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Q6WV20

- GALT1_DROME

UniProt

Q6WV20 - GALT1_DROME

Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

GalNAc-T1

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 91 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      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 the monoglycosylated Muc5AC-3 as substrate.

    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 sitei189 – 1891SubstrateBy similarity
    Binding sitei221 – 2211SubstrateBy similarity
    Metal bindingi244 – 2441ManganeseBy similarity
    Metal bindingi246 – 2461ManganeseBy similarity
    Binding sitei358 – 3581SubstrateBy similarity
    Metal bindingi386 – 3861ManganeseBy similarity
    Binding sitei389 – 3891SubstrateBy similarity
    Binding sitei392 – 3921SubstrateBy similarity
    Binding sitei394 – 3941SubstrateBy 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

    BRENDAi2.4.1.41. 1994.
    UniPathwayiUPA00378.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 1 (EC:2.4.1.41)
    Short name:
    pp-GaNTase 1
    Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 1
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
    Gene namesi
    Name:GalNAc-T1
    Synonyms:pgant1
    ORF Names:CG8182
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0034025. GalNAc-T1.

    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 – 601601Polypeptide N-acetylgalactosaminyltransferase 1PRO_0000059155Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi138 ↔ 381PROSITE-ProRule annotation
    Disulfide bondi372 ↔ 450PROSITE-ProRule annotation
    Disulfide bondi485 ↔ 504PROSITE-ProRule annotation
    Disulfide bondi528 ↔ 546PROSITE-ProRule annotation
    Disulfide bondi571 ↔ 588PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ6WV20.

    Expressioni

    Tissue specificityi

    Expressed in developing oocytes and egg chambers. No expression observed during embryonic stages 9-11. During embryonic stages 12-13, specific expression is observed in the developing tracheal branches and brain. During embryonic stages 14-17, expression is restricted to the dorsal longitudinal trachea. In third instar larvae imaginal wing disk, expressed in clusters of cells in the presumptive pleura and notum. In eye-antennal imaginal disk, shows a very distinct band of expression at the morphogenetic furrow and weaker expression in the presumptive eye posterior to the furrow, no expression is detected in the presumptive antennal or head region anterior to the furrow. No expression observed in leg or haltere imaginal disks.2 Publications

    Developmental stagei

    Expressed both maternally and zygotically. Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development.2 Publications

    Gene expression databases

    BgeeiQ6WV20.

    Interactioni

    Protein-protein interaction databases

    BioGridi62452. 2 interactions.
    MINTiMINT-977265.
    STRINGi7227.FBpp0086464.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6WV20.
    SMRiQ6WV20. Positions 111-597.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 77CytoplasmicSequence Analysis
    Topological domaini29 – 601573LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini472 – 600129Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni148 – 260113Catalytic subdomain AAdd
    BLAST
    Regioni327 – 38963Catalytic 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

    eggNOGiNOG302022.
    GeneTreeiENSGT00740000115054.
    InParanoidiQ6WV20.
    KOiK00710.
    OMAiREICPAY.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ6WV20.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF02709. Glyco_transf_7C. 1 hit.
    PF00535. 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.

    Q6WV20-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPRFRSFYG KLIIFILVAL CFILYSKVQQ NGSPEEPPVA PLVRAAALRG    50
    HGRERFEAYS DSENEIARPA TQSPYEQIIQ LDLQKQKVGL GEQGVAVHLS 100
    GAAKERGDEI YKKIALNEEL SEQLTYNRSV GDHRNPLCAK QRFDSDSLPT 150
    ASVVIIFFNE PYSVLLRTVH STLSTCNEKA LKEIILVDDG SDNVELGAKL 200
    DYYVRTRIPS GKVTILRLKN RLGLIRARLA GARIATGDVL IFLDAHCEGN 250
    IGWCEPLLQR IKESRTSVLV PIIDVIDAND FQYSTNGYKS FQVGGFQWNG 300
    HFDWINLPER EKQRQRRECK QEREICPAYS PTMAGGLFAI DRRYFWEVGS 350
    YDEQMDGWGG ENLEMSFRIW QCGGTIETIP CSRVGHIFRD FHPYKFPNDR 400
    DTHGINTARM ALVWMDEYIN IFFLNRPDLK FHADIGDVTH RVMLRKKLRC 450
    KSFEWYLKNI YPEKFVPTKD VQGWGKVHAV NSNICLDDLL QNNEKPYNAG 500
    LYPCGKVLQK SQLFSFTNTN VLRNELSCAT VQHSESPPYR VVMVPCMEND 550
    EFNEQWRYEH QHIIHSNTGM CLDHQGLKSL DDAQVAPCDP HSESQRWTIE 600
    H 601
    Length:601
    Mass (Da):68,961
    Last modified:August 16, 2004 - v2
    Checksum:i81BAF81E04C35BC2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti146 – 1461D → E in AAQ56699. (PubMed:12829714)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY268063 mRNA. Translation: AAQ56699.1.
    AF218236 mRNA. Translation: AAG13184.1.
    AE013599 Genomic DNA. Translation: AAM70974.1.
    AY113411 mRNA. Translation: AAM29416.1.
    RefSeqiNP_611043.1. NM_137199.3.
    NP_725472.1. NM_166099.2.
    UniGeneiDm.3404.

    Genome annotation databases

    EnsemblMetazoaiFBtr0087331; FBpp0086464; FBgn0034025.
    FBtr0087332; FBpp0086465; FBgn0034025.
    GeneIDi36717.
    KEGGidme:Dmel_CG8182.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY268063 mRNA. Translation: AAQ56699.1 .
    AF218236 mRNA. Translation: AAG13184.1 .
    AE013599 Genomic DNA. Translation: AAM70974.1 .
    AY113411 mRNA. Translation: AAM29416.1 .
    RefSeqi NP_611043.1. NM_137199.3.
    NP_725472.1. NM_166099.2.
    UniGenei Dm.3404.

    3D structure databases

    ProteinModelPortali Q6WV20.
    SMRi Q6WV20. Positions 111-597.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62452. 2 interactions.
    MINTi MINT-977265.
    STRINGi 7227.FBpp0086464.

    Protein family/group databases

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

    Proteomic databases

    PaxDbi Q6WV20.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0087331 ; FBpp0086464 ; FBgn0034025 .
    FBtr0087332 ; FBpp0086465 ; FBgn0034025 .
    GeneIDi 36717.
    KEGGi dme:Dmel_CG8182.

    Organism-specific databases

    CTDi 36717.
    FlyBasei FBgn0034025. GalNAc-T1.

    Phylogenomic databases

    eggNOGi NOG302022.
    GeneTreei ENSGT00740000115054.
    InParanoidi Q6WV20.
    KOi K00710.
    OMAi REICPAY.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q6WV20.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.41. 1994.

    Miscellaneous databases

    GenomeRNAii 36717.
    NextBioi 800028.

    Gene expression databases

    Bgeei Q6WV20.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR027791. Galactosyl_T_C.
    IPR001173. Glyco_trans_2-like.
    IPR029044. Nucleotide-diphossugar_trans.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF02709. Glyco_transf_7C. 1 hit.
    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 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: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: Canton-S.
      Tissue: Embryo.
    2. "Cloning of Drosophila protein-UDP acetylgalactosaminyltransferase."
      Farkas R., Medvedova L., Mechler B.M.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    6. "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 nameiGALT1_DROME
    AccessioniPrimary (citable) accession number: Q6WV20
    Secondary accession number(s): Q0E964, Q9V7C8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 91 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