P83337 (OFUT1_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GDP-fucose protein O-fucosyltransferase 1
EC=2.4.1.221

Alternative name(s):
Peptide-O-fucosyltransferase 1
Short name=O-FucT-1

Gene names

Name:

POFUT1

Organism

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	61 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in EGF domains. Plays a crucial role in Notch signaling. Ref.2 Ref.3 Ref.4
Catalytic activity	Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor. Ref.2 Ref.3 Ref.4
Cofactor	Manganese. Other divalent cations increase activity: calcium, cobalt, cadmium, magnesium and nickel. Ref.3 Ref.4
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum By similarity.
Post-translational modification	N-glycosylated. Ref.4
Sequence similarities	Belongs to the glycosyltransferase 68 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Fucose metabolism Notch signaling pathway
Cellular component	Endoplasmic reticulum
Ligand	Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	Notch signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW fucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	peptide-O-fucosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›61	›61	GDP-fucose protein O-fucosyltransferase 1		PRO_0000220935
Experimental info
	Non-terminal residue	61	1

Sequences

	Sequence		Length	Mass (Da)
	P83337 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: E9507AE60018F23A	FASTA	61	6,955
	10 20 30 40 50 60 RLAGSWDLAG YLLYXPXMGR FGNQADHFLG SLAFAKLXVR TLAVPPWIEY QHHKPPFTNL H

References

[1]	"Modification of epidermal growth factor-like repeats with O-fucose: molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase." Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P., Haltiwanger R.S. J. Biol. Chem. 276:40338-40345(2001) [PubMed: 11524432] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"O-linked fucose and other post-translational modifications unique to EGF modules." Harris R.J., Spellman M.W. Glycobiology 3:219-224(1993) [PubMed: 8358148] [Abstract] Cited for: FUNCTION.
[3]	"Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains." Wang Y., Lee G.F., Kelley R.F., Spellman M.W. Glycobiology 6:837-842(1996) [PubMed: 9023546] [Abstract] Cited for: FUNCTION.
[4]	"Purification and characterization of a GDP-fucose:polypeptide fucosyltransferase from Chinese hamster ovary cells." Wang Y., Spellman M.W. J. Biol. Chem. 273:8112-8118(1998) [PubMed: 9525914] [Abstract] Cited for: FUNCTION, GLYCOSYLATION. Tissue: Ovary.

Cross-references

3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR019378. GDP-Fuc_O-FucTrfase. [Graphical view]
Pfam	PF10250. O-FucT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OFUT1_CRIGR

Accession

Primary (citable) accession number: P83337

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 13, 2004
Last sequence update:	June 1, 2002
Last modified:	January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program