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Q91ZW2

- OFUT1_MOUSE

UniProt

Q91ZW2 - OFUT1_MOUSE

Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

Pofut1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei340 – 3401SubstrateBy similarity

    GO - Molecular functioni

    1. fucosyltransferase activity Source: UniProtKB
    2. peptide-O-fucosyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. angiogenesis Source: MGI
    2. fucose metabolic process Source: MGI
    3. heart development Source: MGI
    4. nervous system development Source: MGI
    5. Notch signaling pathway Source: UniProtKB
    6. protein O-linked glycosylation Source: UniProtKB
    7. somitogenesis Source: MGI

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

    Keywords - Ligandi

    Manganese

    Enzyme and pathway databases

    ReactomeiREACT_196492. 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: Chromosome 2

    Organism-specific databases

    MGIiMGI:2153207. Pofut1.

    Subcellular locationi

    Endoplasmic reticulum By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB

    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

    ArrayExpressiQ91ZW2.
    BgeeiQ91ZW2.
    CleanExiMM_POFUT1.
    GenevestigatoriQ91ZW2.

    Interactioni

    Protein-protein interaction databases

    IntActiQ91ZW2. 1 interaction.
    MINTiMINT-4105805.

    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.
    OMAiSEHPVLA.
    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

    MGAAAWAPPH LLLRASFLLL LLLLPLRGRS AGSWDLAGYL LYCPCMGRFG    50
    NQADHFLGSL AFAKLLNRTL AVPPWIEYQH HKPPFTNLHV SYQKYFKLEP 100
    LQAYHRVVSL EDFMENLAPS HWPPEKRVAY CFEVAAQRSP DKKTCPMKEG 150
    NPFGPFWDQF HVSFNKSELF TGISFSASYK EQWTQRFPAK EHPVLALPGA 200
    PAQFPVLEEH RELQKYMVWS DEMVRTGEAL ISAHLVRPYV GIHLRIGSDW 250
    KNACAMLKDG TAGSHFMASP QCVGYSRSTA TPLTMTMCLP DLKEIQRAVT 300
    LWVRALNARS VYIATDSESY VSEIQQLFKD KVRVVSLKPE VAQIDLYILG 350
    QADHFIGNCV SSFTAFVKRE RDLHGRQSSF FGMDRPSQLR DEF 393
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF375885 mRNA. Translation: AAL09577.1 .
    AK044629 mRNA. Translation: BAC32009.1 .
    AK132301 mRNA. Translation: BAE21090.1 .
    BC046295 mRNA. Translation: AAH46295.1 .
    CCDSi CCDS16909.1.
    RefSeqi NP_536711.3. NM_080463.3.
    UniGenei Mm.293761.

    3D structure databases

    ProteinModelPortali Q91ZW2.
    SMRi Q91ZW2. Positions 35-383.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q91ZW2. 1 interaction.
    MINTi MINT-4105805.

    Protein family/group databases

    CAZyi GT65. Glycosyltransferase Family 65.

    PTM databases

    PhosphoSitei Q91ZW2.

    Proteomic databases

    MaxQBi Q91ZW2.
    PaxDbi Q91ZW2.
    PRIDEi Q91ZW2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049863 ; ENSMUSP00000053122 ; ENSMUSG00000046020 .
    GeneIDi 140484.
    KEGGi mmu:140484.
    UCSCi uc008nhm.1. mouse.

    Organism-specific databases

    CTDi 23509.
    MGIi MGI:2153207. Pofut1.

    Phylogenomic databases

    eggNOGi NOG250895.
    GeneTreei ENSGT00390000015634.
    HOGENOMi HOG000231651.
    HOVERGENi HBG059976.
    InParanoidi Q91ZW2.
    KOi K03691.
    OMAi SEHPVLA.
    OrthoDBi EOG7ZD1VC.
    PhylomeDBi Q91ZW2.
    TreeFami TF314805.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_196492. Pre-NOTCH Processing in the Endoplasmic Reticulum.

    Miscellaneous databases

    NextBioi 369790.
    PROi Q91ZW2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91ZW2.
    Bgeei Q91ZW2.
    CleanExi MM_POFUT1.
    Genevestigatori Q91ZW2.

    Family and domain databases

    InterProi IPR019378. GDP-Fuc_O-FucTrfase.
    [Graphical view ]
    Pfami PF10250. O-FucT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 113 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