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Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

POFUT1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, an acetylglucosaminyltransferase that can then extend the fucosylation on the NOTCH EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by DELTA1 or JAGGED1 (By similarity). Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs) (By similarity).By similarity1 Publication

Catalytic activityi

Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.3 Publications

Enzyme regulationi

Activated by manganese and, to a lesser extent, by other divalent metals such as cobalt and calcium. Inhibited by copper, ferric and zinc ions.1 Publication

Kineticsi

  1. KM=11 µM for His(6)-F7-EGF-11 Publication
  2. KM=15 µM for F7-EGF-11 Publication
  1. Vmax=2.5 µmol/min/mg enzyme1 Publication
  2. Vmax=2.4 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 5.5-8.0.1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei339SubstrateBy similarity1

GO - Molecular functioni

  • peptide-O-fucosyltransferase activity Source: UniProtKB
  • transferase activity Source: UniProtKB
  • transferase activity, transferring glycosyl groups Source: UniProtKB

GO - Biological processi

  • fucose metabolic process Source: UniProtKB-KW
  • Notch signaling pathway Source: UniProtKB-KW
  • protein glycosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
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 namesi
Name:POFUT1
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus
Proteomesi
  • UP000001075 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002209351 – 392GDP-fucose protein O-fucosyltransferase 1Add BLAST392

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi42 ↔ 44By similarity
Glycosylationi66N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi130 ↔ 144By similarity
Glycosylationi164N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi253 ↔ 287By similarity
Disulfide bondi271 ↔ 358By similarity

Post-translational modificationi

N-glycosylated. Contains high mannose-type carbohydrates.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni48 – 50Substrate bindingBy similarity3
Regioni242 – 244Substrate bindingBy similarity3
Regioni360 – 361Substrate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi389 – 392Prevents secretion from ERSequence analysis4

Sequence similaritiesi

Belongs to the glycosyltransferase 68 family.Curated

Phylogenomic databases

InParanoidiP83337.
KOiK03691.

Family and domain databases

InterProiIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamiPF10250. O-FucT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAAAWAPPH LLLRVSLLLL LLLPLRGRLA GSWDLAGYLL YCPCMGRFGN
60 70 80 90 100
QADHFLGSLA FAKLLNRTLA VPPWIEYQHH KPPFTNLHVS YQKYFKLEPL
110 120 130 140 150
QAYHRVISLE EFMEKLAPIH WPPEKRVAYC FEVAAQRSPD KKTCPMKEGN
160 170 180 190 200
PFGPFWDQFH VSFNKSELFT GISFSASYKE QWIQRFPPEE HPVLALPGAP
210 220 230 240 250
AQFPVLEEHR ALQKYMVWSD EMVKTGEAQI STHLIRPYVG IHLRIGSDWK
260 270 280 290 300
NACAMLKDGT AGSHFMASPQ CVGYSRSTAT PLTMTMCLPD LNEIQRAVKL
310 320 330 340 350
WVRALNARSI YIATDSESYV PEIQQLFKEK VKVVSLKPEV AQVDLYILGQ
360 370 380 390
ADHFIGNCVS SFTAFVKRER DLHGRQSSFF GMDRPSQPRD EF
Length:392
Mass (Da):44,669
Last modified:January 9, 2013 - v2
Checksum:i45E1421CBA0880C4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66N → V AA sequence (PubMed:11524432).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JH000311 Genomic DNA. Translation: EGW00282.1.
RefSeqiXP_003502364.1. XM_003502316.2.

Genome annotation databases

GeneIDi100753417.
KEGGicge:100753417.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JH000311 Genomic DNA. Translation: EGW00282.1.
RefSeqiXP_003502364.1. XM_003502316.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100753417.
KEGGicge:100753417.

Organism-specific databases

CTDi23509.

Phylogenomic databases

InParanoidiP83337.
KOiK03691.

Enzyme and pathway databases

UniPathwayiUPA00378.

Family and domain databases

InterProiIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamiPF10250. O-FucT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiOFUT1_CRIGR
AccessioniPrimary (citable) accession number: P83337
Secondary accession number(s): G3HE95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: January 9, 2013
Last modified: July 6, 2016
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.