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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

Catalytic activityi

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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei340 – 3401SubstrateBy similarity

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
  • somitogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

Keywords - Ligandi

Manganese

Enzyme and pathway databases

BRENDAi2.4.1.221. 3474.
ReactomeiREACT_291428. Pre-NOTCH Processing in the Endoplasmic Reticulum.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2153207. Pofut1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 393363GDP-fucose protein O-fucosyltransferase 1PRO_0000012149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi43 ↔ 45By similarity
Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi131 ↔ 145By similarity
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi254 ↔ 288By similarity
Disulfide bondi272 ↔ 359By similarity

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ91ZW2.
PaxDbiQ91ZW2.
PRIDEiQ91ZW2.

PTM databases

PhosphoSiteiQ91ZW2.

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

BgeeiQ91ZW2.
CleanExiMM_POFUT1.
ExpressionAtlasiQ91ZW2. baseline and differential.
GenevisibleiQ91ZW2. MM.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ91ZW2.
SMRiQ91ZW2. Positions 35-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 513Substrate bindingBy similarity
Regioni243 – 2453Substrate bindingBy similarity
Regioni361 – 3622Substrate bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi390 – 3934Prevents secretion from ERSequence Analysis

Sequence similaritiesi

Belongs to the glycosyltransferase 68 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG250895.
GeneTreeiENSGT00390000015634.
HOGENOMiHOG000231651.
HOVERGENiHBG059976.
InParanoidiQ91ZW2.
KOiK03691.
OMAiCISSFTS.
OrthoDBiEOG7ZD1VC.
PhylomeDBiQ91ZW2.
TreeFamiTF314805.

Family and domain databases

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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2331A → S in BAC32009 (PubMed:16141072).Curated

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.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Peptide-O-fucosyltransferase 1

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.

3D structure databases

ProteinModelPortaliQ91ZW2.
SMRiQ91ZW2. Positions 35-383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

CAZyiGT65. Glycosyltransferase Family 65.

PTM databases

PhosphoSiteiQ91ZW2.

Proteomic databases

MaxQBiQ91ZW2.
PaxDbiQ91ZW2.
PRIDEiQ91ZW2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23509.
MGIiMGI:2153207. Pofut1.

Phylogenomic databases

eggNOGiNOG250895.
GeneTreeiENSGT00390000015634.
HOGENOMiHOG000231651.
HOVERGENiHBG059976.
InParanoidiQ91ZW2.
KOiK03691.
OMAiCISSFTS.
OrthoDBiEOG7ZD1VC.
PhylomeDBiQ91ZW2.
TreeFamiTF314805.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.221. 3474.
ReactomeiREACT_291428. Pre-NOTCH Processing in the Endoplasmic Reticulum.

Miscellaneous databases

ChiTaRSiPofut1. mouse.
NextBioi369790.
PROiQ91ZW2.
SOURCEiSearch...

Gene expression databases

BgeeiQ91ZW2.
CleanExiMM_POFUT1.
ExpressionAtlasiQ91ZW2. baseline and differential.
GenevisibleiQ91ZW2. MM.

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. "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: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129/SvJ.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N-3.
    Tissue: Mammary gland.
  4. "Protein O-fucosyltransferase 1 is an essential component of Notch signaling pathways."
    Shi S., Stanley P.
    Proc. Natl. Acad. Sci. U.S.A. 100:5234-5239(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, FUNCTION.
  5. "O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors."
    Kim M.L., Chandrasekharan K., Glass M., Shi S., Stahl M.C., Kaspar B., Stanley P., Martin P.T.
    Mol. Cell. Neurosci. 39:452-464(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Notch signalling in the paraxial mesoderm is most sensitive to reduced Pofut1 levels during early mouse development."
    Schuster-Gossler K., Harris B., Johnson K.R., Serth J., Gossler A.
    BMC Dev. Biol. 9:6-6(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE CAX MUTATION.

Entry informationi

Entry nameiOFUT1_MOUSE
AccessioniPrimary (citable) accession number: Q91ZW2
Secondary accession number(s): Q3V1R0, Q8C8R4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

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. 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.