Reviewed, UniProtKB/Swiss-Prot Q18014 (OFUT1_CAEEL)

Names and origin

Protein names

Recommended name:
    Putative 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

ORF Names:

C15C7.7

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
Catalytic activity	Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.
Cofactor	Manganese By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulumBy similarity.
Sequence similarities	Belongs to the glycosyltransferase 68 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Fucose metabolism Notch signaling pathway
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
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 protein amino acid O-linked glycosylation Ref.2 Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to Golgi membrane Ref.2 Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 389	368	Putative GDP-fucose protein O-fucosyltransferase 1		PRO_0000012152
Amino acid modifications
	Glycosylation	24	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q18014-1 [UniParc]. Last modified February 1, 2005. Version 5. Checksum: 0C84F202AA184554	FASTA	389	44,051
	10 20 30 40 50 60 MRVSKVLTLA SFISVCSYSE AKSNETDPNG YIVFCPCMGR FGNQVDQFLG VLAFAKALDR 70 80 90 100 110 120 TLVLPNFIEF KHPETKMIPF EFLFQVGTVA KYTRVVTMQE FTKKIMPTVW PPEKRKAFCW 130 140 150 160 170 180 TPRQAIYDKS AEPGCHSKEG NPFGPYWDQI DVSFVGDEYF GDIPGGFDLN QMGSRKKWLE 190 200 210 220 230 240 KFPSEEYPVL AFSSAPAPFP SKGKVWSIQK YLRWSSRITE QAKKFISANL AKPFVAVHLR 250 260 270 280 290 300 NDADWVRVCE HIDTTTNRPL FASEQCLGEG HHLGTLTKEI CSPSKQQILE QIVEKVGSIG 310 320 330 340 350 360 AKSVFVASDK DHMIDEINEA LKPYEIEAHR QEPDDMYTSL AIMGRADLFV GNCVSTFSHI 370 380 VKRERDHAGQ SPRPSAFFGI RAVKRHIDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[2]	"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: HOMOLOGY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U41528 Genomic DNA. Translation: AAM51514.2.
RefSeq	NP_741744.2.
UniGene	Cel.30602
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	C15C7.7. Caenorhabditis elegans. [Contig view]
GeneID	180607.
KEGG	cel:C15C7.7.
NMPDR	fig|6239.3.peg.22809.
Organism-specific databases
WormBase	WBGene00015793. C15C7.7.
WormPep	C15C7.7. CE36786. [WorfDB]
Gene expression databases
ArrayExpress	Q18014.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	910082.

Entry information

Entry name

OFUT1_CAEEL

Accession

Primary (citable) accession number: Q18014

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	February 1, 2005
Last modified:	November 25, 2008
This is version 49 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project