Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N-acetylgalactosaminyltransferase 4

Gene

pgant4

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

Functioni

Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. Prefers the diglycosylated Muc5AC-3/13 as substrate.

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 sitei218SubstrateBy similarity1
Binding sitei249SubstrateBy similarity1
Metal bindingi272ManganeseBy similarity1
Binding sitei273SubstrateBy similarity1
Metal bindingi274ManganeseBy similarity1
Binding sitei376SubstrateBy similarity1
Metal bindingi404ManganeseBy similarity1
Binding sitei407SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • oligosaccharide biosynthetic process Source: UniProtKB
  • positive regulation of secretion Source: FlyBase
  • protein O-linked glycosylation Source: FlyBase
  • secretory granule organization 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.
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:
N-acetylgalactosaminyltransferase 4 (EC:2.4.1.-)
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 4
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
Short name:
pp-GaNTase 4
Gene namesi
Name:pgant4
ORF Names:CG31956
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0051956. pgant4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 13CytoplasmicSequence analysisAdd BLAST13
Transmembranei14 – 34Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini35 – 644LumenalSequence analysisAdd BLAST610

GO - Cellular componenti

  • 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591581 – 644N-acetylgalactosaminyltransferase 4Add BLAST644

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi157N-linked (GlcNAc...)Sequence analysis1
Glycosylationi179N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi509 ↔ 526PROSITE-ProRule annotation
Glycosylationi529N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi556 ↔ 573PROSITE-ProRule annotation
Glycosylationi565N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi600 ↔ 617PROSITE-ProRule annotation
Glycosylationi632N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8IA42.
PRIDEiQ8IA42.

Expressioni

Tissue specificityi

Expressed in developing oocytes and egg chambers. During embryonic stages 9-11, expressed in the primordium of the foregut, midgut and hindgut. During embryonic stages 12-13, shows specific expression in the proventriculus that continues until the end of embryogenesis. In third instar larvae, ubiquitously expressed in wing, eye-antennal, leg and haltere imaginal disks.2 Publications

Developmental stagei

Expressed both maternally and zygotically. Expressed during embryonic, larval, pupal and adult stages. Weakly expressed during early embryonic stages but displays a dramatic increase at 12-24 hours of embryonic development. Continues to be in adult but displays much lower levels in the female adult as compared with the male.2 Publications

Gene expression databases

BgeeiFBgn0051956.
ExpressionAtlasiQ8IA42. baseline.
GenevisibleiQ8IA42. DM.

Interactioni

Protein-protein interaction databases

IntActiQ8IA42. 1 interactor.
STRINGi7227.FBpp0305447.

Structurei

3D structure databases

ProteinModelPortaliQ8IA42.
SMRiQ8IA42.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini496 – 629Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST134

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni177 – 288Catalytic subdomain ABy similarityAdd BLAST112
Regioni345 – 407Catalytic subdomain BBy similarityAdd 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.
InParanoidiQ8IA42.
KOiK00710.
OMAiFGFVNHT.
OrthoDBiEOG091G085O.

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.

Q8IA42-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIKKRYVKR LLRKVVLLLV VIVTVSLVTT LVVERRMKNA AELTEQLDPN
60 70 80 90 100
GDPITPVFRA ANIHPTRKAP RPPFQDRNSV VDIPRSDKLQ GFRLPEPKGE
110 120 130 140 150
RKDWHDYAAM EADRKRSGFG EHGVAVKIEN PDEKQLEKEH YEMNGFNGLI
160 170 180 190 200
SDRISVNRSV PDLRLEACKT RKYLAKLPNI SVIFIFFNEH FNTLLRSIYS
210 220 230 240 250
VINRTPPELL KQIVLVDDGS EWDVLKQPLD DYVQQHFPHL VTIVRNPERQ
260 270 280 290 300
GLIGARIAGA KVAVGQVMVF FDSHIEVNYN WLPPLIEPIA INPKISTCPM
310 320 330 340 350
VDTISHEDFS YFSGNKDGAR GGFDWKMLYK QLPVLPEDAL DKSMPYRSPV
360 370 380 390 400
MMGGLFAINT DFFWDLGGYD DQLDIWGGEQ YELSFKIWMC GGMLLDVPCS
410 420 430 440 450
RVAHIFRGPM KPRGNPRGHN FVAKNHKRVA EVWMDEYKQY VYKRDPKTYD
460 470 480 490 500
NLDAGDLTRQ RGVRERLKCK SFHWFMTEVA PDFLVKFPPV EPPSYAAGII
510 520 530 540 550
QNVANPVYCL DNMGKSTEEA VGMFSCADNR THPQPNQFWE LSIFRDLRMK
560 570 580 590 600
GFDSVCLDVH EGPPNATVWM WSCHSQGGNQ FWYYDRQTQR LVHGENNKRC
610 620 630 640
LEGFVENGIA KVVANSCENG NDRQRWEFGF VNHTMLDTFY DGLK
Length:644
Mass (Da):74,040
Last modified:March 16, 2016 - v3
Checksum:i884B9D91B4978F46
GO

Sequence cautioni

The sequence AAQ56701 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY268065 mRNA. Translation: AAQ56701.1. Different initiation.
AE014134 Genomic DNA. Translation: AAN10370.2.
AF324752 mRNA. Translation: AAN75751.1.
RefSeqiNP_001137779.1. NM_001144307.2.
NP_722910.2. NM_164539.2.
UniGeneiDm.14883.

Genome annotation databases

EnsemblMetazoaiFBtr0114524; FBpp0113016; FBgn0051956.
FBtr0333248; FBpp0305447; FBgn0051956.
GeneIDi261610.
KEGGidme:Dmel_CG31956.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY268065 mRNA. Translation: AAQ56701.1. Different initiation.
AE014134 Genomic DNA. Translation: AAN10370.2.
AF324752 mRNA. Translation: AAN75751.1.
RefSeqiNP_001137779.1. NM_001144307.2.
NP_722910.2. NM_164539.2.
UniGeneiDm.14883.

3D structure databases

ProteinModelPortaliQ8IA42.
SMRiQ8IA42.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8IA42. 1 interactor.
STRINGi7227.FBpp0305447.

Protein family/group databases

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

Proteomic databases

PaxDbiQ8IA42.
PRIDEiQ8IA42.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0114524; FBpp0113016; FBgn0051956.
FBtr0333248; FBpp0305447; FBgn0051956.
GeneIDi261610.
KEGGidme:Dmel_CG31956.

Organism-specific databases

CTDi261610.
FlyBaseiFBgn0051956. pgant4.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
InParanoidiQ8IA42.
KOiK00710.
OMAiFGFVNHT.
OrthoDBiEOG091G085O.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii261610.
PROiQ8IA42.

Gene expression databases

BgeeiFBgn0051956.
ExpressionAtlasiQ8IA42. baseline.
GenevisibleiQ8IA42. 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 nameiGALT4_DROME
AccessioniPrimary (citable) accession number: Q8IA42
Secondary accession number(s): Q8IQ11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 16, 2016
Last modified: November 30, 2016
This is version 106 of the entry and version 3 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.