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Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

Pofut1

Organism
Mus musculus (Mouse)
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 DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs).2 Publications

Miscellaneous

The cax (compact axial skeleton) spontaneous mutation is a hypomorphic allele that reduces Pofut1 expression and protein levels leading to reduced Notch signaling. cax mutant embryos have somites of variable size, partly abnormal Lfng expression, defective anterior-posterior somite patterning and abnormal axial skeleton development. Mice have kinky and shortened tails and shortened body length (PubMed:19161597).1 Publication

Catalytic activityi

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

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 sitei345SubstrateBy similarity1

GO - Molecular functioni

  • fucosyltransferase activity Source: UniProtKB
  • peptide-O-fucosyltransferase activity Source: MGI

GO - Biological processi

  • angiogenesis Source: MGI
  • fucose metabolic process Source: MGI
  • heart development Source: MGI
  • nervous system development Source: MGI
  • Notch signaling pathway Source: UniProtKB
  • protein O-linked fucosylation Source: MGI
  • protein O-linked glycosylation Source: UniProtKB
  • regulation of Notch signaling pathway Source: UniProtKB
  • somitogenesis Source: MGI

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processCarbohydrate metabolism, Fucose metabolism, Notch signaling pathway
LigandManganese

Enzyme and pathway databases

BRENDAi2.4.1.221. 3474.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT65. Glycosyltransferase Family 65.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2153207. Pofut1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Early embryos of null mice are defective in somitogenesis. At E8.5, embryos are of normal size and appearance but somites adjacent to the presomitic mesoderm (PSM) are fused. In E8.25 embryos, expression of NOTCH target genes such as HES5 and JAG1 as well as LFNG and UNCX4.1 is severly reduced in somites. There is up-regulation of a number of these genes such as HES5 and LFNG as well as DLL1 and NOTCH1 in the neural tube and brain. Mice die at midgestation with severe defects in somitogenesis, vasculogenesis, cardiogenesis and neurogenesis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000001214931 – 393GDP-fucose protein O-fucosyltransferase 1Add BLAST363

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi43 ↔ 45By similarity
Glycosylationi67N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi131 ↔ 145By similarity
Glycosylationi165N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi254 ↔ 288By similarity
Disulfide bondi272 ↔ 359By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ91ZW2.
MaxQBiQ91ZW2.
PaxDbiQ91ZW2.
PeptideAtlasiQ91ZW2.
PRIDEiQ91ZW2.

PTM databases

PhosphoSitePlusiQ91ZW2.

Expressioni

Developmental stagei

Increased expression throughout embryo development. Ubiquitous expression at E9.5 and E11.5 with lower expression at E9.5.1 Publication

Gene expression databases

BgeeiENSMUSG00000046020.
CleanExiMM_POFUT1.
ExpressionAtlasiQ91ZW2. baseline and differential.
GenevisibleiQ91ZW2. MM.

Interactioni

Protein-protein interaction databases

IntActiQ91ZW2. 1 interactor.
MINTiMINT-4105805.
STRINGi10090.ENSMUSP00000053122.

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 42Combined sources4
Beta strandi46 – 48Combined sources3
Helixi49 – 66Combined sources18
Beta strandi69 – 72Combined sources4
Beta strandi75 – 77Combined sources3
Beta strandi88 – 90Combined sources3
Helixi92 – 95Combined sources4
Helixi99 – 103Combined sources5
Beta strandi107 – 109Combined sources3
Helixi110 – 116Combined sources7
Helixi118 – 121Combined sources4
Helixi124 – 126Combined sources3
Beta strandi128 – 132Combined sources5
Helixi133 – 137Combined sources5
Beta strandi142 – 144Combined sources3
Beta strandi147 – 150Combined sources4
Helixi153 – 158Combined sources6
Turni159 – 161Combined sources3
Beta strandi165 – 170Combined sources6
Helixi177 – 179Combined sources3
Helixi180 – 186Combined sources7
Turni189 – 191Combined sources3
Beta strandi193 – 199Combined sources7
Helixi208 – 216Combined sources9
Helixi221 – 234Combined sources14
Beta strandi237 – 244Combined sources8
Helixi248 – 250Combined sources3
Helixi251 – 255Combined sources5
Beta strandi260 – 262Combined sources3
Turni267 – 269Combined sources3
Helixi270 – 273Combined sources4
Beta strandi275 – 278Combined sources4
Helixi285 – 288Combined sources4
Helixi292 – 306Combined sources15
Beta strandi309 – 317Combined sources9
Helixi321 – 325Combined sources5
Turni326 – 330Combined sources5
Beta strandi332 – 336Combined sources5
Helixi342 – 350Combined sources9
Beta strandi353 – 357Combined sources5
Helixi362 – 373Combined sources12
Beta strandi378 – 380Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5KXHX-ray1.33A33-384[»]
5KXQX-ray1.90A/B/C/D32-385[»]
5KY0X-ray1.53A33-384[»]
5KY2X-ray1.47A33-384[»]
5KY3X-ray1.53A33-384[»]
5KY4X-ray1.47A33-384[»]
5KY5X-ray1.50A33-384[»]
5KY7X-ray1.60A33-384[»]
5KY8X-ray1.65A33-384[»]
5KY9X-ray1.83A33-384[»]
ProteinModelPortaliQ91ZW2.
SMRiQ91ZW2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni48 – 51Substrate bindingBy similarity4
Regioni243 – 245Substrate bindingBy similarity3
Regioni362 – 363Substrate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi390 – 393Prevents secretion from ERSequence analysis4

Sequence similaritiesi

Belongs to the glycosyltransferase 65 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3849. Eukaryota.
ENOG410Y3JQ. LUCA.
GeneTreeiENSGT00390000015634.
HOGENOMiHOG000231651.
HOVERGENiHBG059976.
InParanoidiQ91ZW2.
KOiK03691.
OMAiGQSNHFI.
OrthoDBiEOG091G048B.
PhylomeDBiQ91ZW2.
TreeFamiTF314805.

Family and domain databases

InterProiView protein in InterPro
IPR019378. GDP-Fuc_O-FucTrfase.
PfamiView protein in Pfam
PF10250. O-FucT. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91ZW2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAAAWAPPH LLLRASFLLL LLLLPLRGRS AGSWDLAGYL LYCPCMGRFG
60 70 80 90 100
NQADHFLGSL AFAKLLNRTL AVPPWIEYQH HKPPFTNLHV SYQKYFKLEP
110 120 130 140 150
LQAYHRVVSL EDFMENLAPS HWPPEKRVAY CFEVAAQRSP DKKTCPMKEG
160 170 180 190 200
NPFGPFWDQF HVSFNKSELF TGISFSASYK EQWTQRFPAK EHPVLALPGA
210 220 230 240 250
PAQFPVLEEH RELQKYMVWS DEMVRTGEAL ISAHLVRPYV GIHLRIGSDW
260 270 280 290 300
KNACAMLKDG TAGSHFMASP QCVGYSRSTA TPLTMTMCLP DLKEIQRAVT
310 320 330 340 350
LWVRALNARS VYIATDSESY VSEIQQLFKD KVRVVSLKPE VAQIDLYILG
360 370 380 390
QADHFIGNCV SSFTAFVKRE RDLHGRQSSF FGMDRPSQLR DEF
Length:393
Mass (Da):44,688
Last modified:December 1, 2001 - v1
Checksum:iD982104E95E5CF3B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti233A → S in BAC32009 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF375885 mRNA. Translation: AAL09577.1.
AK044629 mRNA. Translation: BAC32009.1.
AK132301 mRNA. Translation: BAE21090.1.
BC046295 mRNA. Translation: AAH46295.1.
CCDSiCCDS16909.1.
RefSeqiNP_536711.3. NM_080463.3.
UniGeneiMm.293761.

Genome annotation databases

EnsembliENSMUST00000049863; ENSMUSP00000053122; ENSMUSG00000046020.
GeneIDi140484.
KEGGimmu:140484.
UCSCiuc008nhm.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiOFUT1_MOUSE
AccessioniPrimary (citable) accession number: Q91ZW2
Secondary accession number(s): Q3V1R0, Q8C8R4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: December 1, 2001
Last modified: October 25, 2017
This is version 136 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families