Q6EV70 (OFUT1_RAT) 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
Synonyms:	Fut12

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	395 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. Ref.2 UniProtKB P83337
Catalytic activity	Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor. UniProtKB P83337
Cofactor	Manganese By similarity. UniProtKB P83337
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum Ref.2.
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 Reference 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 O-linked glycosylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	endoplasmic reticulum Inferred from direct assay Ref.2. Source: RGD membrane Inferred from sequence or structural similarity. Source: UniProtKB
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
	Signal peptide	1 – 32	32	Potential
	Chain	33 – 395	363	GDP-fucose protein O-fucosyltransferase 1		PRO_0000012151
Regions
	Motif	392 – 395	4	Prevents secretion from ER
Amino acid modifications
	Glycosylation	69	1	N-linked (GlcNAc...) Potential
	Glycosylation	167	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6EV70 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 2A85521E22F38920	FASTA	395	44,983
	10 20 30 40 50 60 MGAAAWAPSH LLLRASFLLL LLLLPLPLRG RAGGSWDLAG YLLYCPCMGR FGNQADHFLG 70 80 90 100 110 120 SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL EPLQAYHRVI SLEDFMEKLA 130 140 150 160 170 180 PFHWPPEKRV AYCFEVAAQR SPDKKTCPMK EGNPFGPFWD QFHVSFNKSE LFTGISFSAS 190 200 210 220 230 240 YKEQWIQRFP PKEHPVLALP GAPAQFPVLE EHRELQKYMV WSDEMVRTGE AQISTHLVRP 250 260 270 280 290 300 YVGIHLRIGS DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TATPLTTTMC LPDLKEIQRA 310 320 330 340 350 360 VKLWVRALDA RSVYIATDSE SYVSEIQQLF KEKVKVVSLK PEVAQIDLYI LGQADHFIGN 370 380 390 CVSSFTAFVK RERDLHGRPS SFFGMDRPSQ LRDEF

References

[1]	"A new superfamily of protein-O-fucosyltransferases, alpha2-fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and identification of conserved peptide motifs." Martinez-Duncker I., Mollicone R., Candelier J.-J., Breton C., Oriol R. Glycobiology 13:1C-5C(2003) [PubMed: 12966037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar.
[2]	"O-fucosylation of notch occurs in the endoplasmic reticulum." Luo Y., Haltiwanger R.S. J. Biol. Chem. 280:11289-11294(2005) [PubMed: 15653671] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ781499 mRNA. Translation: CAH03711.1.
IPI	IPI00454554.
RefSeq	NP_001002278.1. NM_001002278.1.
UniGene	Rn.214685.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6EV70.
Protein family/group databases
CAZy	GT65. Glycosyltransferase Family 65.
Proteomic databases
PRIDE	Q6EV70.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000013730; ENSRNOP00000013730; ENSRNOG00000010104.
GeneID	311551.
KEGG	rno:311551.
NMPDR	fig|10116.3.peg.20024.
Organism-specific databases
CTD	23509.
RGD	1303001. Pofut1.
Phylogenomic databases
eggNOG	roNOG06430.
GeneTree	ENSGT00390000015634.
HOVERGEN	HBG059976.
InParanoid	Q6EV70.
OMA	SAFVKRE.
OrthoDB	EOG43TZVN.
PhylomeDB	Q6EV70.
Gene expression databases
Genevestigator	Q6EV70.
Family and domain databases
InterPro	IPR019378. GDP-Fuc_O-FucTrfase. [Graphical view]
KO	K03691.
Pfam	PF10250. O-FucT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	663802.

Entry information

Entry name

OFUT1_RAT

Accession

Primary (citable) accession number: Q6EV70

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	August 16, 2004
Last modified:	November 16, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program