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Q6WV17

- GALT5_DROME

UniProt

Q6WV17 - GALT5_DROME

Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene

pgant5

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 94 (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 EA2 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 sitei227 – 2271SubstrateBy similarity
    Binding sitei257 – 2571SubstrateBy similarity
    Metal bindingi280 – 2801ManganeseBy similarity
    Metal bindingi282 – 2821ManganeseBy similarity
    Binding sitei387 – 3871SubstrateBy similarity
    Metal bindingi415 – 4151ManganeseBy similarity
    Binding sitei418 – 4181SubstrateBy similarity
    Binding sitei423 – 4231SubstrateBy 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 5 (EC:2.4.1.41)
    Short name:
    pp-GaNTase 5
    Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 5
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
    Gene namesi
    Name:pgant5
    ORF Names:CG31651
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0031681. pgant5.

    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 – 630630Polypeptide N-acetylgalactosaminyltransferase 5PRO_0000059159Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi177 ↔ 410PROSITE-ProRule annotation
    Disulfide bondi401 ↔ 479PROSITE-ProRule annotation
    Disulfide bondi513 ↔ 530PROSITE-ProRule annotation
    Disulfide bondi553 ↔ 568PROSITE-ProRule annotation
    Disulfide bondi594 ↔ 611PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ6WV17.

    Expressioni

    Tissue specificityi

    Expressed during oogenesis, in the somatically derived follicle cells that surround the developing oocyte, which are involved in the maturation of the oocyte and construction of the egg shell, as well as playing a role in subsequent embryonic pattern formation. 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 14-17, expressed in the hindgut and the posterior spiracles. Expression is also detected in the epidermis and antennomaxillary complex at embryonic stages 16-17. In third instar larvae, ubiquitously expressed in wing, eye-antennal, leg and haltere imaginal disks.2 Publications

    Developmental stagei

    Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development. Transcripts are first detected during embryonic stages 9-11.2 Publications

    Gene expression databases

    BgeeiQ6WV17.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6WV17.
    SMRiQ6WV17. Positions 166-623.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini39 – 630592LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei21 – 3818Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini500 – 622123Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni186 – 296111Catalytic subdomain AAdd
    BLAST
    Regioni356 – 41863Catalytic 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.
    GeneTreeiENSGT00750000117385.
    InParanoidiQ6WV17.
    KOiK00710.
    OMAiETFEYMA.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ6WV17.

    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q6WV17-1) [UniParc]FASTAAdd to Basket

    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

    MTFSTFTRKM RGRMRSNTCR IVLLTSLVWV IFDFVLIARY SDCIGKDGWR    50
    CKRSGEYDVE LPNAERLVDD NQLVDDNEIN TEKSLDGESG GALIMGQGFA 100
    SGGISMTYPS VVLKKWFLAP SVQEAKGKPG EMGKPVKIPA DMKDLMKEKF 150
    KENQFNLLAS DMISLNRSLT DVRHEGCRRK HYASKLPTTS IVIVFHNEAW 200
    TTLLRTVWSV INRSPRALLK EIILVDDASE RDFLGKQLEE YVAKLPVKTF 250
    VLRTEKRSGL IRARLLGAEH VSGEVITFLD AHCECTEGWL EPLLARIVQN 300
    RRTVVCPIID VISDETFEYI TASDSTWGGF NWKLNFRWYR VPSREMARRN 350
    NDRTAPLRTP TMAGGLFSID KDYFYEIGSY DEGMDIWGGE NLEMSFRIWQ 400
    CGGILEIIPC SHVGHVFRDK SPYTFPGGVA KIVLHNAARV AEVWLDEWRD 450
    FYYSMSTGAR KASAGDVSDR KALRDRLKCK SFRWYLENVY PESLMPLDYY 500
    YLGEIRNAET ETCLDTMGRK YNEKVGISYC HGLGGNQVFA YTKRQQIMSD 550
    DLCLDASSSN GPVNMVRCHN MGGNQEWVYD AEEKWIRHTN TGQCLQRATR 600
    DDANTPLLRP CSYGKGQQWL MESKFKWQAH 630
    Length:630
    Mass (Da):72,097
    Last modified:August 16, 2004 - v2
    Checksum:iA822748C9EC96175
    GO
    Isoform B (identifier: Q6WV17-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         398-457: IWQCGGILEI...WRDFYYSMST → VWMCGGVLEI...WKEFYYSFYP

    Note: No experimental confirmation available.

    Show »
    Length:630
    Mass (Da):72,214
    Checksum:i51E9F2F0F41525AE
    GO

    Sequence cautioni

    The sequence AAL25377.1 differs from that shown. Reason: Erroneous termination at position 29. Translated as Trp.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti591 – 5911T → S in AAQ56702. (PubMed:12829714)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei398 – 45760IWQCG…YSMST → VWMCGGVLEIAPCSRVGHVF RKSTPYTFPGGTTEIVNHNN ARLVEVWLDDWKEFYYSFYP in isoform B. CuratedVSP_034631Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF52218.2.
    AE014134 Genomic DNA. Translation: ABI31292.1.
    AY060338 mRNA. Translation: AAL25377.1. Sequence problems.
    AY268066 mRNA. Translation: AAQ56702.1.
    RefSeqiNP_001036338.1. NM_001042873.2. [Q6WV17-2]
    NP_608906.2. NM_135062.4. [Q6WV17-1]
    UniGeneiDm.4033.

    Genome annotation databases

    EnsemblMetazoaiFBtr0079026; FBpp0078663; FBgn0031681. [Q6WV17-1]
    GeneIDi326151.
    KEGGidme:Dmel_CG31651.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF52218.2 .
    AE014134 Genomic DNA. Translation: ABI31292.1 .
    AY060338 mRNA. Translation: AAL25377.1 . Sequence problems.
    AY268066 mRNA. Translation: AAQ56702.1 .
    RefSeqi NP_001036338.1. NM_001042873.2. [Q6WV17-2 ]
    NP_608906.2. NM_135062.4. [Q6WV17-1 ]
    UniGenei Dm.4033.

    3D structure databases

    ProteinModelPortali Q6WV17.
    SMRi Q6WV17. Positions 166-623.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Proteomic databases

    PaxDbi Q6WV17.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0079026 ; FBpp0078663 ; FBgn0031681 . [Q6WV17-1 ]
    GeneIDi 326151.
    KEGGi dme:Dmel_CG31651.

    Organism-specific databases

    CTDi 326151.
    FlyBasei FBgn0031681. pgant5.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117385.
    InParanoidi Q6WV17.
    KOi K00710.
    OMAi ETFEYMA.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q6WV17.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.41. 1994.

    Miscellaneous databases

    ChiTaRSi pgant5. drosophila.
    GenomeRNAii 326151.
    NextBioi 847327.
    PROi Q6WV17.

    Gene expression databases

    Bgeei Q6WV17.

    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: Head.
    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: NUCLEOTIDE SEQUENCE [MRNA] OF 14-630 (ISOFORM A), ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: Canton-S.
      Tissue: Embryo.
    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 nameiGALT5_DROME
    AccessioniPrimary (citable) accession number: Q6WV17
    Secondary accession number(s): Q0E8T2, Q95T43, Q9VMU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 94 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