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Protein

N-acetylgalactosaminyltransferase 6

Gene

pgant6

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 sitei242SubstrateBy similarity1
Binding sitei272SubstrateBy similarity1
Metal bindingi295ManganeseBy similarity1
Binding sitei296SubstrateBy similarity1
Metal bindingi297ManganeseBy similarity1
Binding sitei398SubstrateBy similarity1
Metal bindingi426ManganeseBy similarity1
Binding sitei429SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • oligosaccharide biosynthetic process Source: UniProtKB
  • protein glycosylation Source: UniProtKB-UniPathway
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 6 (EC:2.4.1.-)
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 6
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6
Short name:
pp-GaNTase 6
Gene namesi
Name:pgant6
ORF Names:CG2103
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0035375. pgant6.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 11CytoplasmicSequence analysisAdd BLAST11
Transmembranei12 – 31Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini32 – 666LumenalSequence analysisAdd BLAST635

GO - Cellular componenti

  • endoplasmic reticulum 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591601 – 666N-acetylgalactosaminyltransferase 6Add BLAST666

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi181N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi192 ↔ 421PROSITE-ProRule annotation
Glycosylationi285N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi412 ↔ 491PROSITE-ProRule annotation
Disulfide bondi531 ↔ 548PROSITE-ProRule annotation
Disulfide bondi577 ↔ 594PROSITE-ProRule annotation
Disulfide bondi621 ↔ 636PROSITE-ProRule annotation
Glycosylationi651N-linked (GlcNAc...)Sequence analysis1
Glycosylationi657N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ6WV16.
PRIDEiQ6WV16.

Expressioni

Tissue specificityi

Expressed during oogenesis, in the somatically derived follicle cells that surround the developing oocyte, which are involved in the maturation of the oocyte and construction of the egg shell, as well as playing a role in subsequent embryonic pattern formation. Expressed in the salivary glands from embryonic stage 12 onwards, becoming stronger at stage 13. During embryonic stages 12-13, also expressed in the posterior midgut and hindgut. During embryonic stages 14-15, expression continues in the hindgut. Expression is detected in the epidermis and antennomaxillary complex during embryonic stages 16-17. In third instar larvae, ubiquitously expressed in wing, eye-antennal, leg and haltere imaginal disks.2 Publications

Developmental stagei

Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development. Transcripts first detected during embryonic stages 12-13.2 Publications

Gene expression databases

BgeeiFBgn0035375.
ExpressionAtlasiQ6WV16. baseline.
GenevisibleiQ6WV16. DM.

Interactioni

Protein-protein interaction databases

BioGridi63848. 4 interactors.
MINTiMINT-877547.
STRINGi7227.FBpp0072842.

Structurei

3D structure databases

ProteinModelPortaliQ6WV16.
SMRiQ6WV16.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini518 – 648Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST131

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni201 – 311Catalytic subdomain AAdd BLAST111
Regioni367 – 429Catalytic 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.
InParanoidiQ6WV16.
KOiK00710.
OMAiQKKTFFL.
OrthoDBiEOG091G085O.
PhylomeDBiQ6WV16.

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.

Q6WV16-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRPNLKWIV KASLLLLISL TLFVLITSWI SSTPYTNKPV HHGVEPVPEK
60 70 80 90 100
AGLSGDVKVK VPAIKQPEPQ KPQEPDFEED PELQKIDEPE PVEEEVDNPH
110 120 130 140 150
PADDEPQQQP QEELQMAAPA DASVKKDWHD YTFMEKDAKR VGLGEGGKAS
160 170 180 190 200
TLDDESQRDL EKRMSLENGF NALLSDSISV NRSVPDIRHP LCRKKEYVAK
210 220 230 240 250
LPTVSVIIIF YNEYLSVLMR SVHSLINRSP PELMKEIILV DDHSDREYLG
260 270 280 290 300
KELETYIAEH FKWVRVVRLP RRTGLIGARA AGARNATAEV LIFLDSHVEA
310 320 330 340 350
NYNWLPPLLE PIALNKRTAV CPFIDVIDHT NFHYRAQDEG ARGAFDWEFF
360 370 380 390 400
YKRLPLLPED LKHPADPFKS PIMAGGLFAI SREFFWELGG YDEGLDIWGG
410 420 430 440 450
EQYELSFKIW MCGGEMYDAP CSRIGHIYRG PRNHQPSPRK GDYLHKNYKR
460 470 480 490 500
VAEVWMDEYK NYLYSHGDGL YESVDPGDLT EQKAIRTKLN CKSFKWFMEE
510 520 530 540 550
VAFDLMKTYP PVDPPSYAMG ALQNVGNQNL CLDTLGRKKH NKMGMYACAD
560 570 580 590 600
NIKTPQRTQF WELSWKRDLR LRRKKECLDV QIWDANAPVW LWDCHSQGGN
610 620 630 640 650
QYWYYDYRHK QLKHGTEGRR CLELLPFSQE VVANKCDTDN RFQQWNFGSF
660
NKTALDNYSQ DLVLSL
Length:666
Mass (Da):76,972
Last modified:August 16, 2004 - v2
Checksum:iCAECA6CE4860600C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti95 – 96EV → DA in AAQ56703 (PubMed:12829714).Curated2
Sequence conflicti107Q → R in AAQ56703 (PubMed:12829714).Curated1
Sequence conflicti107Q → R in AAL29177 (PubMed:12537569).Curated1
Sequence conflicti499E → K in AAL29177 (PubMed:12537569).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY268067 mRNA. Translation: AAQ56703.1.
AE014296 Genomic DNA. Translation: AAF47689.1.
AE014296 Genomic DNA. Translation: AAF47690.1.
AY061629 mRNA. Translation: AAL29177.1.
RefSeqiNP_001261342.1. NM_001274413.1.
NP_647749.2. NM_139492.3.
NP_728779.1. NM_167966.2.
UniGeneiDm.3519.

Genome annotation databases

EnsemblMetazoaiFBtr0072972; FBpp0072842; FBgn0035375.
FBtr0072973; FBpp0072843; FBgn0035375.
FBtr0333442; FBpp0305633; FBgn0035375.
GeneIDi38346.
KEGGidme:Dmel_CG2103.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY268067 mRNA. Translation: AAQ56703.1.
AE014296 Genomic DNA. Translation: AAF47689.1.
AE014296 Genomic DNA. Translation: AAF47690.1.
AY061629 mRNA. Translation: AAL29177.1.
RefSeqiNP_001261342.1. NM_001274413.1.
NP_647749.2. NM_139492.3.
NP_728779.1. NM_167966.2.
UniGeneiDm.3519.

3D structure databases

ProteinModelPortaliQ6WV16.
SMRiQ6WV16.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63848. 4 interactors.
MINTiMINT-877547.
STRINGi7227.FBpp0072842.

Protein family/group databases

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

Proteomic databases

PaxDbiQ6WV16.
PRIDEiQ6WV16.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072972; FBpp0072842; FBgn0035375.
FBtr0072973; FBpp0072843; FBgn0035375.
FBtr0333442; FBpp0305633; FBgn0035375.
GeneIDi38346.
KEGGidme:Dmel_CG2103.

Organism-specific databases

CTDi38346.
FlyBaseiFBgn0035375. pgant6.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
InParanoidiQ6WV16.
KOiK00710.
OMAiQKKTFFL.
OrthoDBiEOG091G085O.
PhylomeDBiQ6WV16.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii38346.
PROiQ6WV16.

Gene expression databases

BgeeiFBgn0035375.
ExpressionAtlasiQ6WV16. baseline.
GenevisibleiQ6WV16. 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 nameiGALT6_DROME
AccessioniPrimary (citable) accession number: Q6WV16
Secondary accession number(s): Q0E8I9, Q95R40, Q9VZX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: November 30, 2016
This is version 108 of the entry and version 2 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.