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Q8MYY6

- GLT13_DROME

UniProt

Q8MYY6 - GLT13_DROME

Protein

Putative polypeptide N-acetylgalactosaminyltransferase 13

Gene

pgant13

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      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 sitei150 – 1501SubstrateBy similarity
    Binding sitei186 – 1861SubstrateBy similarity
    Metal bindingi209 – 2091ManganeseBy similarity
    Binding sitei210 – 2101SubstrateBy similarity
    Metal bindingi211 – 2111ManganeseBy similarity
    Binding sitei312 – 3121SubstrateBy similarity
    Metal bindingi340 – 3401ManganeseBy similarity
    Binding sitei343 – 3431SubstrateBy similarity
    Binding sitei346 – 3461SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. multicellular organism reproduction Source: FlyBase
    2. oligosaccharide biosynthetic process Source: UniProtKB
    3. 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 13 (EC:2.4.1.41)
    Short name:
    pp-GaNTase 13
    Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 13
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
    Gene namesi
    Name:pgant13
    ORF Names:CG10000
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0039596. CG10000.

    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 – 558558Putative polypeptide N-acetylgalactosaminyltransferase 13PRO_0000059167Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi97 ↔ 335PROSITE-ProRule annotation
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi326 ↔ 412PROSITE-ProRule annotation
    Disulfide bondi445 ↔ 460PROSITE-ProRule annotation
    Disulfide bondi484 ↔ 498PROSITE-ProRule annotation
    Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi525 ↔ 539PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ8MYY6.

    Expressioni

    Tissue specificityi

    During embryonic stages 16-17, very weak expression in the midgut.

    Developmental stagei

    Transcripts first detected during embryonic stages 16-17.

    Gene expression databases

    BgeeiQ8MYY6.

    Interactioni

    Protein-protein interaction databases

    STRINGi7227.FBpp0084684.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8MYY6.
    SMRiQ8MYY6. Positions 74-552.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini33 – 558526LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3220Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini422 – 556135Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni109 – 225117Catalytic subdomain AAdd
    BLAST
    Regioni281 – 34363Catalytic 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

    eggNOGiNOG81400.
    GeneTreeiENSGT00670000097647.
    InParanoidiQ8MYY6.
    KOiK00710.
    OMAiWGGESIE.
    OrthoDBiEOG7QVM26.
    PhylomeDBiQ8MYY6.

    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.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8MYY6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHAGGKYCGP RHCSFYIIAF LICQLFFLVI FIRNDDASSA NELLSFMNES    50
    EESDHLDWRV FISHTPETSE DFYQYNIHLS NALGLIRKLP VTRHHSCTTR 100
    NSILPAPLEA NVSVVISFHN EARSMLLRTI VSLLSRSPED YLHELILVDD 150
    GSQRDVTLLD DLKRWMGGVF GSRYRLGLTF LRNQERMGLI WSRNRGASLA 200
    SGRYVLFLDS HCEVNEGWLE PLLERLALNT NLAVSPLLDP IDPTTLSYRK 250
    GNELLKGGFD WSLHFHWLKR QLTNQESLEM PYQSPAFAGG VLMMSREWFL 300
    KLGSFNPYLK IWGGESIELA IKLWLCGGQI EIVPCSRIGH IFRRRHAFDF 350
    PPQSDRQLSP AQETYLHNSK IIAESWLDEY KNMFYALRPA ARRIPLDHTY 400
    DELQRMRKER RCHPFEWYLR HVSPELRMHF DELSATGTLR NEDRCVHARQ 450
    KDSQPILASC YLSDITQWSM LRQSGQLSTH RELCLAVGFG MRIALEPCGR 500
    NETVRRSQRW VRLGTHLLHA ESHLCLDNPL KDRLEMSTCR SHAVSQSFQF 550
    ALEMEGQT 558
    Length:558
    Mass (Da):64,626
    Last modified:August 16, 2004 - v2
    Checksum:iB9CB8EDB60F8D245
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti171 – 1711G → E in AAM29489. (PubMed:12537569)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF56810.2.
    AY113484 mRNA. Translation: AAM29489.1.
    RefSeqiNP_651630.3. NM_143373.3.
    UniGeneiDm.13252.

    Genome annotation databases

    EnsemblMetazoaiFBtr0085315; FBpp0084684; FBgn0039596.
    GeneIDi43394.
    KEGGidme:Dmel_CG10000.
    UCSCiCG10000-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014297 Genomic DNA. Translation: AAF56810.2 .
    AY113484 mRNA. Translation: AAM29489.1 .
    RefSeqi NP_651630.3. NM_143373.3.
    UniGenei Dm.13252.

    3D structure databases

    ProteinModelPortali Q8MYY6.
    SMRi Q8MYY6. Positions 74-552.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7227.FBpp0084684.

    Protein family/group databases

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

    Proteomic databases

    PaxDbi Q8MYY6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0085315 ; FBpp0084684 ; FBgn0039596 .
    GeneIDi 43394.
    KEGGi dme:Dmel_CG10000.
    UCSCi CG10000-RA. d. melanogaster.

    Organism-specific databases

    FlyBasei FBgn0039596. CG10000.

    Phylogenomic databases

    eggNOGi NOG81400.
    GeneTreei ENSGT00670000097647.
    InParanoidi Q8MYY6.
    KOi K00710.
    OMAi WGGESIE.
    OrthoDBi EOG7QVM26.
    PhylomeDBi Q8MYY6.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    GenomeRNAii 43394.
    NextBioi 833701.

    Gene expression databases

    Bgeei Q8MYY6.

    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.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF53448. SSF53448. 1 hit.
    PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.

    Entry informationi

    Entry nameiGLT13_DROME
    AccessioniPrimary (citable) accession number: Q8MYY6
    Secondary accession number(s): Q9VAT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 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