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Q8WR51

- OFUT2_CAEEL

UniProt

Q8WR51 - OFUT2_CAEEL

Protein

GDP-fucose protein O-fucosyltransferase 2

Gene

pad-2

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (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.By similarity

    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 sitei52 – 521Proton donor/acceptorBy similarity
    Binding sitei290 – 2901SubstrateBy similarity
    Sitei391 – 3911Essential for catalytic activityBy similarity

    GO - Molecular functioni

    1. peptide-O-fucosyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. fucose metabolic process Source: UniProtKB-KW
    2. protein O-linked fucosylation Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism

    Enzyme and pathway databases

    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):
    Patterning defective protein 2
    Peptide-O-fucosyltransferase 2
    Short name:
    O-FucT-2
    Gene namesi
    Name:pad-2
    ORF Names:K10G9.3
    OrganismiCaenorhabditis elegansImported
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome III

    Organism-specific databases

    WormBaseiK10G9.3a; CE31715; WBGene00010757; pad-2.

    Subcellular locationi

    Endoplasmic reticulum By similarity. Golgi apparatus 1 Publication
    Note: Mainly located in the endoplasmic reticulum.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 424404GDP-fucose protein O-fucosyltransferase 2PRO_0000012157Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi154 ↔ 187By similarity
    Glycosylationi205 – 2051N-linked (GlcNAc...)1 Publication
    Disulfide bondi407 ↔ 414By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ8WR51.

    Expressioni

    Tissue specificityi

    Expressed in the anterior part of embryos, in the hypodermal and neuronal cells of the head. Expressed at different levels in a variety of cell types after hatching, including neuronal, hypodermal, muscle, intestinal, and somatic gonadal cells. Expressed in the nerve ring around the pharynx, in dorsal and ventral nerve cords, intestine, and a variety of hypodermal cells of L1-L3 larvae. Expressed in gonadal sheath cells, spermatheca, and tissues surrounding the vulva of adult hermaphrodites, and in the body wall muscle and hypodermal cells of adults of both sexes.1 Publication

    Developmental stagei

    Expressed starts at morphogenetic embryonic stages and continues throughout development.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi6239.K10G9.3.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8WR51.
    SMRiQ8WR51. Positions 39-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 544Substrate bindingBy similarity
    Regioni383 – 3842Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyltransferase 68 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG77810.
    GeneTreeiENSGT00390000007989.
    HOGENOMiHOG000015874.
    InParanoidiQ8WR51.
    KOiK03691.
    PhylomeDBiQ8WR51.

    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.

    Q8WR51-1 [UniParc]FASTAAdd to Basket

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    MHFFPIQLLV LFFAEKIAFA ENSDQTVSRV DSNRYSVAAE KKFLLYDVNF    50
    GEGFNLRRDV YMRVANTVRS LRDSGENYIL VLPPWGRLHH WKRMEVALSW 100
    RLFFDLESLN RFIPVIEFED FLDENRPIDQ VIYLQHYAEG WGTEYVRKFE 150
    KRSCLPPAES HYKQVEEFKW KGWFYSYEDV YSRNFQCVSI QGDSGTLKDL 200
    LKHSNFSEST SIMVDRAETI LHEHYGEVDY WKARRSMRYS NDLVDVADAF 250
    RKKYLDSDDK RDKTKLVDDW TKEKPRRTAI GGPYLGIHWR RRDFLYARRA 300
    QLPTIPGTAK ILQDLCKKLD LQKIYLATDA PDQEVDELKA LLNGELEVYR 350
    FTDTQKLNDG QIAIIDQYLC AHAAYFIGSY ESTFTFRIQE DREIIGFPIS 400
    TTFNRLCPDT EPTCEQPAKW KIVY 424
    Length:424
    Mass (Da):50,106
    Last modified:March 1, 2002 - v1
    Checksum:i2A35F5FC04EF70B3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF455271 mRNA. Translation: AAL65193.1.
    Z36282 Genomic DNA. Translation: CAD45602.1.
    RefSeqiNP_001255070.1. NM_001268141.1.
    UniGeneiCel.9168.

    Genome annotation databases

    EnsemblMetazoaiK10G9.3a; K10G9.3a; WBGene00010757.
    GeneIDi259529.
    KEGGicel:CELE_K10G9.3.
    UCSCiK10G9.3. c. elegans.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF455271 mRNA. Translation: AAL65193.1 .
    Z36282 Genomic DNA. Translation: CAD45602.1 .
    RefSeqi NP_001255070.1. NM_001268141.1.
    UniGenei Cel.9168.

    3D structure databases

    ProteinModelPortali Q8WR51.
    SMRi Q8WR51. Positions 39-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 6239.K10G9.3.

    Protein family/group databases

    CAZyi GT68. Glycosyltransferase Family 68.

    Proteomic databases

    PaxDbi Q8WR51.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai K10G9.3a ; K10G9.3a ; WBGene00010757 .
    GeneIDi 259529.
    KEGGi cel:CELE_K10G9.3.
    UCSCi K10G9.3. c. elegans.

    Organism-specific databases

    CTDi 259529.
    WormBasei K10G9.3a ; CE31715 ; WBGene00010757 ; pad-2.

    Phylogenomic databases

    eggNOGi NOG77810.
    GeneTreei ENSGT00390000007989.
    HOGENOMi HOG000015874.
    InParanoidi Q8WR51.
    KOi K03691.
    PhylomeDBi Q8WR51.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    NextBioi 952052.
    PROi Q8WR51.

    Family and domain databases

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

    Publicationsi

    1. "The Caenorhabditis elegans ortholog of C21orf80, a potential new protein O-fucosyltransferase, is required for normal development."
      Menzel O., Vellai T., Takacs-Vellai K., Reymond A., Mueller F., Antonarakis S.E., Guipponi M.
      Genomics 84:320-330(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.
    3. "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
      Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
      Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Bristol N2.

    Entry informationi

    Entry nameiOFUT2_CAEEL
    AccessioniPrimary (citable) accession number: Q8WR51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2002
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3