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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 similarity

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

Vmax=2.5 µmol/min/mg enzyme1 Publication

Vmax=2.4 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 5.5-8.0.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei339 – 3391SubstrateBy similarity

GO - Molecular functioni

  1. peptide-O-fucosyltransferase activity Source: UniProtKB
  2. transferase activity Source: UniProtKB
  3. transferase activity, transferring glycosyl groups Source: UniProtKB

GO - Biological processi

  1. fucose metabolic process Source: UniProtKB-KW
  2. Notch signaling pathway Source: UniProtKB-KW
  3. protein glycosylation Source: UniProtKB
  4. protein O-linked fucosylation Source: GOC
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
ProteomesiUP000001075 Componenti: Unassembled WGS sequence

Subcellular locationi

  1. Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392GDP-fucose protein O-fucosyltransferase 1PRO_0000220935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 44By similarity
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi130 ↔ 144By similarity
Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
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)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 503Substrate bindingBy similarity
Regioni242 – 2443Substrate bindingBy similarity
Regioni360 – 3612Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi389 – 3924Prevents secretion from ERSequence Analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661N → V AA sequence (PubMed:11524432).Curated

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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-88.
  3. "O-linked fucose and other post-translational modifications unique to EGF modules."
    Harris R.J., Spellman M.W.
    Glycobiology 3:219-224(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY.
  4. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "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] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES.

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: January 7, 2015
This is version 46 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

External Data

Dasty 3

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 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.