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Q8IA43

- GLT10_DROME

UniProt

Q8IA43 - GLT10_DROME

Protein

Putative polypeptide N-acetylgalactosaminyltransferase 10

Gene

pgant10

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 84 (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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei207 – 2071SubstrateBy similarity
    Binding sitei238 – 2381SubstrateBy similarity
    Metal bindingi261 – 2611ManganeseBy similarity
    Binding sitei262 – 2621SubstrateBy similarity
    Metal bindingi263 – 2631ManganeseBy similarity
    Binding sitei363 – 3631SubstrateBy similarity
    Metal bindingi391 – 3911ManganeseBy similarity

    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 10 (EC:2.4.1.41)
    Short name:
    pp-GaNTase 10
    Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 10
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
    Gene namesi
    Name:pgant10
    ORF Names:CG31776
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0051776. CG31776.

    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 – 630630Putative polypeptide N-acetylgalactosaminyltransferase 10PRO_0000059164Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi157 ↔ 386PROSITE-ProRule annotation
    Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi377 ↔ 456PROSITE-ProRule annotation
    Disulfide bondi496 ↔ 513PROSITE-ProRule annotation
    Glycosylationi525 – 5251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi543 ↔ 559PROSITE-ProRule annotation
    Disulfide bondi586 ↔ 606PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ8IA43.

    Expressioni

    Tissue specificityi

    During embryonic stages 9-11, weakly expressed in the mesoderm. During embryonic stages 12-13, very weak expression is observed in the somatic mesoderm region. No expression detected from stage 14-15. During embryonic stages 16-17, expressed in the epidermis and the antennomaxillary complex. In third instar larvae, expressed ubiquitously in wing, eye-antennal, leg and haltere imaginal disks.1 Publication

    Developmental stagei

    Expressed both maternally and zygotically. Expressed throughout embryonic and larval stages.1 Publication

    Gene expression databases

    BgeeiQ8IA43.

    Interactioni

    Protein-protein interaction databases

    STRINGi7227.FBpp0077211.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8IA43.
    SMRiQ8IA43. Positions 93-615.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini27 – 630604LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2620Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini483 – 618136Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni166 – 277112Catalytic subdomain AAdd
    BLAST
    Regioni333 – 39462Catalytic 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

    eggNOGiNOG254892.
    GeneTreeiENSGT00740000115054.
    InParanoidiQ8IA43.
    KOiK00710.
    OMAiNALECKT.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ8IA43.

    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.

    Q8IA43-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVDLRLIVR LLLAILLTSL VTTILMGKQI HRRLVKSMVK TTGEKDSLPA    50
    RQLPKREISP KVADFPPPLT LNQTELDILK IQRNNSFRLP QQEAIKEWQD 100
    AIFFKEDSNR RGLGEQGRAV QLPNAKLNPD DFQDFYAELS DRIPLNRSLP 150
    DTRPISCRKR KYLENLPNVT VIIAFHDEHL SVLLRSITSI INRSPVELLK 200
    QIVLVDDDSN LPELGQQLEE IVAQNFPKII HILRLPERRG SIKARMEAIR 250
    VSSCQVLVFL DSHIEVNTNW LPPLLEPIVI NPHIVTRPIL DAISRKTFAY 300
    AKQNTMTRSG FNWWLESESL PIFPEDKSPD STPYRTPVLS GAMAIDRNYF 350
    LNLGGFDEQL DTWEAEKFEI SFKVWMCGGM MLYVPCARVG HIGKRPMKSI 400
    SSPGYHNFLA RNYKRVAEVW MDNYKKYVYD KNPKLYKMAN AGLLFQRKTK 450
    RNALECKTFD WYMTKVAPDF LKRYLALDSP LVFSGVIESV AFPGFCVDSL 500
    NCRHTKPVVL ARCTGHNSMP GEHQNWSLTQ DHEIQLTNSK DDCLEAQGLR 550
    SKSVWLFRCH KNGGNQYWYY NHRHRWIQQG QIWVWCLEAQ LASGHKVGKV 600
    LANKICDKNQ LEQQWKVGRN APYDPQREPH 630
    Length:630
    Mass (Da):72,795
    Last modified:March 1, 2003 - v1
    Checksum:i7E2748165A9293CA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF324751 mRNA. Translation: AAN75750.1.
    AE014134 Genomic DNA. Translation: AAF51101.3.
    BT022827 mRNA. Translation: AAY55243.1.
    RefSeqiNP_722909.2. NM_164538.4.
    UniGeneiDm.14884.

    Genome annotation databases

    EnsemblMetazoaiFBtr0077522; FBpp0077211; FBgn0051776.
    GeneIDi33568.
    KEGGidme:Dmel_CG31776.
    UCSCiCG31776-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF324751 mRNA. Translation: AAN75750.1 .
    AE014134 Genomic DNA. Translation: AAF51101.3 .
    BT022827 mRNA. Translation: AAY55243.1 .
    RefSeqi NP_722909.2. NM_164538.4.
    UniGenei Dm.14884.

    3D structure databases

    ProteinModelPortali Q8IA43.
    SMRi Q8IA43. Positions 93-615.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7227.FBpp0077211.

    Protein family/group databases

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

    Proteomic databases

    PRIDEi Q8IA43.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0077522 ; FBpp0077211 ; FBgn0051776 .
    GeneIDi 33568.
    KEGGi dme:Dmel_CG31776.
    UCSCi CG31776-RA. d. melanogaster.

    Organism-specific databases

    FlyBasei FBgn0051776. CG31776.

    Phylogenomic databases

    eggNOGi NOG254892.
    GeneTreei ENSGT00740000115054.
    InParanoidi Q8IA43.
    KOi K00710.
    OMAi NALECKT.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q8IA43.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    GenomeRNAii 33568.
    NextBioi 784234.

    Gene expression databases

    Bgeei Q8IA43.

    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 [MRNA].
    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.
    4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
    5. "Expression of the UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase family is spatially and temporally regulated during Drosophila development."
      Tian E., Ten Hagen K.G.
      Glycobiology 16:83-95(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiGLT10_DROME
    AccessioniPrimary (citable) accession number: Q8IA43
    Secondary accession number(s): Q4V529, Q9VQR4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    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