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Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

GalNAc-T1

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

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 sitei189SubstrateBy similarity1
Binding sitei221SubstrateBy similarity1
Metal bindingi244ManganeseBy similarity1
Metal bindingi246ManganeseBy similarity1
Binding sitei358SubstrateBy similarity1
Metal bindingi386ManganeseBy similarity1
Binding sitei389SubstrateBy similarity1
Binding sitei392SubstrateBy similarity1
Binding sitei394SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • oligosaccharide biosynthetic process Source: UniProtKB
  • protein glycosylation Source: UniProtKB-UniPathway

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandLectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 1994.
ReactomeiR-DME-913709. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 1 (EC:2.4.1.41)
Short name:
pp-GaNTase 1
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 1
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
Gene namesi
Name:GalNAc-T1
Synonyms:pgant1
ORF Names:CG8182
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0034025. GalNAc-T1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 7CytoplasmicSequence analysis7
Transmembranei8 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini29 – 601LumenalSequence analysisAdd BLAST573

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591551 – 601Polypeptide N-acetylgalactosaminyltransferase 1Add BLAST601

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi127N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi138 ↔ 381PROSITE-ProRule annotation
Disulfide bondi372 ↔ 450PROSITE-ProRule annotation
Disulfide bondi485 ↔ 504PROSITE-ProRule annotation
Disulfide bondi528 ↔ 546PROSITE-ProRule annotation
Disulfide bondi571 ↔ 588PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ6WV20.
PRIDEiQ6WV20.

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 throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development.2 Publications

Gene expression databases

BgeeiFBgn0034025.
ExpressionAtlasiQ6WV20. differential.
GenevisibleiQ6WV20. DM.

Interactioni

Protein-protein interaction databases

BioGridi62452. 2 interactors.
IntActiQ6WV20. 3 interactors.
MINTiMINT-977265.
STRINGi7227.FBpp0086464.

Structurei

3D structure databases

ProteinModelPortaliQ6WV20.
SMRiQ6WV20.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini472 – 600Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST129

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni148 – 260Catalytic subdomain AAdd BLAST113
Regioni327 – 389Catalytic 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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
InParanoidiQ6WV20.
KOiK00710.
OMAiYFWEVGS.
OrthoDBiEOG091G085O.
PhylomeDBiQ6WV20.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiView protein in InterPro
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
PfamiView protein in Pfam
PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
SMARTiView protein in SMART
SM00458. RICIN. 1 hit.
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiView protein in PROSITE
PS50231. RICIN_B_LECTIN. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6WV20-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPRFRSFYG KLIIFILVAL CFILYSKVQQ NGSPEEPPVA PLVRAAALRG
60 70 80 90 100
HGRERFEAYS DSENEIARPA TQSPYEQIIQ LDLQKQKVGL GEQGVAVHLS
110 120 130 140 150
GAAKERGDEI YKKIALNEEL SEQLTYNRSV GDHRNPLCAK QRFDSDSLPT
160 170 180 190 200
ASVVIIFFNE PYSVLLRTVH STLSTCNEKA LKEIILVDDG SDNVELGAKL
210 220 230 240 250
DYYVRTRIPS GKVTILRLKN RLGLIRARLA GARIATGDVL IFLDAHCEGN
260 270 280 290 300
IGWCEPLLQR IKESRTSVLV PIIDVIDAND FQYSTNGYKS FQVGGFQWNG
310 320 330 340 350
HFDWINLPER EKQRQRRECK QEREICPAYS PTMAGGLFAI DRRYFWEVGS
360 370 380 390 400
YDEQMDGWGG ENLEMSFRIW QCGGTIETIP CSRVGHIFRD FHPYKFPNDR
410 420 430 440 450
DTHGINTARM ALVWMDEYIN IFFLNRPDLK FHADIGDVTH RVMLRKKLRC
460 470 480 490 500
KSFEWYLKNI YPEKFVPTKD VQGWGKVHAV NSNICLDDLL QNNEKPYNAG
510 520 530 540 550
LYPCGKVLQK SQLFSFTNTN VLRNELSCAT VQHSESPPYR VVMVPCMEND
560 570 580 590 600
EFNEQWRYEH QHIIHSNTGM CLDHQGLKSL DDAQVAPCDP HSESQRWTIE

H
Length:601
Mass (Da):68,961
Last modified:August 16, 2004 - v2
Checksum:i81BAF81E04C35BC2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti146D → E in AAQ56699 (PubMed:12829714).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY268063 mRNA. Translation: AAQ56699.1.
AF218236 mRNA. Translation: AAG13184.1.
AE013599 Genomic DNA. Translation: AAM70974.1.
AY113411 mRNA. Translation: AAM29416.1.
RefSeqiNP_611043.1. NM_137199.3.
NP_725472.1. NM_166099.2.
UniGeneiDm.3404.

Genome annotation databases

EnsemblMetazoaiFBtr0087331; FBpp0086464; FBgn0034025.
FBtr0087332; FBpp0086465; FBgn0034025.
GeneIDi36717.
KEGGidme:Dmel_CG8182.

Similar proteinsi

Entry informationi

Entry nameiGALT1_DROME
AccessioniPrimary (citable) accession number: Q6WV20
Secondary accession number(s): Q0E964, Q9V7C8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: September 27, 2017
This is version 119 of the entry and version 2 of the sequence. See 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