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Q8MRC9

- GALT9_DROME

UniProt

Q8MRC9 - GALT9_DROME

Protein

Putative polypeptide N-acetylgalactosaminyltransferase 9

Gene

pgant9

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 105 (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 sitei249 – 2491SubstrateBy similarity
    Binding sitei278 – 2781SubstrateBy similarity
    Metal bindingi301 – 3011ManganeseBy similarity
    Binding sitei302 – 3021SubstrateBy similarity
    Metal bindingi303 – 3031ManganeseBy similarity
    Binding sitei409 – 4091SubstrateBy similarity
    Metal bindingi437 – 4371ManganeseBy similarity
    Binding sitei440 – 4401SubstrateBy similarity
    Binding sitei445 – 4451SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. multicellular organism reproduction Source: FlyBase
    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 9 (EC:2.4.1.41)
    Short name:
    pp-GaNTase 9
    Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 9
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
    Gene namesi
    Name:pgant9
    ORF Names:CG30463
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0050463. CG30463.

    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 – 650650Putative polypeptide N-acetylgalactosaminyltransferase 9PRO_0000059163Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi198 ↔ 432PROSITE-ProRule annotation
    Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi423 ↔ 499PROSITE-ProRule annotation
    Disulfide bondi535 ↔ 554PROSITE-ProRule annotation
    Disulfide bondi577 ↔ 590PROSITE-ProRule annotation
    Disulfide bondi616 ↔ 631PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ8MRC9.

    Expressioni

    Tissue specificityi

    During embryonic stages 9-11, expressed in the developing anterior midgut and amnioserosa. Expressed in the salivary glands from embryonic stage 12 onwards. During embryonic stages 12-13, still expressed in the amnioserosa region. In third instar larvae, expressed ubiquitously in wing, with increased expression in the notum and ventral wing pouch, leg and haltere imaginal disks. In eye-antennal imaginal disk, expressed in the presumptive eye region only.1 Publication

    Developmental stagei

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

    Gene expression databases

    BgeeiQ8MRC9.

    Interactioni

    Protein-protein interaction databases

    BioGridi73174. 1 interaction.
    IntActiQ8MRC9. 1 interaction.
    MINTiMINT-964044.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8MRC9.
    SMRiQ8MRC9. Positions 147-650.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini32 – 650619LumenalSequence 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
    Domaini521 – 643123Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni208 – 317110Catalytic subdomain AAdd
    BLAST
    Regioni378 – 44063Catalytic subdomain BAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi43 – 9048Gly-richAdd
    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

    eggNOGiNOG239675.
    GeneTreeiENSGT00750000117385.
    InParanoidiQ8MRC9.
    KOiK00710.
    OMAiYNENLPR.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ8MRC9.

    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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q8MRC9-1) [UniParc]FASTAAdd to Basket

    Also known as: D

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAFIWRRRST TIVKLVAFAL AIWFCIAFLV YTDDTRRRAA QEGAGASGAG    50
    SAPGVGGGAG GLGDPIALAL RNEPAGEDFG INGNVIGGGG QKQAHDEADI 100
    PPTVGKHKAD LQAERMRKKA AEQPKKKPQE DSKKVIDPPA NFEENPGELG 150
    KPVRLPKEMS DEMKKAVDDG WTKNAFNQYV SDLISVHRTL PDPRDAWCKD 200
    EARYLTNLPK TDVIICFHNE AWTVLLRTVH SVLDRSPEHL IGKIILVDDY 250
    SDMPHLKRQL EDYFAAYPKV QIIRGQKREG LIRARILGAN HAKSPVLTYL 300
    DSHCECTEGW LEPLLDRIAR NSTTVVCPVI DVISDETLEY HYRDSGGVNV 350
    GGFDWNLQFS WHPVPERERK RHNSTAEPVY SPTMAGGLFS IDREFFDRLG 400
    TYDSGFDIWG GENLELSFKT WMCGGTLEIV PCSHVGHIFR KRSPYKWRSG 450
    VNVLKKNSVR LAEVWMDEYS QYYYHRIGND KGDWGDVSDR RKLRNDLKCK 500
    SFKWYLDNIY PELFIPGDSV AHGEIRNLGY GGRTCLDAPA GKKHQKKAVG 550
    TYPCHRQGGN QYWMLSKAGE IRRDDSCLDY AGKDVTLFGC HGGKGNQFWT 600
    YRENTKQLHH GTSGKCLAIS ESKDKLLMEE CSASLSRQQW TLENYDSSKL 650

    Note: No experimental confirmation available.

    Length:650
    Mass (Da):73,193
    Last modified:August 16, 2004 - v2
    Checksum:iAC847736AD1C07CA
    GO
    Isoform B (identifier: Q8MRC9-2) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG

    Note: No experimental confirmation available.

    Show »
    Length:647
    Mass (Da):72,860
    Checksum:iA25855E919100BFE
    GO
    Isoform E (identifier: Q8MRC9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-383: Missing.
         526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG

    Note: No experimental confirmation available.

    Show »
    Length:264
    Mass (Da):30,256
    Checksum:i06D95D4D4B3D00E8
    GO
    Isoform F (identifier: Q8MRC9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-22: AFIWRRRSTTIVKLVAFALAI → NFYLSSWHCQVTQSGLVAGLE
         23-273: Missing.
         526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG

    Note: No experimental confirmation available.

    Show »
    Length:396
    Mass (Da):45,208
    Checksum:i8AB540EC2C239DF6
    GO

    Sequence cautioni

    The sequence ABL75647.1 differs from that shown. Reason: Intron retention.
    The sequence ABL75689.1 differs from that shown. Reason: Intron retention.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451N → D in AAM51988. (PubMed:12537569)Curated
    Sequence conflicti454 – 4541L → P in AAM51988. (PubMed:12537569)Curated
    Sequence conflicti472 – 4721Y → C in AAM51988. (PubMed:12537569)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 383383Missing in isoform E. CuratedVSP_034632Add
    BLAST
    Alternative sequencei2 – 2221AFIWR…FALAI → NFYLSSWHCQVTQSGLVAGL E in isoform F. 1 PublicationVSP_034633Add
    BLAST
    Alternative sequencei23 – 273251Missing in isoform F. 1 PublicationVSP_034634Add
    BLAST
    Alternative sequencei526 – 55631RNLGY…YPCHR → ANVPNGMCLDAKEKSEEETP VSIYECHG in isoform B, isoform E and isoform F. 1 PublicationVSP_034635Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF57964.3.
    AE013599 Genomic DNA. Translation: AAF57966.2.
    AE013599 Genomic DNA. Translation: ABV53822.1.
    AE013599 Genomic DNA. Translation: ABV53823.1.
    AE013599 Genomic DNA. Translation: ABV53824.1.
    AY121661 mRNA. Translation: AAM51988.1.
    BT029588 mRNA. Translation: ABL75647.1. Sequence problems.
    BT029630 mRNA. Translation: ABL75689.1. Sequence problems.
    RefSeqiNP_001097341.1. NM_001103871.1. [Q8MRC9-2]
    NP_001097342.1. NM_001103872.1. [Q8MRC9-1]
    NP_001097343.1. NM_001103873.1. [Q8MRC9-3]
    NP_725602.1. NM_166188.1. [Q8MRC9-1]
    NP_725603.2. NM_166189.2. [Q8MRC9-2]
    UniGeneiDm.24533.

    Genome annotation databases

    EnsemblMetazoaiFBtr0087112; FBpp0086258; FBgn0050463. [Q8MRC9-1]
    FBtr0113380; FBpp0112292; FBgn0050463. [Q8MRC9-1]
    GeneIDi246627.
    KEGGidme:Dmel_CG30463.
    UCSCiCG30463-RA. d. melanogaster. [Q8MRC9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013599 Genomic DNA. Translation: AAF57964.3 .
    AE013599 Genomic DNA. Translation: AAF57966.2 .
    AE013599 Genomic DNA. Translation: ABV53822.1 .
    AE013599 Genomic DNA. Translation: ABV53823.1 .
    AE013599 Genomic DNA. Translation: ABV53824.1 .
    AY121661 mRNA. Translation: AAM51988.1 .
    BT029588 mRNA. Translation: ABL75647.1 . Sequence problems.
    BT029630 mRNA. Translation: ABL75689.1 . Sequence problems.
    RefSeqi NP_001097341.1. NM_001103871.1. [Q8MRC9-2 ]
    NP_001097342.1. NM_001103872.1. [Q8MRC9-1 ]
    NP_001097343.1. NM_001103873.1. [Q8MRC9-3 ]
    NP_725602.1. NM_166188.1. [Q8MRC9-1 ]
    NP_725603.2. NM_166189.2. [Q8MRC9-2 ]
    UniGenei Dm.24533.

    3D structure databases

    ProteinModelPortali Q8MRC9.
    SMRi Q8MRC9. Positions 147-650.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 73174. 1 interaction.
    IntActi Q8MRC9. 1 interaction.
    MINTi MINT-964044.

    Protein family/group databases

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

    Proteomic databases

    PaxDbi Q8MRC9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0087112 ; FBpp0086258 ; FBgn0050463 . [Q8MRC9-1 ]
    FBtr0113380 ; FBpp0112292 ; FBgn0050463 . [Q8MRC9-1 ]
    GeneIDi 246627.
    KEGGi dme:Dmel_CG30463.
    UCSCi CG30463-RA. d. melanogaster. [Q8MRC9-1 ]

    Organism-specific databases

    FlyBasei FBgn0050463. CG30463.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117385.
    InParanoidi Q8MRC9.
    KOi K00710.
    OMAi YNENLPR.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q8MRC9.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    ChiTaRSi CG30463. drosophila.
    GenomeRNAii 246627.
    NextBioi 843268.
    PROi Q8MRC9.

    Gene expression databases

    Bgeei Q8MRC9.

    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, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Strain: Berkeley.
      Tissue: Embryo.
    4. Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM F).
      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 nameiGALT9_DROME
    AccessioniPrimary (citable) accession number: Q8MRC9
    Secondary accession number(s): A1A6R7
    , A1A6V9, A8DYG1, A8DYG2, A8DYG3, Q0E950, Q9V7T0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 105 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