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Q8MVS5

- GLT35_DROME

UniProt

Q8MVS5 - GLT35_DROME

Protein

Polypeptide N-acetylgalactosaminyltransferase 35A

Gene

Pgant35A

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      Previous versions | rss
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    Functioni

    Essential glycotransferase, which 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.

    Catalytic activityi

    UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.2 Publications

    Cofactori

    Manganese.By similarity

    Kineticsi

    1. KM=8.5 µM for UDP-GalNAc1 Publication
    2. KM=0.35 mM for EA2 acceptor peptide1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei188 – 1881SubstrateBy similarity
    Binding sitei220 – 2201SubstrateBy similarity
    Metal bindingi243 – 2431ManganeseBy similarity
    Binding sitei244 – 2441SubstrateBy similarity
    Metal bindingi245 – 2451ManganeseBy similarity
    Binding sitei348 – 3481SubstrateBy similarity
    Metal bindingi376 – 3761ManganeseBy similarity
    Binding sitei379 – 3791SubstrateBy similarity
    Binding sitei384 – 3841SubstrateBy 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. open tracheal system development Source: FlyBase
    3. protein glycosylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    SABIO-RKQ8MVS5.
    UniPathwayiUPA00378.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 35A (EC:2.4.1.41)
    Alternative name(s):
    Protein l(2)35Aa
    Protein-UDP acetylgalactosaminyltransferase 35A
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 35A
    Short name:
    pp-GaNTase 35A
    dGalNAc-T1
    Gene namesi
    Name:Pgant35A
    ORF Names:CG7480
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0001970. Pgant35A.

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi227 – 2271R → W in SF32; induces lethality. 2 Publications
    Mutagenesisi243 – 2431D → N: Abolishes glycosyltransferase activity. Not able to rescue lethality caused by SF32 mutation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 632632Polypeptide N-acetylgalactosaminyltransferase 35APRO_0000059168Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi49 – 491N-linked (GlcNAc...)1 Publication
    Glycosylationi69 – 691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi136 ↔ 371PROSITE-ProRule annotation
    Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi362 ↔ 439PROSITE-ProRule annotation
    Disulfide bondi493 ↔ 516PROSITE-ProRule annotation
    Disulfide bondi539 ↔ 553PROSITE-ProRule annotation
    Disulfide bondi580 ↔ 597PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ8MVS5.

    Expressioni

    Tissue specificityi

    Expressed at high level in ovaries. Expressed at low level in testis. Expressed at higher level in adult females than males. During oogenesis, it is detected in germ cells and follicle epithelia of all developmental stages. Initially expressed during early stages of oogenesis in region I and reaches high levels in regions IIa and IIb of the germarium. Highly expressed in stage 2 egg chambers. Remains highly expressed during later stages of oogenesis. During embryonic stages 9-11, expressed in the primordium of the foregut, midgut and hindgut. Expressed in salivary glands from embryonic stage 12 onwards. During embryonic stages 12-13, expressed in the posterior midgut and hindgut. During embryonic stages 14-15, expression continues in the hindgut. During embryonic stages 16-17, expressed in the dorsal longitudinal trachea and posterior spiracles. In third instar larvae, ubiquitously expressed in wing, eye-antennal, leg and 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.3 Publications

    Gene expression databases

    BgeeiQ8MVS5.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8MVS5.
    SMRiQ8MVS5. Positions 113-607.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini30 – 632603LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini526 – 632107Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni147 – 259113Catalytic subdomain AAdd
    BLAST
    Regioni317 – 37963Catalytic 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

    eggNOGiNOG239675.
    GeneTreeiENSGT00740000115054.
    InParanoidiQ8MVS5.
    KOiK00710.
    OMAiKCHEMGG.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ8MVS5.

    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.

    Q8MVS5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMQIKRLLCK SCGLGTLLVA VVWLLALLFY SHSLRSSIRS AGWRIDEGNA    50
    TPRAELSYQA RVTVGCTPNA SITTGESPAA PKPPSDPEQL ELLGVVRNKQ 100
    DKYIRDIGYK HHAFNALVSN NIGLFRAIPD TRHKVCDRQE TTEAENLPQA 150
    SIVMCFYNEH KMTLMRSIKT VLERTPSYLL REIILVDDHS DLPELEFHLH 200
    GDLRARLKYD NLRYIKNEQR EGLIRSRVIG AREAVGDVLV FLDSHIEVNQ 250
    QWLEPLLRLI KSENATLAVP VIDLINADTF EYTPSPLVRG GFNWGLHFRW 300
    ENLPEGTLKV PEDFRGPFRS PTMAGGLFAV NRKYFQHLGE YDMAMDIWGG 350
    ENIEISFRAW QCGGAIKIVP CSRVGHIFRK RRPYTSPDGA NTMLKNSLRL 400
    AHVWMDQYKD YYLKHEKVPK TYDYGDISDR LKLRERLQCR DFAWYLKNVY 450
    PELHVPGEES KKSAAAPIFQ PWHSRKRNYV DTFQLRLTGT ELCAAVVAPK 500
    VKGFWKKGSS LQLQTCRRTP NQLWYETEKA EIVLDKLLCL EASGDAQVTV 550
    NKCHEMLGDQ QWRHTRNANS PVYNMAKGTC LRAAAPTTGA LISLDLCSKS 600
    NGAGGSWDIV QLKKPTEAEG RAKEARNSDK AL 632
    Length:632
    Mass (Da):71,828
    Last modified:August 16, 2004 - v2
    Checksum:iE726B9F32481E4E9
    GO

    Sequence cautioni

    The sequence AAK66862.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 721I → T in AAM62405. (PubMed:11925446)Curated
    Sequence conflicti628 – 6281S → T in AAL49213. (PubMed:12537569)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF478697 mRNA. Translation: AAM62405.1.
    AF478698 Genomic DNA. Translation: AAM62406.1.
    AF478699 Genomic DNA. Translation: AAM62407.1.
    AF478700 Genomic DNA. Translation: AAM62408.1.
    AF158747 mRNA. Translation: AAK66862.1. Different initiation.
    AE014134 Genomic DNA. Translation: AAF53391.1.
    AY071591 mRNA. Translation: AAL49213.1.
    RefSeqiNP_652069.2. NM_143812.4.
    UniGeneiDm.1528.

    Genome annotation databases

    EnsemblMetazoaiFBtr0080629; FBpp0080202; FBgn0001970.
    GeneIDi48775.
    KEGGidme:Dmel_CG7480.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF478697 mRNA. Translation: AAM62405.1 .
    AF478698 Genomic DNA. Translation: AAM62406.1 .
    AF478699 Genomic DNA. Translation: AAM62407.1 .
    AF478700 Genomic DNA. Translation: AAM62408.1 .
    AF158747 mRNA. Translation: AAK66862.1 . Different initiation.
    AE014134 Genomic DNA. Translation: AAF53391.1 .
    AY071591 mRNA. Translation: AAL49213.1 .
    RefSeqi NP_652069.2. NM_143812.4.
    UniGenei Dm.1528.

    3D structure databases

    ProteinModelPortali Q8MVS5.
    SMRi Q8MVS5. Positions 113-607.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Proteomic databases

    PaxDbi Q8MVS5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0080629 ; FBpp0080202 ; FBgn0001970 .
    GeneIDi 48775.
    KEGGi dme:Dmel_CG7480.

    Organism-specific databases

    CTDi 48775.
    FlyBasei FBgn0001970. Pgant35A.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00740000115054.
    InParanoidi Q8MVS5.
    KOi K00710.
    OMAi KCHEMGG.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q8MVS5.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    SABIO-RK Q8MVS5.

    Miscellaneous databases

    GenomeRNAii 48775.
    NextBioi 839543.
    PROi Q8MVS5.

    Gene expression databases

    Bgeei Q8MVS5.

    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. "A UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster."
      Ten Hagen K.G., Tran D.T.
      J. Biol. Chem. 277:22616-22622(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, MUTAGENESIS OF ARG-227.
      Strain: Canton-S.
      Tissue: Embryo.
    2. "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], ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF ARG-227.
    3. "An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
      Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.
      , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
      Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. "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.
    5. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    7. "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.
    8. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
      Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
      Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Oregon-R.
      Tissue: Head.
    9. "Rescue of Drosophila Melanogaster l(2)35Aa lethality is only mediated by polypeptide GalNAc-transferase pgant35A, but not by the evolutionary conserved human ortholog GalNAc-transferase-T11."
      Bennett E.P., Chen Y.W., Schwientek T., Mandel U., Schjoldager K.T., Cohen S.M., Clausen H.
      Glycoconj. J. 27:435-444(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-243.

    Entry informationi

    Entry nameiGLT35_DROME
    AccessioniPrimary (citable) accession number: Q8MVS5
    Secondary accession number(s): Q8MVS2
    , Q8MVS3, Q8MVS4, Q8SYF1, Q965E4, Q9V3C9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 96 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

    The human ortholog GALNT11 (AC Q8NCW6) is not able to rescue lethality caused by the SF32 mutation.1 Publication

    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