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Q91ZW2 (OFUT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.4 Ref.5

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum By similarity.

Developmental stage

Increased expression throughout embryo development. Ubiquitous expression at E9.5 and E11.5 with lower expression at E9.5. Ref.4

Post-translational modification

N-glycosylated By similarity.

Disruption phenotype

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. Ref.4

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 (Ref.6).

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 393363GDP-fucose protein O-fucosyltransferase 1
PRO_0000012149

Regions

Region49 – 513Substrate binding By similarity
Region243 – 2453Substrate binding By similarity
Region361 – 3622Substrate binding By similarity
Motif390 – 3934Prevents secretion from ER Potential

Sites

Binding site3401Substrate By similarity

Amino acid modifications

Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential
Disulfide bond43 ↔ 45 By similarity
Disulfide bond131 ↔ 145 By similarity
Disulfide bond254 ↔ 288 By similarity
Disulfide bond272 ↔ 359 By similarity

Experimental info

Sequence conflict2331A → S in BAC32009. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q91ZW2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: D982104E95E5CF3B

FASTA39344,688
        10         20         30         40         50         60 
MGAAAWAPPH LLLRASFLLL LLLLPLRGRS AGSWDLAGYL LYCPCMGRFG NQADHFLGSL 

        70         80         90        100        110        120 
AFAKLLNRTL AVPPWIEYQH HKPPFTNLHV SYQKYFKLEP LQAYHRVVSL EDFMENLAPS 

       130        140        150        160        170        180 
HWPPEKRVAY CFEVAAQRSP DKKTCPMKEG NPFGPFWDQF HVSFNKSELF TGISFSASYK 

       190        200        210        220        230        240 
EQWTQRFPAK EHPVLALPGA PAQFPVLEEH RELQKYMVWS DEMVRTGEAL ISAHLVRPYV 

       250        260        270        280        290        300 
GIHLRIGSDW KNACAMLKDG TAGSHFMASP QCVGYSRSTA TPLTMTMCLP DLKEIQRAVT 

       310        320        330        340        350        360 
LWVRALNARS VYIATDSESY VSEIQQLFKD KVRVVSLKPE VAQIDLYILG QADHFIGNCV 

       370        380        390 
SSFTAFVKRE RDLHGRQSSF FGMDRPSQLR DEF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Peptide-O-fucosyltransferase 1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF375885 mRNA. Translation: AAL09577.1.
AK044629 mRNA. Translation: BAC32009.1.
AK132301 mRNA. Translation: BAE21090.1.
BC046295 mRNA. Translation: AAH46295.1.
CCDSCCDS16909.1.
RefSeqNP_536711.3. NM_080463.3.
UniGeneMm.293761.

3D structure databases

ProteinModelPortalQ91ZW2.
SMRQ91ZW2. Positions 35-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91ZW2. 1 interaction.
MINTMINT-4105805.

Protein family/group databases

CAZyGT65. Glycosyltransferase Family 65.

PTM databases

PhosphoSiteQ91ZW2.

Proteomic databases

MaxQBQ91ZW2.
PaxDbQ91ZW2.
PRIDEQ91ZW2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049863; ENSMUSP00000053122; ENSMUSG00000046020.
GeneID140484.
KEGGmmu:140484.
UCSCuc008nhm.1. mouse.

Organism-specific databases

CTD23509.
MGIMGI:2153207. Pofut1.

Phylogenomic databases

eggNOGNOG250895.
GeneTreeENSGT00390000015634.
HOGENOMHOG000231651.
HOVERGENHBG059976.
InParanoidQ91ZW2.
KOK03691.
OMASEHPVLA.
OrthoDBEOG7ZD1VC.
PhylomeDBQ91ZW2.
TreeFamTF314805.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ91ZW2.
BgeeQ91ZW2.
CleanExMM_POFUT1.
GenevestigatorQ91ZW2.

Family and domain databases

InterProIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamPF10250. O-FucT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio369790.
PROQ91ZW2.
SOURCESearch...

Entry information

Entry nameOFUT1_MOUSE
AccessionPrimary (citable) accession number: Q91ZW2
Secondary accession number(s): Q3V1R0, Q8C8R4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot