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Q8VHI3

- OFUT2_MOUSE

UniProt

Q8VHI3 - OFUT2_MOUSE

Protein

GDP-fucose protein O-fucosyltransferase 2

Gene

Pofut2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      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 in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of several protein families including the ADAMTS superfamily and the thrombosporin (TSP) and spondin families. Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13 By similarity. O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm.By similarity1 Publication

    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
    Active sitei54 – 541Proton donor/acceptorBy similarity
    Binding sitei294 – 2941SubstrateBy similarity
    Sitei396 – 3961Required for enzyme activity

    GO - Molecular functioni

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

    GO - Biological processi

    1. fucose metabolic process Source: UniProtKB-KW
    2. fucosylation Source: MGI
    3. mesoderm formation Source: MGI
    4. protein O-linked fucosylation Source: UniProtKB
    5. regulation of epithelial to mesenchymal transition Source: MGI
    6. regulation of gene expression Source: MGI
    7. regulation of secretion Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism

    Enzyme and pathway databases

    ReactomeiREACT_211817. O-glycosylation of TSR domain-containing proteins.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT68. Glycosyltransferase Family 68.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GDP-fucose protein O-fucosyltransferase 2 (EC:2.4.1.221)
    Alternative name(s):
    Peptide-O-fucosyltransferase 2
    Short name:
    O-FucT-2
    Gene namesi
    Name:Pofut2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1916863. Pofut2.

    Subcellular locationi

    Endoplasmic reticulum By similarity. Golgi apparatus By similarity
    Note: Mainly located in the endoplasmic reticulum.By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. Golgi apparatus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus

    Pathology & Biotechi

    Disruption phenotypei

    Null mice embryos die before E10.5. At the onset of gastrulation at E6.5, embryos are rounder and the embryonic and extra-embryonic ectoderm appears thickened and disorganized. Expression of NODAL and WNT3 is significantly expanded and/or displaced in the primitive streak as is BMP4 in the extra-embryonic ectoderm. By E7.5, embryos are unusually dense and shorter characterized by a dumb-bell appearance. There is unrestricted epithelial to mesenchymal transition (EMT) producing an abundance of mesenchymal cells. SNAIL1 expression is expanded and E-cadherin expression decreased. There is distal expansion of the proximal visceral endoderm.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi396 – 3961E → A: Abolishes in vitro enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 429408GDP-fucose protein O-fucosyltransferase 2PRO_0000012155Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi161 ↔ 192By similarity
    Glycosylationi189 – 1891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi412 ↔ 419By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ8VHI3.
    PaxDbiQ8VHI3.
    PRIDEiQ8VHI3.

    PTM databases

    PhosphoSiteiQ8VHI3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8VHI3.
    BgeeiQ8VHI3.
    CleanExiMM_POFUT2.
    GenevestigatoriQ8VHI3.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VHI3.
    SMRiQ8VHI3. Positions 41-429.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 564Substrate bindingBy similarity
    Regioni388 – 3892Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyltransferase 68 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG77810.
    GeneTreeiENSGT00390000007989.
    HOGENOMiHOG000015874.
    HOVERGENiHBG053367.
    InParanoidiQ8VHI3.
    KOiK03691.
    OMAiICAHARF.
    OrthoDBiEOG76T9S1.
    PhylomeDBiQ8VHI3.
    TreeFamiTF314337.

    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.

    Q8VHI3-1 [UniParc]FASTAAdd to Basket

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    MAALSVVCLL LAAASWRPVS ASGEEFWPGQ SAADILSGAA SRRRYLLYDV    50
    NPPEGFNLRR DVYIRVASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV 100
    RIPWSEFFDL PSLNKNIPVI EYEQFIAESG GPFIDQVYVL QGYAEGWKEG 150
    TWEEKVDARP CIDPLLYSQD KHEYYRGWFW GYEETRGLNV SCLSVQGSAS 200
    IVAPVLLKNT SARSVMLDRA ENLLHDHYGG REYWDTRRSM VFAKHLRAVG 250
    DEFRSQHLNS TDAADKMAPE EDWTKMKVKL GSALGGPYLG VHLRRKDFIW 300
    GHREDVPSLE GAVKKIRSLM KTHQLDKVFV ATDAIRKEQE ELRKLLPEMV 350
    RFEPTWEELE LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL 400
    GLDPKTTYNR FCGDQEKACE QPTHWKIAY 429
    Length:429
    Mass (Da):49,429
    Last modified:March 1, 2002 - v1
    Checksum:i0E7AFF5F1CD33560
    GO

    Sequence cautioni

    The sequence BC018194 differs from that shown. Reason: Frameshift at position 380.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF455270 mRNA. Translation: AAL65192.1.
    BC018194 mRNA. No translation available.
    AK009301 mRNA. Translation: BAB26202.1.
    CCDSiCCDS23954.1.
    RefSeqiNP_084538.2. NM_030262.3.
    UniGeneiMm.203556.

    Genome annotation databases

    EnsembliENSMUST00000020493; ENSMUSP00000020493; ENSMUSG00000020260.
    GeneIDi80294.
    KEGGimmu:80294.
    UCSCiuc007fvj.1. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Peptide-O-fucosyltransferase 2

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF455270 mRNA. Translation: AAL65192.1 .
    BC018194 mRNA. No translation available.
    AK009301 mRNA. Translation: BAB26202.1 .
    CCDSi CCDS23954.1.
    RefSeqi NP_084538.2. NM_030262.3.
    UniGenei Mm.203556.

    3D structure databases

    ProteinModelPortali Q8VHI3.
    SMRi Q8VHI3. Positions 41-429.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT68. Glycosyltransferase Family 68.

    PTM databases

    PhosphoSitei Q8VHI3.

    Proteomic databases

    MaxQBi Q8VHI3.
    PaxDbi Q8VHI3.
    PRIDEi Q8VHI3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020493 ; ENSMUSP00000020493 ; ENSMUSG00000020260 .
    GeneIDi 80294.
    KEGGi mmu:80294.
    UCSCi uc007fvj.1. mouse.

    Organism-specific databases

    CTDi 23275.
    MGIi MGI:1916863. Pofut2.

    Phylogenomic databases

    eggNOGi NOG77810.
    GeneTreei ENSGT00390000007989.
    HOGENOMi HOG000015874.
    HOVERGENi HBG053367.
    InParanoidi Q8VHI3.
    KOi K03691.
    OMAi ICAHARF.
    OrthoDBi EOG76T9S1.
    PhylomeDBi Q8VHI3.
    TreeFami TF314337.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_211817. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    ChiTaRSi POFUT2. mouse.
    NextBioi 350013.
    PROi Q8VHI3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8VHI3.
    Bgeei Q8VHI3.
    CleanExi MM_POFUT2.
    Genevestigatori Q8VHI3.

    Family and domain databases

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

    Publicationsi

    1. "C21orf80, a new gene from the 21q22.3 region: using RNAi to get insight into the function."
      Menzel O., Reymond A., Antonarakis S.E., Guipponi M.
      Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
    3. "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] OF 1-119.
      Strain: C57BL/6J.
      Tissue: Tongue.
    4. "O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulation."
      Du J., Takeuchi H., Leonhard-Melief C., Shroyer K.R., Dlugosz M., Haltiwanger R.S., Holdener B.C.
      Dev. Biol. 346:25-38(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION, MUTAGENESIS OF GLU-396.

    Entry informationi

    Entry nameiOFUT2_MOUSE
    AccessioniPrimary (citable) accession number: Q8VHI3
    Secondary accession number(s): Q8VEM2, Q9CV66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 2002
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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