UniProtKB - Q9Y117 (GALT3_DROME)
Protein
Polypeptide N-acetylgalactosaminyltransferase 3
Gene
Pgant3
Organism
Drosophila melanogaster (Fruit fly)
Status
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 (PubMed:12829714). 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. Has weak activity toward Muc5AC-3, -13 and -3/13 substrates (PubMed:12829714). Plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface (PubMed:18835818, PubMed:20371600, PubMed:20807760, PubMed:22157008). Might have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure (PubMed:20807760). Together with Pgant35A, regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles (PubMed:25253852).6 Publications
Catalytic activityi
- L-seryl-[protein] + UDP-N-acetyl-α-D-galactosamine = 3-O-[N-acetyl-α-D-galactosaminyl]-L-seryl-[protein] + H+ + UDP1 PublicationEC:2.4.1.411 Publication
- L-threonyl-[protein] + UDP-N-acetyl-α-D-galactosamine = 3-O-[N-acetyl-α-D-galactosaminyl]-L-threonyl-[protein] + H+ + UDP1 PublicationEC:2.4.1.411 Publication
Cofactori
Mn2+By similarity
: protein glycosylation Pathwayi
This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 PublicationView all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 190 | SubstrateBy similarity | 1 | |
Binding sitei | 220 | SubstrateBy similarity | 1 | |
Metal bindingi | 243 | ManganeseBy similarity | 1 | |
Metal bindingi | 245 | ManganeseBy similarity | 1 | |
Binding sitei | 352 | SubstrateBy similarity | 1 | |
Metal bindingi | 380 | ManganeseBy similarity | 1 | |
Binding sitei | 383 | SubstrateBy similarity | 1 | |
Binding sitei | 388 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- acetylgalactosaminyltransferase activity Source: FlyBase
- carbohydrate binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB
- transferase activity, transferring glycosyl groups Source: FlyBase
GO - Biological processi
- cell-substrate adhesion Source: FlyBase
- extracellular matrix constituent secretion Source: FlyBase
- O-glycan processing Source: FlyBase
- oligosaccharide biosynthetic process Source: UniProtKB
- protein O-linked glycosylation Source: FlyBase
- regulation of cell adhesion mediated by integrin Source: FlyBase
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Ligand | Lectin, Manganese, Metal-binding |
Enzyme and pathway databases
BRENDAi | 2.4.1.41, 1994 |
Reactomei | R-DME-190372, FGFR3c ligand binding and activation R-DME-913709, O-linked glycosylation of mucins |
UniPathwayi | UPA00378 |
Protein family/group databases
CAZyi | CBM13, Carbohydrate-Binding Module Family 13 GT27, Glycosyltransferase Family 27 |
Names & Taxonomyi
Protein namesi | Recommended name: Polypeptide N-acetylgalactosaminyltransferase 3 (EC:2.4.1.411 Publication)Short name: pp-GaNTase 3 Alternative name(s): Protein-UDP acetylgalactosaminyltransferase 3 UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3 |
Gene namesi | Name:Pgant3Imported ORF Names:CG4445Imported |
Organismi | Drosophila melanogaster (Fruit fly) |
Taxonomic identifieri | 7227 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora › |
Proteomesi |
|
Organism-specific databases
FlyBasei | FBgn0027558, Pgant3 |
Subcellular locationi
Golgi apparatus
- Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication
Golgi apparatus
- Golgi apparatus Source: FlyBase
- Golgi membrane Source: UniProtKB-SubCell
- Golgi stack Source: UniProtKB
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 12 | CytoplasmicSequence analysisAdd BLAST | 12 | |
Transmembranei | 13 – 35 | Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST | 23 | |
Topological domaini | 36 – 667 | LumenalSequence analysisAdd BLAST | 632 |
Keywords - Cellular componenti
Golgi apparatus, MembranePathology & Biotechi
Disruption phenotypei
Mutant larval wing disks show a decrease in thickness and in the content of O-glycoproteins specifically along the basal surface of the columnar epithelial cells (PubMed:18835818, PubMed:20371600). Adult mutants display blistered wings (PubMed:18835818, PubMed:20371600). Mutant larval shows down-regulation of synaptic O-linked glycosylation, integrin level and signaling via Ten-m and if. Synapses show smaller synaptic boutons, expanded activity-dependent postsynaptic pockets which affect synaptic plasticity and synaptic strength in both the pre-synaptic and post-synaptic assembly, no differences in neuromuscular junction morphology (PubMed:25253852). Simultaneous knockout of Pgant35A, restores normal synaptic strength (PubMed:25253852). RNAi-mediated knockdown in the developing wing results in a blistered phenotype (PubMed:22157008).4 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 130 | R → C: Does not affect subcellular location. Loss of catalytic activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000059157 | 1 – 667 | Polypeptide N-acetylgalactosaminyltransferase 3Add BLAST | 667 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 75 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 129 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 140 ↔ 375 | PROSITE-ProRule annotation | ||
Glycosylationi | 279 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 313 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 366 ↔ 446 | PROSITE-ProRule annotation | ||
Glycosylationi | 433 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 526 ↔ 547 | PROSITE-ProRule annotation | ||
Disulfide bondi | 572 ↔ 601 | PROSITE-ProRule annotation | ||
Glycosylationi | 590 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 626 ↔ 649 | PROSITE-ProRule annotation |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PaxDbi | Q9Y117 |
PRIDEi | Q9Y117 |
Expressioni
Tissue specificityi
Expressed in developing oocytes and egg chambers. During embryonic stages 9-11, expressed in the primordiums of the foregut, midgut and hindgut. During embryonic stages 12-13, expression is found uniquely in the posterior spiracle. During embryonic stages 14-17, expressed in the pharynx, esophagus and posterior spiracles. Expression observed in the epidermis during embryonic stages 16-17. In third instar larvae, expressed ubiquitously in wing, with increased expression in pleura and notum, eye-antennal, leg and haltere imaginal disks.2 Publications
Developmental stagei
Expressed both maternally and zygotically. Expressed throughout embryonic, larval, pupal and adult stages.2 Publications
Gene expression databases
Bgeei | FBgn0027558, Expressed in embryo and 50 other tissues |
Genevisiblei | Q9Y117, DM |
Interactioni
Protein-protein interaction databases
BioGRIDi | 61516, 8 interactors |
IntActi | Q9Y117, 2 interactors |
STRINGi | 7227.FBpp0088130 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 513 – 661 | Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST | 149 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 149 – 259 | Catalytic subdomain AAdd BLAST | 111 | |
Regioni | 321 – 383 | Catalytic subdomain BAdd BLAST | 63 |
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
Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3736, Eukaryota |
HOGENOMi | CLU_013477_0_1_1 |
InParanoidi | Q9Y117 |
OMAi | FAFFMFA |
OrthoDBi | 606683at2759 |
PhylomeDBi | Q9Y117 |
Family and domain databases
CDDi | cd00161, RICIN, 1 hit |
Gene3Di | 3.90.550.10, 1 hit |
InterProi | View protein in InterPro IPR001173, Glyco_trans_2-like IPR029044, Nucleotide-diphossugar_trans IPR035992, Ricin_B-like_lectins IPR000772, Ricin_B_lectin |
Pfami | View protein in Pfam PF00535, Glycos_transf_2, 1 hit PF00652, Ricin_B_lectin, 1 hit |
SMARTi | View protein in SMART SM00458, RICIN, 1 hit |
SUPFAMi | SSF50370, SSF50370, 1 hit SSF53448, SSF53448, 1 hit |
PROSITEi | View protein in PROSITE PS50231, RICIN_B_LECTIN, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9Y117-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGLRFQQLKK LWLLYLFLLF FAFFMFAISI NLYVASIQGG DAEMRHPKPP
60 70 80 90 100
PKRRSLWPHK NIVAHYIGKG DIFGNMTADD YNINLFQPIN GEGADGRPVV
110 120 130 140 150
VPPRDRFRMQ RFFRLNSFNL LASDRIPLNR TLKDYRTPEC RDKKYASGLP
160 170 180 190 200
STSVIIVFHN EAWSVLLRTI TSVINRSPRH LLKEIILVDD ASDRSYLKRQ
210 220 230 240 250
LESYVKVLAV PTRIFRMKKR SGLVPARLLG AENARGDVLT FLDAHCECSR
260 270 280 290 300
GWLEPLLSRI KESRKVVICP VIDIISDDNF SYTKTFENHW GAFNWQLSFR
310 320 330 340 350
WFSSDRKRQT AGNSSKDSTD PIATPGMAGG LFAIDRKYFY EMGSYDSNMR
360 370 380 390 400
VWGGENVEMS FRIWQCGGRV EISPCSHVGH VFRSSTPYTF PGGMSEVLTD
410 420 430 440 450
NLARAATVWM DDWQYFIMLY TSGLTLGAKD KVNVTERVAL RERLQCKPFS
460 470 480 490 500
WYLENIWPEH FFPAPDRFFG KIIWLDGETE CAQAYSKHMK NLPGRALSRE
510 520 530 540 550
WKRAFEEIDS KAEELMALID LERDKCLRPL KEDVPRSSLS AVTVGDCTSH
560 570 580 590 600
AQSMDMFVIT PKGQIMTNDN VCLTYRQQKL GVIKMLKNRN ATTSNVMLAQ
610 620 630 640 650
CASDSSQLWT YDMDTQQISH RDTKLCLTLK AATNSRLQKV EKVVLSMECD
660
FKDITQKWGF IPLPWRM
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE013599 Genomic DNA Translation: AAF59298.1 AF145655 mRNA Translation: AAD38630.1 |
RefSeqi | NP_610256.1, NM_136412.4 |
Genome annotation databases
EnsemblMetazoai | FBtr0089061; FBpp0088130; FBgn0027558 |
GeneIDi | 35627 |
KEGGi | dme:Dmel_CG4445 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE013599 Genomic DNA Translation: AAF59298.1 AF145655 mRNA Translation: AAD38630.1 |
RefSeqi | NP_610256.1, NM_136412.4 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
BioGRIDi | 61516, 8 interactors |
IntActi | Q9Y117, 2 interactors |
STRINGi | 7227.FBpp0088130 |
Protein family/group databases
CAZyi | CBM13, Carbohydrate-Binding Module Family 13 GT27, Glycosyltransferase Family 27 |
Proteomic databases
PaxDbi | Q9Y117 |
PRIDEi | Q9Y117 |
Genome annotation databases
EnsemblMetazoai | FBtr0089061; FBpp0088130; FBgn0027558 |
GeneIDi | 35627 |
KEGGi | dme:Dmel_CG4445 |
Organism-specific databases
CTDi | 35627 |
FlyBasei | FBgn0027558, Pgant3 |
Phylogenomic databases
eggNOGi | KOG3736, Eukaryota |
HOGENOMi | CLU_013477_0_1_1 |
InParanoidi | Q9Y117 |
OMAi | FAFFMFA |
OrthoDBi | 606683at2759 |
PhylomeDBi | Q9Y117 |
Enzyme and pathway databases
UniPathwayi | UPA00378 |
BRENDAi | 2.4.1.41, 1994 |
Reactomei | R-DME-190372, FGFR3c ligand binding and activation R-DME-913709, O-linked glycosylation of mucins |
Miscellaneous databases
BioGRID-ORCSi | 35627, 0 hits in 1 CRISPR screen |
ChiTaRSi | pgant3, fly |
GenomeRNAii | 35627 |
PROi | PR:Q9Y117 |
Gene expression databases
Bgeei | FBgn0027558, Expressed in embryo and 50 other tissues |
Genevisiblei | Q9Y117, DM |
Family and domain databases
CDDi | cd00161, RICIN, 1 hit |
Gene3Di | 3.90.550.10, 1 hit |
InterProi | View protein in InterPro IPR001173, Glyco_trans_2-like IPR029044, Nucleotide-diphossugar_trans IPR035992, Ricin_B-like_lectins IPR000772, Ricin_B_lectin |
Pfami | View protein in Pfam PF00535, Glycos_transf_2, 1 hit PF00652, Ricin_B_lectin, 1 hit |
SMARTi | View protein in SMART SM00458, RICIN, 1 hit |
SUPFAMi | SSF50370, SSF50370, 1 hit SSF53448, SSF53448, 1 hit |
PROSITEi | View protein in PROSITE PS50231, RICIN_B_LECTIN, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | GALT3_DROME | |
Accessioni | Q9Y117Primary (citable) accession number: Q9Y117 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 16, 2004 |
Last sequence update: | November 1, 1999 | |
Last modified: | April 7, 2021 | |
This is version 149 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Drosophila annotation project |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Drosophila
Drosophila: entries, gene names and cross-references to FlyBase - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families