GDP-fucose protein O-fucosyltransferase 2

POFUT2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4AP5, 4AP6
Identifiers
Aliases	POFUT2, C21orf80, FUT13, protein O-fucosyltransferase 2
External IDs	OMIM: 610249; MGI: 1916863; HomoloGene: 12724; GeneCards: POFUT2; OMA:POFUT2 - orthologs
Gene location (Human) Chr. Chromosome 21 (human)[1] Band 21q22.3 Start 45,263,928 bp[1] End 45,287,898 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10|10 C1 Start 77,095,052 bp[2] End 77,105,409 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube stromal cell of endometrium anterior pituitary right lobe of thyroid gland canal of the cervix left lobe of thyroid gland left ovary sural nerve pancreatic ductal cell right ovary Top expressed in external carotid artery internal carotid artery fossa condyle vas deferens Gonadal ridge human fetus molar body of femur umbilical cord More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity fucosyltransferase activity glycosyltransferase activity peptide-O-fucosyltransferase activity Cellular component Golgi apparatus endoplasmic reticulum endoplasmic reticulum membrane Biological process regulation of gene expression fucose metabolic process protein glycosylation regulation of epithelial to mesenchymal transition mesoderm formation regulation of secretion protein O-linked fucosylation fucosylation carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23275 80294 Ensembl ENSG00000186866 ENSMUSG00000020260 UniProt Q9Y2G5 Q8VHI3 RefSeq (mRNA) NM_015227 NM_133634 NM_133635 NM_030262 RefSeq (protein) NP_056042 NP_598368 NP_084538 Location (UCSC) Chr 21: 45.26 – 45.29 Mb Chr 10: 77.1 – 77.11 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

GDP-fucose protein O-fucosyltransferase 2 (POFUT2) is an enzyme responsible for adding fucose sugars in O linkage to serine or threonine residues in Thrombospondin repeats.[5] The protein is an inverting glycosyltransferase, which means that the enzyme uses GDP-β-L-fucose as a donor substrate and transfers the fucose in O linkage to the protein producing fucose-α-O-serine/threonine.

Almost all glycosyltransferases reside in the Golgi apparatus. However, POFUT2 as well as the related enzyme POFUT1 have recently been shown to reside in the endoplasmic reticulum.

The malaria parasite Plasmodium falciparum requires POFUT2 for efficient transmission to mosquitoes and infection of human liver cells.[6]

See also

• Peptide-O-fucosyltransferase

References

1. GRCh38: Ensembl release 89: ENSG00000186866 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020260 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. GDP-fucose protein O-fucosyltransferase 2, The Universal Protein Resource
6. Lopaticki S, Yang AS, John A, Scott NE, Lingford JP, O'Neill MT, et al. (September 2017). "Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts". Nature Communications. 8 (1): 561. Bibcode:2017NatCo...8..561L. doi:10.1038/s41467-017-00571-y. PMC 5601480. PMID 28916755.

External links

• POFUT2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)