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Protein

Putative polypeptide N-acetylgalactosaminyltransferase 9

Gene

pgant9

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

Functioni

May catalyze 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.By similarity

Catalytic activityi

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

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 sitei249SubstrateBy similarity1
Binding sitei278SubstrateBy similarity1
Metal bindingi301ManganeseBy similarity1
Binding sitei302SubstrateBy similarity1
Metal bindingi303ManganeseBy similarity1
Binding sitei409SubstrateBy similarity1
Metal bindingi437ManganeseBy similarity1
Binding sitei440SubstrateBy similarity1
Binding sitei445SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • multicellular organism reproduction Source: FlyBase
  • protein O-linked glycosylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

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:
Putative polypeptide N-acetylgalactosaminyltransferase 9 (EC:2.4.1.41)
Short name:
pp-GaNTase 9
Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 9
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
Gene namesi
Name:pgant9
ORF Names:CG30463
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0050463. CG30463.

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 – 650LumenalSequence analysisAdd BLAST619

GO - Cellular componenti

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

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591631 – 650Putative polypeptide N-acetylgalactosaminyltransferase 9Add BLAST650

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi198 ↔ 432PROSITE-ProRule annotation
Glycosylationi321N-linked (GlcNAc...)Sequence analysis1
Glycosylationi373N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi423 ↔ 499PROSITE-ProRule annotation
Disulfide bondi535 ↔ 554PROSITE-ProRule annotation
Disulfide bondi577 ↔ 590PROSITE-ProRule annotation
Disulfide bondi616 ↔ 631PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8MRC9.
PRIDEiQ8MRC9.

Expressioni

Tissue specificityi

During embryonic stages 9-11, expressed in the developing anterior midgut and amnioserosa. Expressed in the salivary glands from embryonic stage 12 onwards. During embryonic stages 12-13, still expressed in the amnioserosa region. In third instar larvae, expressed ubiquitously in wing, with increased expression in the notum and ventral wing pouch, leg and haltere imaginal disks. In eye-antennal imaginal disk, expressed in the presumptive eye region only.1 Publication

Developmental stagei

Expressed both maternally and zygotically. Expressed through embryonic and larval stages.1 Publication

Gene expression databases

BgeeiFBgn0050463.
GenevisibleiQ8MRC9. DM.

Interactioni

Protein-protein interaction databases

BioGridi73174. 1 interactor.
IntActiQ8MRC9. 2 interactors.
MINTiMINT-964044.
STRINGi7227.FBpp0086258.

Structurei

3D structure databases

ProteinModelPortaliQ8MRC9.
SMRiQ8MRC9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini521 – 643Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST123

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni208 – 317Catalytic subdomain AAdd BLAST110
Regioni378 – 440Catalytic subdomain BAdd BLAST63

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi43 – 90Gly-richAdd BLAST48

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.
InParanoidiQ8MRC9.
KOiK00710.
OMAiFALAIWF.
OrthoDBiEOG091G085O.
PhylomeDBiQ8MRC9.

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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q8MRC9-1) [UniParc]FASTAAdd to basket
Also known as: D

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAFIWRRRST TIVKLVAFAL AIWFCIAFLV YTDDTRRRAA QEGAGASGAG
60 70 80 90 100
SAPGVGGGAG GLGDPIALAL RNEPAGEDFG INGNVIGGGG QKQAHDEADI
110 120 130 140 150
PPTVGKHKAD LQAERMRKKA AEQPKKKPQE DSKKVIDPPA NFEENPGELG
160 170 180 190 200
KPVRLPKEMS DEMKKAVDDG WTKNAFNQYV SDLISVHRTL PDPRDAWCKD
210 220 230 240 250
EARYLTNLPK TDVIICFHNE AWTVLLRTVH SVLDRSPEHL IGKIILVDDY
260 270 280 290 300
SDMPHLKRQL EDYFAAYPKV QIIRGQKREG LIRARILGAN HAKSPVLTYL
310 320 330 340 350
DSHCECTEGW LEPLLDRIAR NSTTVVCPVI DVISDETLEY HYRDSGGVNV
360 370 380 390 400
GGFDWNLQFS WHPVPERERK RHNSTAEPVY SPTMAGGLFS IDREFFDRLG
410 420 430 440 450
TYDSGFDIWG GENLELSFKT WMCGGTLEIV PCSHVGHIFR KRSPYKWRSG
460 470 480 490 500
VNVLKKNSVR LAEVWMDEYS QYYYHRIGND KGDWGDVSDR RKLRNDLKCK
510 520 530 540 550
SFKWYLDNIY PELFIPGDSV AHGEIRNLGY GGRTCLDAPA GKKHQKKAVG
560 570 580 590 600
TYPCHRQGGN QYWMLSKAGE IRRDDSCLDY AGKDVTLFGC HGGKGNQFWT
610 620 630 640 650
YRENTKQLHH GTSGKCLAIS ESKDKLLMEE CSASLSRQQW TLENYDSSKL
Note: No experimental confirmation available.
Length:650
Mass (Da):73,193
Last modified:August 16, 2004 - v2
Checksum:iAC847736AD1C07CA
GO
Isoform B (identifier: Q8MRC9-2) [UniParc]FASTAAdd to basket
Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG

Note: No experimental confirmation available.
Show »
Length:647
Mass (Da):72,860
Checksum:iA25855E919100BFE
GO
Isoform E (identifier: Q8MRC9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-383: Missing.
     526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG

Note: No experimental confirmation available.
Show »
Length:264
Mass (Da):30,256
Checksum:i06D95D4D4B3D00E8
GO
Isoform F (identifier: Q8MRC9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-22: AFIWRRRSTTIVKLVAFALAI → NFYLSSWHCQVTQSGLVAGLE
     23-273: Missing.
     526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG

Note: No experimental confirmation available.
Show »
Length:396
Mass (Da):45,208
Checksum:i8AB540EC2C239DF6
GO

Sequence cautioni

The sequence ABL75647 differs from that shown. Intron retention.Curated
The sequence ABL75689 differs from that shown. Intron retention.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145N → D in AAM51988 (PubMed:12537569).Curated1
Sequence conflicti454L → P in AAM51988 (PubMed:12537569).Curated1
Sequence conflicti472Y → C in AAM51988 (PubMed:12537569).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0346321 – 383Missing in isoform E. CuratedAdd BLAST383
Alternative sequenceiVSP_0346332 – 22AFIWR…FALAI → NFYLSSWHCQVTQSGLVAGL E in isoform F. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_03463423 – 273Missing in isoform F. 1 PublicationAdd BLAST251
Alternative sequenceiVSP_034635526 – 556RNLGY…YPCHR → ANVPNGMCLDAKEKSEEETP VSIYECHG in isoform B, isoform E and isoform F. 1 PublicationAdd BLAST31

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57964.3.
AE013599 Genomic DNA. Translation: AAF57966.2.
AE013599 Genomic DNA. Translation: ABV53822.1.
AE013599 Genomic DNA. Translation: ABV53823.1.
AE013599 Genomic DNA. Translation: ABV53824.1.
AY121661 mRNA. Translation: AAM51988.1.
BT029588 mRNA. Translation: ABL75647.1. Sequence problems.
BT029630 mRNA. Translation: ABL75689.1. Sequence problems.
RefSeqiNP_001097341.1. NM_001103871.1. [Q8MRC9-2]
NP_001097342.1. NM_001103872.1. [Q8MRC9-1]
NP_001097343.1. NM_001103873.1. [Q8MRC9-3]
NP_725602.1. NM_166188.2. [Q8MRC9-1]
NP_725603.2. NM_166189.2. [Q8MRC9-2]
UniGeneiDm.24533.

Genome annotation databases

EnsemblMetazoaiFBtr0087112; FBpp0086258; FBgn0050463. [Q8MRC9-1]
FBtr0113380; FBpp0112292; FBgn0050463. [Q8MRC9-1]
GeneIDi246627.
KEGGidme:Dmel_CG30463.
UCSCiCG30463-RA. d. melanogaster. [Q8MRC9-1]
CG30463-RC. d. melanogaster.
CG30463-RD. d. melanogaster.
CG30463-RE. d. melanogaster.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57964.3.
AE013599 Genomic DNA. Translation: AAF57966.2.
AE013599 Genomic DNA. Translation: ABV53822.1.
AE013599 Genomic DNA. Translation: ABV53823.1.
AE013599 Genomic DNA. Translation: ABV53824.1.
AY121661 mRNA. Translation: AAM51988.1.
BT029588 mRNA. Translation: ABL75647.1. Sequence problems.
BT029630 mRNA. Translation: ABL75689.1. Sequence problems.
RefSeqiNP_001097341.1. NM_001103871.1. [Q8MRC9-2]
NP_001097342.1. NM_001103872.1. [Q8MRC9-1]
NP_001097343.1. NM_001103873.1. [Q8MRC9-3]
NP_725602.1. NM_166188.2. [Q8MRC9-1]
NP_725603.2. NM_166189.2. [Q8MRC9-2]
UniGeneiDm.24533.

3D structure databases

ProteinModelPortaliQ8MRC9.
SMRiQ8MRC9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi73174. 1 interactor.
IntActiQ8MRC9. 2 interactors.
MINTiMINT-964044.
STRINGi7227.FBpp0086258.

Protein family/group databases

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

Proteomic databases

PaxDbiQ8MRC9.
PRIDEiQ8MRC9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087112; FBpp0086258; FBgn0050463. [Q8MRC9-1]
FBtr0113380; FBpp0112292; FBgn0050463. [Q8MRC9-1]
GeneIDi246627.
KEGGidme:Dmel_CG30463.
UCSCiCG30463-RA. d. melanogaster. [Q8MRC9-1]
CG30463-RC. d. melanogaster.
CG30463-RD. d. melanogaster.
CG30463-RE. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0050463. CG30463.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
InParanoidiQ8MRC9.
KOiK00710.
OMAiFALAIWF.
OrthoDBiEOG091G085O.
PhylomeDBiQ8MRC9.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-DME-913709. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSiCG30463. fly.
GenomeRNAii246627.
PROiQ8MRC9.

Gene expression databases

BgeeiFBgn0050463.
GenevisibleiQ8MRC9. 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 nameiGALT9_DROME
AccessioniPrimary (citable) accession number: Q8MRC9
Secondary accession number(s): A1A6R7
, A1A6V9, A8DYG1, A8DYG2, A8DYG3, Q0E950, Q9V7T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: November 30, 2016
This is version 124 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.