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Q8IA41

- GLT11_DROME

UniProt

Q8IA41 - GLT11_DROME

Protein

Putative polypeptide N-acetylgalactosaminyltransferase 11

Gene

pgant11

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor.By similarity

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

    Cofactori

    Manganese.By similarity

    Pathwayi

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. oligosaccharide biosynthetic process Source: UniProtKB
    2. protein glycosylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative polypeptide N-acetylgalactosaminyltransferase 11 (EC:2.4.1.41)
    Short name:
    pp-GaNTase 11
    Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 11
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
    Gene namesi
    Name:pgant11
    ORF Names:CG7579
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0036528. CG7579.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 557557Putative polypeptide N-acetylgalactosaminyltransferase 11PRO_0000059165Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi99 ↔ 325PROSITE-ProRule annotation
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi316 ↔ 397PROSITE-ProRule annotation
    Glycosylationi379 – 3791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi437 ↔ 450PROSITE-ProRule annotation
    Disulfide bondi472 ↔ 486PROSITE-ProRule annotation
    Disulfide bondi511 ↔ 526PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ8IA41.

    Expressioni

    Gene expression databases

    BgeeiQ8IA41.

    Interactioni

    Protein-protein interaction databases

    STRINGi7227.FBpp0075334.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IA41.
    SMRiQ8IA41. Positions 65-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini28 – 557530LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2723Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini456 – 557102Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni109 – 215107Catalytic subdomain AAdd
    BLAST
    Regioni271 – 33363Catalytic subdomain BAdd
    BLAST

    Domaini

    There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.By similarity
    The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.By similarity

    Sequence similaritiesi

    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiKOG3736.
    InParanoidiQ8IA41.
    KOiK00710.
    OrthoDBiEOG7R56S5.
    PhylomeDBiQ8IA41.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view]
    SMARTiSM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8IA41-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSLLFGTPC SCAIFILVYC IITLFIWFLY TDNLSNAIVD FEYFSIKNLG    50
    ELGKEAHLQM TETDLVDAQL QNEKYQYNAW LSERIPLKRT LEDYRDPQCL 100
    KINYSSEKTV TVSIVIAIQQ EHPHTLLRGI YSVITQTSPY LLKEIVLVHD 150
    GHPDLDLIRH IHHKLPIVIQ LEMESSKGII HARLTGAGVA TGDILVFLNG 200
    HMEVTRGWLP PLLEPILLNN QTVTEPIVDA ISRESFAYRK LVEPEQLAFD 250
    WQLDHIFLPL DQHSWNSLPK PYPSSQLEGR VFAIDRKWFW HLGGWDEGLR 300
    DYGGDALELS LKVWQCGGLI LAVPCSRVGI IYKRDELEAQ MAPNRNPSLQ 350
    VQKNFKRVVD VWLDEYKLHF YRYNPKLRNL TAESLDKPRD LRRRLNCKSF 400
    EWYRSQVAPQ IRNHFLHAGL TNYPIGKIMP FVAPHFCLSI KGGFPVIRKC 450
    HSTNFEDWTL TSRCQLKHGN MCLDVDYKNN VRATKCTKKL SKNPWHYNYQ 500
    HSSFVSNGNK CLQIDVNKVG LILSACDSDV TEQRWMFTKV QDFKLDHMRD 550
    ICLSVNH 557
    Length:557
    Mass (Da):64,539
    Last modified:March 1, 2003 - v1
    Checksum:iB6F58FBAF8DB5F75
    GO

    Sequence cautioni

    The sequence AAF49588.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF326979 Genomic DNA. Translation: AAO13781.1.
    AE014296 Genomic DNA. Translation: AAF49588.1. Different initiation.
    RefSeqiNP_648799.1. NM_140542.2.
    UniGeneiDm.27150.

    Genome annotation databases

    GeneIDi39714.
    KEGGidme:Dmel_CG7579.
    UCSCiCG7579-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF326979 Genomic DNA. Translation: AAO13781.1 .
    AE014296 Genomic DNA. Translation: AAF49588.1 . Different initiation.
    RefSeqi NP_648799.1. NM_140542.2.
    UniGenei Dm.27150.

    3D structure databases

    ProteinModelPortali Q8IA41.
    SMRi Q8IA41. Positions 65-537.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7227.FBpp0075334.

    Protein family/group databases

    CAZyi CBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    Proteomic databases

    PRIDEi Q8IA41.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 39714.
    KEGGi dme:Dmel_CG7579.
    UCSCi CG7579-RA. d. melanogaster.

    Organism-specific databases

    FlyBasei FBgn0036528. CG7579.

    Phylogenomic databases

    eggNOGi KOG3736.
    InParanoidi Q8IA41.
    KOi K00710.
    OrthoDBi EOG7R56S5.
    PhylomeDBi Q8IA41.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    GenomeRNAii 39714.
    NextBioi 815008.

    Gene expression databases

    Bgeei Q8IA41.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF00535. Glycos_transf_2. 1 hit.
    PF00652. Ricin_B_lectin. 1 hit.
    [Graphical view ]
    SMARTi SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila."
      Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R., Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H.
      J. Biol. Chem. 277:22623-22638(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.

    Entry informationi

    Entry nameiGLT11_DROME
    AccessioniPrimary (citable) accession number: Q8IA41
    Secondary accession number(s): Q9VUT5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Caution

    Although strongly related to polypeptide N-acetylgalactosaminyltransferase proteins, it lacks the conserved Asp-Xaa-His motif in positions 199-201 and the conserved His residue in position 330. This suggests that it may have lost its activity.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3