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Q9VUT6

- GALT8_DROME

UniProt

Q9VUT6 - GALT8_DROME

Protein

Polypeptide N-acetylgalactosaminyltransferase 8

Gene

pgant8

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 95 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalyzes 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. It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels fro Muc5AC-3/13.

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei168 – 1681SubstrateBy similarity
    Metal bindingi220 – 2201ManganeseBy similarity
    Binding sitei221 – 2211SubstrateBy similarity
    Metal bindingi222 – 2221ManganeseBy similarity
    Binding sitei322 – 3221SubstrateBy similarity
    Metal bindingi350 – 3501ManganeseBy similarity
    Binding sitei353 – 3531SubstrateBy 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:
    Polypeptide N-acetylgalactosaminyltransferase 8 (EC:2.4.1.41)
    Short name:
    pp-GaNTase 8
    Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 8
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8
    Gene namesi
    Name:pgant8
    ORF Names:CG7297
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0036529. pgant8.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 590590Polypeptide N-acetylgalactosaminyltransferase 8PRO_0000059162Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi117 ↔ 345PROSITE-ProRule annotation
    Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi336 ↔ 419PROSITE-ProRule annotation
    Disulfide bondi459 ↔ 475PROSITE-ProRule annotation
    Disulfide bondi502 ↔ 517PROSITE-ProRule annotation
    Disulfide bondi546 ↔ 561PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9VUT6.
    PRIDEiQ9VUT6.

    Expressioni

    Tissue specificityi

    Expressed in developing oocytes and egg chambers. During embryonic stages 9-11, expressed in the primordium of the foregut, midgut and hindgut. During embryonic stages 12-13, expressed in the posterior midgut and hindgut. During embryonic stages 14-15, expression continues in the hindgut. No expression detected during embryonic stages 16-17 or in third instar larvae imaginal disks.2 Publications

    Developmental stagei

    Expressed both maternally and zygotically. Weakly expressed during early embryonic stages but increases during 12-24 hours of embryogenesis through larval development and continues to be expressed throughout adulthood, albeit at slightly lower levels in males than females.2 Publications

    Gene expression databases

    BgeeiQ9VUT6.

    Interactioni

    Protein-protein interaction databases

    STRINGi7227.FBpp0075331.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VUT6.
    SMRiQ9VUT6. Positions 50-586.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini32 – 590559LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei12 – 3120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini446 – 573128Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni127 – 236110Catalytic subdomain AAdd
    BLAST
    Regioni291 – 35363Catalytic 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

    eggNOGiNOG259651.
    GeneTreeiENSGT00740000115054.
    InParanoidiQ9VUT6.
    KOiK00710.
    OMAiHRSCKKL.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ9VUT6.

    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.

    Q9VUT6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCLDIWRHKK KVLPLLLLMA IGSIIYYLYT LKLEGERDES ATSTTSRLER    50
    DIRDLQAVFE SEVIPDLGAL GRPARGNWTE EQLEAIAKSQ RETGYNAWLS 100
    KRISPERSLY DMRHRSCKKL KYPMEKLPSV SVVITYHNEE ASVLLRTLSS 150
    LRSRTPIQLL REVILVDDGS TQADEKLNDF IKIKFLNMVQ HRRITTQVGL 200
    MHARVVGAEL ALADVLVFLD SHVEVTKGWL EPLIAPILED NRTCTTPIID 250
    TIDFDNFAYR RGKPSRGFFN WEFNYIQLPL LKEEAVAMPA PHKNPIMNGG 300
    LFAIGREWFS ELGGYDKGLK IWGAEQFELS LKLWLCGGQI LEVPCSRVGH 350
    LFRDGNFQIR YTNKDKNSEK KLISRNYRRV AEIWLDEYKD KLFANMPHLT 400
    VIPVGNLAEQ RDLKNRLHCK PFKWFLDNLA TDFLNLYPIL DPAEYASGVL 450
    QSISSPKLCL DRKDPSHGQP KLAPCSSDHV FPSPEQYWSL TNHRELRSGF 500
    YCLEVRNHGV NVHIYQCHGQ SGNQFWSFDS KTHQVISGQQ QNFRHCLEAQ 550
    PELNAVTSSV CDPKNHKQQW KFGYLNSQRL QHFWDNVKTQ 590
    Length:590
    Mass (Da):68,100
    Last modified:May 1, 2000 - v1
    Checksum:iB18B759A9FC2B021
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF49587.1.
    AY070966 mRNA. Translation: AAL48588.1.
    RefSeqiNP_648800.1. NM_140543.4.
    UniGeneiDm.6188.

    Genome annotation databases

    EnsemblMetazoaiFBtr0075578; FBpp0075331; FBgn0036529.
    GeneIDi39715.
    KEGGidme:Dmel_CG7297.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF49587.1 .
    AY070966 mRNA. Translation: AAL48588.1 .
    RefSeqi NP_648800.1. NM_140543.4.
    UniGenei Dm.6188.

    3D structure databases

    ProteinModelPortali Q9VUT6.
    SMRi Q9VUT6. Positions 50-586.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7227.FBpp0075331.

    Protein family/group databases

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

    Proteomic databases

    PaxDbi Q9VUT6.
    PRIDEi Q9VUT6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0075578 ; FBpp0075331 ; FBgn0036529 .
    GeneIDi 39715.
    KEGGi dme:Dmel_CG7297.

    Organism-specific databases

    CTDi 39715.
    FlyBasei FBgn0036529. pgant8.

    Phylogenomic databases

    eggNOGi NOG259651.
    GeneTreei ENSGT00740000115054.
    InParanoidi Q9VUT6.
    KOi K00710.
    OMAi HRSCKKL.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q9VUT6.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    GenomeRNAii 39715.
    NextBioi 815013.

    Gene expression databases

    Bgeei Q9VUT6.

    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. "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: Embryo.
    4. "Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster."
      Ten Hagen K.G., Tran D.T., Gerken T.A., Stein D.S., Zhang Z.
      J. Biol. Chem. 278:35039-35048(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    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 nameiGALT8_DROME
    AccessioniPrimary (citable) accession number: Q9VUT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 95 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