGRPWLIHATQTGPQTASVLSLFPAVNAGFFSACRQHRGGRPPCLLNHRR | ||||||
Transmembrane | 151-171 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LLLGLVSVLTVFLSCLPFTNA | ||||||
Topological domain | 172-858 | Lumenal | ||||
Sequence: TVSPAALQDVCYAFGNISRKLSSFLVPSRVTCPRGATPLSGVEAQDSLEHPEIPDFRFLVYDVKNGEGFHLQKEVIYRVALVISLLNARSAQQGRMTDVHTAEKAREDRGHPQASHMLCASSSFSHACSARSTFPFFPMWVLVLPPWCRLAHWHFSEETITAMAENSWLKHVRWGTFFDFQDLGERLPVMEYEDFLTYQLMRPDPWGERRQRKEKQTTPVELDVVLSVRFSSTPSSRSLPFCACLSSRASEIADEQAQRDDVCCNVNDLPGCPQIHAALTPQERQRAPAQRGGDPREEIDEQTGEFNEGHNPSGDGEREKRKPGRRSDTSRSRKEIQEEAKVSDTWSGVSLWLAGFCETVRALEMWCASLYIADAPRIADLLWRSVAERPPGAIQTVWLKFGENLLVPWPDVLLDAHLLDMLHVHPKLRQIGDLFINKFLSNRDKTETGKGERASTEGGTEGDENLAKHGYIAAHLRRTDFLYLKRSVPLQRAAAYLVSRMKEHGVFKAFICTDGSEDEKRELRDAVRRVGDAASSSPYTVVFFDLPTVRRLMIKTLEASSHVSDDGSFHDLKAVETPGYSGPNHISLLLHPGITALIEVWIAARAAYFIGTKDSRFSQAIRWERHLMGHPLDSSLEVFCVDSSPDQTGGQAQGKCFATKSHDPPEGRSRSELRRKYWPSLDPSSTL |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Loss of MIC2 O-fucosylation (PubMed:30514763, PubMed:30538131).
Nuclear O-fucosylation is normal (PubMed:30538131).
MIC2 protein levels are decreased by 50 percent. Abnormal MIC2 accumulation in the early/mid-secretory pathway (PubMed:30538131).
The number of plaques caused by tachyzoite infection of human foreskin fibroblasts (HFF) is reduced by 40 percent (PubMed:30538131).
The number of tachyzoites that are attached to or invaded the host HFFs is reduced. Egress from the HFFs is also partially impaired (PubMed:30538131).
However, another study shows that loss of POFUT2 only leads to a small decrease in MIC2 protein levels and has no effect on MIC2 trafficking and interaction with M2AP (PubMed:30514763).
Also, the number of plaques caused by tachyzoite infection of HFFs is reduced by only 20 percent and tachyzoite adhesion to and invasion of HFFs are normal (PubMed:30514763).
Nuclear O-fucosylation is normal (PubMed:30538131).
MIC2 protein levels are decreased by 50 percent. Abnormal MIC2 accumulation in the early/mid-secretory pathway (PubMed:30538131).
The number of plaques caused by tachyzoite infection of human foreskin fibroblasts (HFF) is reduced by 40 percent (PubMed:30538131).
The number of tachyzoites that are attached to or invaded the host HFFs is reduced. Egress from the HFFs is also partially impaired (PubMed:30538131).
However, another study shows that loss of POFUT2 only leads to a small decrease in MIC2 protein levels and has no effect on MIC2 trafficking and interaction with M2AP (PubMed:30514763).
Also, the number of plaques caused by tachyzoite infection of HFFs is reduced by only 20 percent and tachyzoite adhesion to and invasion of HFFs are normal (PubMed:30514763).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000455544 | 1-858 | GDP-fucose protein O-fucosyltransferase 2 | |||
Sequence: MHCQLGGQARALIFLMFESCRNSWHVSPWSSVPFLPSPCLFFSFSALPFLHPLSQLIACRGSSATWLFPVSSGTLVLRYALAASPPRGTMRPSTNPRTAEEGRPWLIHATQTGPQTASVLSLFPAVNAGFFSACRQHRGGRPPCLLNHRRLLLGLVSVLTVFLSCLPFTNATVSPAALQDVCYAFGNISRKLSSFLVPSRVTCPRGATPLSGVEAQDSLEHPEIPDFRFLVYDVKNGEGFHLQKEVIYRVALVISLLNARSAQQGRMTDVHTAEKAREDRGHPQASHMLCASSSFSHACSARSTFPFFPMWVLVLPPWCRLAHWHFSEETITAMAENSWLKHVRWGTFFDFQDLGERLPVMEYEDFLTYQLMRPDPWGERRQRKEKQTTPVELDVVLSVRFSSTPSSRSLPFCACLSSRASEIADEQAQRDDVCCNVNDLPGCPQIHAALTPQERQRAPAQRGGDPREEIDEQTGEFNEGHNPSGDGEREKRKPGRRSDTSRSRKEIQEEAKVSDTWSGVSLWLAGFCETVRALEMWCASLYIADAPRIADLLWRSVAERPPGAIQTVWLKFGENLLVPWPDVLLDAHLLDMLHVHPKLRQIGDLFINKFLSNRDKTETGKGERASTEGGTEGDENLAKHGYIAAHLRRTDFLYLKRSVPLQRAAAYLVSRMKEHGVFKAFICTDGSEDEKRELRDAVRRVGDAASSSPYTVVFFDLPTVRRLMIKTLEASSHVSDDGSFHDLKAVETPGYSGPNHISLLLHPGITALIEVWIAARAAYFIGTKDSRFSQAIRWERHLMGHPLDSSLEVFCVDSSPDQTGGQAQGKCFATKSHDPPEGRSRSELRRKYWPSLDPSSTL |
Expression
Developmental stage
Expressed in tachyzoites (at protein level).
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 448-510 | Disordered | ||||
Sequence: AALTPQERQRAPAQRGGDPREEIDEQTGEFNEGHNPSGDGEREKRKPGRRSDTSRSRKEIQEE | ||||||
Compositional bias | 460-510 | Basic and acidic residues | ||||
Sequence: AQRGGDPREEIDEQTGEFNEGHNPSGDGEREKRKPGRRSDTSRSRKEIQEE | ||||||
Region | 819-858 | Disordered | ||||
Sequence: TGGQAQGKCFATKSHDPPEGRSRSELRRKYWPSLDPSSTL | ||||||
Compositional bias | 832-848 | Basic and acidic residues | ||||
Sequence: SHDPPEGRSRSELRRKY |
Sequence similarities
Belongs to the glycosyltransferase 68 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length858
- Mass (Da)95,964
- Last updated2013-10-16 v1
- ChecksumB87490ACFEBAAF25
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 460-510 | Basic and acidic residues | ||||
Sequence: AQRGGDPREEIDEQTGEFNEGHNPSGDGEREKRKPGRRSDTSRSRKEIQEE | ||||||
Compositional bias | 832-848 | Basic and acidic residues | ||||
Sequence: SHDPPEGRSRSELRRKY |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAQM03000021 EMBL· GenBank· DDBJ | EPR64539.1 EMBL· GenBank· DDBJ | Genomic DNA |