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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei218 – 2181SubstrateBy similarity
Binding sitei249 – 2491SubstrateBy similarity
Metal bindingi272 – 2721ManganeseBy similarity
Binding sitei273 – 2731SubstrateBy similarity
Metal bindingi274 – 2741ManganeseBy similarity
Binding sitei376 – 3761SubstrateBy similarity
Metal bindingi404 – 4041ManganeseBy similarity
Binding sitei407 – 4071SubstrateBy similarity

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.
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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence analysisAdd
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini35 – 644610LumenalSequence analysisAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 644644N-acetylgalactosaminyltransferase 4PRO_0000059158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence analysis
Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence analysis
Disulfide bondi509 ↔ 526PROSITE-ProRule annotation
Glycosylationi529 – 5291N-linked (GlcNAc...)Sequence analysis
Disulfide bondi556 ↔ 573PROSITE-ProRule annotation
Glycosylationi565 – 5651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi600 ↔ 617PROSITE-ProRule annotation
Glycosylationi632 – 6321N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8IA42.

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. differential.
GenevisibleiQ8IA42. DM.

Interactioni

Protein-protein interaction databases

IntActiQ8IA42. 1 interaction.
STRINGi7227.FBpp0305447.

Structurei

3D structure databases

ProteinModelPortaliQ8IA42.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini496 – 629134Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 288112Catalytic subdomain ABy similarityAdd
BLAST
Regioni345 – 40763Catalytic subdomain BBy similarityAdd
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

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
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

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8IA42. 1 interaction.
STRINGi7227.FBpp0305447.

Protein family/group databases

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

Proteomic databases

PaxDbiQ8IA42.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi261610.
KEGGidme:Dmel_CG31956.

Organism-specific databases

CTDi261610.
FlyBaseiFBgn0051956. pgant4.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 1994.

Miscellaneous databases

GenomeRNAii261610.
PROiQ8IA42.

Gene expression databases

BgeeiFBgn0051956.
ExpressionAtlasiQ8IA42. differential.
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: September 7, 2016
This is version 103 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.