S7WCF5 · OFUT2_TOXGG

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).

Catalytic activity

Pathway

Protein modification; protein glycosylation.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site237-241GDP-beta-L-fucose (UniProtKB | ChEBI)
Active site238Proton acceptor
Binding site646-648GDP-beta-L-fucose (UniProtKB | ChEBI)
Binding site787-788GDP-beta-L-fucose (UniProtKB | ChEBI)
Site795Essential for catalytic activity

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Molecular Functionpeptide-O-fucosyltransferase activity
Biological Processfucose metabolic process
Biological Processprotein O-linked fucosylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    GDP-fucose protein O-fucosyltransferase 2
  • EC number
  • Alternative names
    • Protein O-fucosyltransferase 2

Gene names

    • Name
      POFUT2
    • ORF names
      TGGT1_273550

Organism names

Accessions

  • Primary accession
    S7WCF5

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-150Cytoplasmic
Transmembrane151-171Helical; Signal-anchor for type II membrane protein
Topological domain172-858Lumenal

Keywords

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).

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004555441-858GDP-fucose protein O-fucosyltransferase 2

Expression

Developmental stage

Expressed in tachyzoites (at protein level).

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region448-510Disordered
Compositional bias460-510Basic and acidic residues
Region819-858Disordered
Compositional bias832-848Basic and acidic residues

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    858
  • Mass (Da)
    95,964
  • Last updated
    2013-10-16 v1
  • Checksum
    B87490ACFEBAAF25
MHCQLGGQARALIFLMFESCRNSWHVSPWSSVPFLPSPCLFFSFSALPFLHPLSQLIACRGSSATWLFPVSSGTLVLRYALAASPPRGTMRPSTNPRTAEEGRPWLIHATQTGPQTASVLSLFPAVNAGFFSACRQHRGGRPPCLLNHRRLLLGLVSVLTVFLSCLPFTNATVSPAALQDVCYAFGNISRKLSSFLVPSRVTCPRGATPLSGVEAQDSLEHPEIPDFRFLVYDVKNGEGFHLQKEVIYRVALVISLLNARSAQQGRMTDVHTAEKAREDRGHPQASHMLCASSSFSHACSARSTFPFFPMWVLVLPPWCRLAHWHFSEETITAMAENSWLKHVRWGTFFDFQDLGERLPVMEYEDFLTYQLMRPDPWGERRQRKEKQTTPVELDVVLSVRFSSTPSSRSLPFCACLSSRASEIADEQAQRDDVCCNVNDLPGCPQIHAALTPQERQRAPAQRGGDPREEIDEQTGEFNEGHNPSGDGEREKRKPGRRSDTSRSRKEIQEEAKVSDTWSGVSLWLAGFCETVRALEMWCASLYIADAPRIADLLWRSVAERPPGAIQTVWLKFGENLLVPWPDVLLDAHLLDMLHVHPKLRQIGDLFINKFLSNRDKTETGKGERASTEGGTEGDENLAKHGYIAAHLRRTDFLYLKRSVPLQRAAAYLVSRMKEHGVFKAFICTDGSEDEKRELRDAVRRVGDAASSSPYTVVFFDLPTVRRLMIKTLEASSHVSDDGSFHDLKAVETPGYSGPNHISLLLHPGITALIEVWIAARAAYFIGTKDSRFSQAIRWERHLMGHPLDSSLEVFCVDSSPDQTGGQAQGKCFATKSHDPPEGRSRSELRRKYWPSLDPSSTL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias460-510Basic and acidic residues
Compositional bias832-848Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAQM03000021
EMBL· GenBank· DDBJ
EPR64539.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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