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Protein

Polypeptide N-acetylgalactosaminyltransferase 3

Gene

pgant3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Has weak activity toward Muc5AC-3, -13 and -3/13 substrates. 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.2 Publications

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

Cofactori

Mn2+By similarity

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei190SubstrateBy similarity1
Binding sitei220SubstrateBy similarity1
Metal bindingi243ManganeseBy similarity1
Metal bindingi245ManganeseBy similarity1
Binding sitei352SubstrateBy similarity1
Metal bindingi380ManganeseBy similarity1
Binding sitei383SubstrateBy similarity1
Binding sitei388SubstrateBy similarity1

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
Complete GO annotation...

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 3 (EC:2.4.1.41)
Short name:
pp-GaNTase 3
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Gene namesi
Name:pgant3
ORF Names:CG4445
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0027558. pgant3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
Transmembranei13 – 35Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini36 – 667LumenalSequence analysisAdd BLAST632

GO - Cellular componenti

  • Golgi apparatus Source: FlyBase
  • Golgi membrane Source: UniProtKB-SubCell
  • Golgi stack Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & 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. Adult mutants display blistered wings.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi130R → C: Does not affect subcellular location. Loss of catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591571 – 667Polypeptide N-acetylgalactosaminyltransferase 3Add BLAST667

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi75N-linked (GlcNAc...)Sequence analysis1
Glycosylationi129N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi140 ↔ 375PROSITE-ProRule annotation
Glycosylationi279N-linked (GlcNAc...)Sequence analysis1
Glycosylationi313N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi366 ↔ 446PROSITE-ProRule annotation
Glycosylationi433N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi526 ↔ 547PROSITE-ProRule annotation
Disulfide bondi572 ↔ 601PROSITE-ProRule annotation
Glycosylationi590N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi626 ↔ 649PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9Y117.
PRIDEiQ9Y117.

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

BgeeiFBgn0027558.
GenevisibleiQ9Y117. DM.

Interactioni

Protein-protein interaction databases

BioGridi61516. 5 interactors.
IntActiQ9Y117. 2 interactors.
MINTiMINT-336298.
STRINGi7227.FBpp0088130.

Structurei

3D structure databases

ProteinModelPortaliQ9Y117.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini513 – 661Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST149

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni149 – 259Catalytic subdomain AAdd BLAST111
Regioni321 – 383Catalytic subdomain BAdd BLAST63

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

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
InParanoidiQ9Y117.
KOiK00710.
OMAiMFAISIN.
OrthoDBiEOG091G085O.
PhylomeDBiQ9Y117.

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.

Q9Y117-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:667
Mass (Da):76,807
Last modified:November 1, 1999 - v1
Checksum:iB8C6924AA8E19805
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF59298.1.
AF145655 mRNA. Translation: AAD38630.1.
RefSeqiNP_610256.1. NM_136412.4.
UniGeneiDm.3144.

Genome annotation databases

EnsemblMetazoaiFBtr0089061; FBpp0088130; FBgn0027558.
GeneIDi35627.
KEGGidme:Dmel_CG4445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF59298.1.
AF145655 mRNA. Translation: AAD38630.1.
RefSeqiNP_610256.1. NM_136412.4.
UniGeneiDm.3144.

3D structure databases

ProteinModelPortaliQ9Y117.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61516. 5 interactors.
IntActiQ9Y117. 2 interactors.
MINTiMINT-336298.
STRINGi7227.FBpp0088130.

Protein family/group databases

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

Proteomic databases

PaxDbiQ9Y117.
PRIDEiQ9Y117.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089061; FBpp0088130; FBgn0027558.
GeneIDi35627.
KEGGidme:Dmel_CG4445.

Organism-specific databases

CTDi35627.
FlyBaseiFBgn0027558. pgant3.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
InParanoidiQ9Y117.
KOiK00710.
OMAiMFAISIN.
OrthoDBiEOG091G085O.
PhylomeDBiQ9Y117.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 1994.

Miscellaneous databases

ChiTaRSipgant3. fly.
GenomeRNAii35627.
PROiQ9Y117.

Gene expression databases

BgeeiFBgn0027558.
GenevisibleiQ9Y117. DM.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiGALT3_DROME
AccessioniPrimary (citable) accession number: Q9Y117
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 120 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.