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Q6WV19

- GALT2_DROME

UniProt

Q6WV19 - GALT2_DROME

Protein

Polypeptide N-acetylgalactosaminyltransferase 2

Gene

pgant2

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 87 (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 sitei242 – 2421SubstrateBy similarity
    Binding sitei267 – 2671SubstrateBy similarity
    Metal bindingi290 – 2901ManganeseBy similarity
    Binding sitei291 – 2911SubstrateBy similarity
    Metal bindingi292 – 2921ManganeseBy similarity
    Binding sitei397 – 3971SubstrateBy similarity
    Metal bindingi425 – 4251ManganeseBy similarity
    Binding sitei428 – 4281SubstrateBy similarity
    Binding sitei431 – 4311SubstrateBy similarity
    Binding sitei433 – 4331SubstrateBy 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 2 (EC:2.4.1.41)
    Short name:
    pp-GaNTase 2
    Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 2
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
    Gene namesi
    Name:pgant2
    ORF Names:CG3254
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0031530. pgant2.

    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 – 633633Polypeptide N-acetylgalactosaminyltransferase 2PRO_0000059156Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi192 ↔ 420PROSITE-ProRule annotation
    Disulfide bondi411 ↔ 489PROSITE-ProRule annotation
    Disulfide bondi521 ↔ 538PROSITE-ProRule annotation
    Disulfide bondi561 ↔ 578PROSITE-ProRule annotation
    Disulfide bondi602 ↔ 618PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ6WV19.
    PRIDEiQ6WV19.

    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 during embryonic, larval, pupal and adult stages. Weakly expressed in the male and female body and correspondingly low levels during early embryonic stages. Significantly expressed from embryonic stage 8-12 hours and reaches maximal levels in the pupae and male head.2 Publications

    Gene expression databases

    BgeeiQ6WV19.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6WV19.
    SMRiQ6WV19. Positions 170-629.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini26 – 633608LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini508 – 630123Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni201 – 306106Catalytic subdomain AAdd
    BLAST
    Regioni366 – 42863Catalytic subdomain BAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi67 – 14175Gly-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.
    HOGENOMiHOG000281220.
    InParanoidiQ6WV19.
    KOiK00710.
    OMAiDDYSDNP.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ6WV19.

    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.

    Q6WV19-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRNIKLIVF VSIIWMFVMV YYFQSSTEKV ENRALRLREV ATAMQQYQDD    50
    SSSAAAASTA RQWAPAGGGA GPGAAAGAAG SGADDPGGNV ILIGSVKDFE 100
    RNAVHGLKLN GIVALEETSQ GLSGGTGGPG GRLPVAPSGR GTEVEYFNEA 150
    GYIRAGALRN GEDPYIRNRF NQEASDALPS NRDIPDTRNP MCRTKKYRED 200
    LPETSVIITF HNEARSTLLR TIVSVLNRSP EHLIREIVLV DDYSDHPEDG 250
    LELAKIDKVR VIRNDKREGL VRSRVKGADA AVSSVLTFLD SHVECNEMWL 300
    EPLLERVRED PTRVVCPVID VISMDNFQYI GASADLRGGF DWNLIFKWEY 350
    LSPSERAMRH NDPTTAIRTP MIAGGLFVID KAYFNKLGKY DMKMDVWGGE 400
    NLEISFRVWQ CGGSLEIIPC SRVGHVFRKR HPYTFPGGSG NVFARNTRRA 450
    AEVWMDDYKQ HYYNAVPLAK NIPFGNIDDR LALKEKLHCK PFKWYLENVY 500
    PDLQAPDPQE VGQFRQDSTE CLDTMGHLID GTVGIFPCHN TGGNQEWAFT 550
    KRGEIKHDDL CLTLVTFARG SQVVLKACDD SENQRWIMRE GGLVRHYKIN 600
    VCLDSRDQSQ QGVSAQHCNS ALGTQRWSFG KYA 633
    Length:633
    Mass (Da):70,736
    Last modified:August 16, 2004 - v2
    Checksum:i8DA64F627BCB08DB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1341P → L in AAQ56700. (PubMed:12829714)Curated
    Sequence conflicti617 – 6171H → R in AAQ22499. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF51113.3.
    BT010030 mRNA. Translation: AAQ22499.1.
    AY268064 mRNA. Translation: AAQ56700.1.
    RefSeqiNP_608773.2. NM_134929.3.
    NP_995625.2. NM_205903.2.
    UniGeneiDm.11992.

    Genome annotation databases

    EnsemblMetazoaiFBtr0077592; FBpp0099799; FBgn0031530.
    FBtr0303992; FBpp0292961; FBgn0031530.
    GeneIDi33556.
    KEGGidme:Dmel_CG3254.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014134 Genomic DNA. Translation: AAF51113.3 .
    BT010030 mRNA. Translation: AAQ22499.1 .
    AY268064 mRNA. Translation: AAQ56700.1 .
    RefSeqi NP_608773.2. NM_134929.3.
    NP_995625.2. NM_205903.2.
    UniGenei Dm.11992.

    3D structure databases

    ProteinModelPortali Q6WV19.
    SMRi Q6WV19. Positions 170-629.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Proteomic databases

    PaxDbi Q6WV19.
    PRIDEi Q6WV19.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0077592 ; FBpp0099799 ; FBgn0031530 .
    FBtr0303992 ; FBpp0292961 ; FBgn0031530 .
    GeneIDi 33556.
    KEGGi dme:Dmel_CG3254.

    Organism-specific databases

    CTDi 33556.
    FlyBasei FBgn0031530. pgant2.

    Phylogenomic databases

    eggNOGi NOG239675.
    GeneTreei ENSGT00750000117385.
    HOGENOMi HOG000281220.
    InParanoidi Q6WV19.
    KOi K00710.
    OMAi DDYSDNP.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q6WV19.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.41. 1994.

    Miscellaneous databases

    GenomeRNAii 33556.
    NextBioi 784182.
    PROi Q6WV19.

    Gene expression databases

    Bgeei Q6WV19.

    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: NUCLEOTIDE SEQUENCE [MRNA] OF 19-633, 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 nameiGALT2_DROME
    AccessioniPrimary (citable) accession number: Q6WV19
    Secondary accession number(s): Q7KU27, Q7YU21, Q9VQQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 87 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