Q8MRC9 · GALT9_DROME
- ProteinPutative polypeptide N-acetylgalactosaminyltransferase 9
- GenePgant9
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids650 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 (PubMed:30158631).
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 (PubMed:30158631).
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 (PubMed:30158631).
Isoform A
N-acetylgalactosaminyltransferase which preferentially O-glycosylates negatively charge substrates. O-glycosylates mucin-like protein Sgs3 in the salivary gland but to a lesser extent than isoform B. By regulating the O-glycosylation of secretory cargo proteins plays a role in the morphology and maturation of salivary gland secretory granules.
Isoform B
N-acetylgalactosaminyltransferase which preferentially O-glycosylates positively charge substrates. O-glycosylates mucin-like protein Sgs3 in the salivary gland. By regulating the O-glycosylation of secretory cargo proteins, plays a role in the morphology and maturation of salivary gland secretory granules.
Catalytic activity
- L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H+ + UDP
Cofactor
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 216 | substrate | ||||
Sequence: C | ||||||
Binding site | 249 | substrate | ||||
Sequence: D | ||||||
Binding site | 278 | substrate | ||||
Sequence: R | ||||||
Binding site | 301 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 302 | substrate | ||||
Sequence: S | ||||||
Binding site | 303 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 303 | substrate | ||||
Sequence: H | ||||||
Binding site | 437 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 440 | substrate | ||||
Sequence: R | ||||||
Binding site | 445 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi cisterna | |
Cellular Component | Golgi membrane | |
Cellular Component | membrane | |
Molecular Function | carbohydrate binding | |
Molecular Function | metal ion binding | |
Molecular Function | polypeptide N-acetylgalactosaminyltransferase activity | |
Biological Process | protein O-linked glycosylation | |
Biological Process | sexual reproduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePutative polypeptide N-acetylgalactosaminyltransferase 9
- EC number
- Short namespp-GaNTase 9
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ8MRC9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform A
Golgi apparatus membrane ; Single-pass type II membrane protein
Isoform B
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-11 | Cytoplasmic | ||||
Sequence: MAFIWRRRSTT | ||||||
Transmembrane | 12-31 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: IVKLVAFALAIWFCIAFLVY | ||||||
Topological domain | 32-650 | Lumenal | ||||
Sequence: TDDTRRRAAQEGAGASGAGSAPGVGGGAGGLGDPIALALRNEPAGEDFGINGNVIGGGGQKQAHDEADIPPTVGKHKADLQAERMRKKAAEQPKKKPQEDSKKVIDPPANFEENPGELGKPVRLPKEMSDEMKKAVDDGWTKNAFNQYVSDLISVHRTLPDPRDAWCKDEARYLTNLPKTDVIICFHNEAWTVLLRTVHSVLDRSPEHLIGKIILVDDYSDMPHLKRQLEDYFAAYPKVQIIRGQKREGLIRARILGANHAKSPVLTYLDSHCECTEGWLEPLLDRIARNSTTVVCPVIDVISDETLEYHYRDSGGVNVGGFDWNLQFSWHPVPERERKRHNSTAEPVYSPTMAGGLFSIDREFFDRLGTYDSGFDIWGGENLELSFKTWMCGGTLEIVPCSHVGHIFRKRSPYKWRSGVNVLKKNSVRLAEVWMDEYSQYYYHRIGNDKGDWGDVSDRRKLRNDLKCKSFKWYLDNIYPELFIPGDSVAHGEIRNLGYGGRTCLDAPAGKKHQKKAVGTYPCHRQGGNQYWMLSKAGEIRRDDSCLDYAGKDVTLFGCHGGKGNQFWTYRENTKQLHHGTSGKCLAISESKDKLLMEECSASLSRQQWTLENYDSSKL |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown in the whole body, in the mesoderm, the respiratory system or the amnioserosa results in lethality (PubMed:22157008).
RNAi-mediated knockdown in the epidermis or the digestive system and reproductive tract results in a reduction in viability (PubMed:22157008).
RNAi-mediated knockdown in salivary glands results in aberrant secretory granule morphology showing angular, shard-like morphology (PubMed:30158631).
RNAi-mediated knockdown in the epidermis or the digestive system and reproductive tract results in a reduction in viability (PubMed:22157008).
RNAi-mediated knockdown in salivary glands results in aberrant secretory granule morphology showing angular, shard-like morphology (PubMed:30158631).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 254-650 | Results in secretory granule defects including an angular and shard-like morphology. | ||||
Sequence: Missing |
PTM/Processing
Features
Showing features for chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059163 | 1-650 | Putative polypeptide N-acetylgalactosaminyltransferase 9 | |||
Sequence: MAFIWRRRSTTIVKLVAFALAIWFCIAFLVYTDDTRRRAAQEGAGASGAGSAPGVGGGAGGLGDPIALALRNEPAGEDFGINGNVIGGGGQKQAHDEADIPPTVGKHKADLQAERMRKKAAEQPKKKPQEDSKKVIDPPANFEENPGELGKPVRLPKEMSDEMKKAVDDGWTKNAFNQYVSDLISVHRTLPDPRDAWCKDEARYLTNLPKTDVIICFHNEAWTVLLRTVHSVLDRSPEHLIGKIILVDDYSDMPHLKRQLEDYFAAYPKVQIIRGQKREGLIRARILGANHAKSPVLTYLDSHCECTEGWLEPLLDRIARNSTTVVCPVIDVISDETLEYHYRDSGGVNVGGFDWNLQFSWHPVPERERKRHNSTAEPVYSPTMAGGLFSIDREFFDRLGTYDSGFDIWGGENLELSFKTWMCGGTLEIVPCSHVGHIFRKRSPYKWRSGVNVLKKNSVRLAEVWMDEYSQYYYHRIGNDKGDWGDVSDRRKLRNDLKCKSFKWYLDNIYPELFIPGDSVAHGEIRNLGYGGRTCLDAPAGKKHQKKAVGTYPCHRQGGNQYWMLSKAGEIRRDDSCLDYAGKDVTLFGCHGGKGNQFWTYRENTKQLHHGTSGKCLAISESKDKLLMEECSASLSRQQWTLENYDSSKL | ||||||
Disulfide bond | 198↔432 | |||||
Sequence: CKDEARYLTNLPKTDVIICFHNEAWTVLLRTVHSVLDRSPEHLIGKIILVDDYSDMPHLKRQLEDYFAAYPKVQIIRGQKREGLIRARILGANHAKSPVLTYLDSHCECTEGWLEPLLDRIARNSTTVVCPVIDVISDETLEYHYRDSGGVNVGGFDWNLQFSWHPVPERERKRHNSTAEPVYSPTMAGGLFSIDREFFDRLGTYDSGFDIWGGENLELSFKTWMCGGTLEIVPC | ||||||
Glycosylation | 321 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 373 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 423↔499 | |||||
Sequence: CGGTLEIVPCSHVGHIFRKRSPYKWRSGVNVLKKNSVRLAEVWMDEYSQYYYHRIGNDKGDWGDVSDRRKLRNDLKC | ||||||
Disulfide bond | 535↔554 | |||||
Sequence: CLDAPAGKKHQKKAVGTYPC | ||||||
Disulfide bond | 577↔590 | |||||
Sequence: CLDYAGKDVTLFGC | ||||||
Disulfide bond | 616↔631 | |||||
Sequence: CLAISESKDKLLMEEC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed both maternally and zygotically (PubMed:16251381).
Expressed through embryonic and larval stages (PubMed:16251381).
During embryonic stages 9-11, expressed in the developing anterior midgut and amnioserosa (PubMed:16251381).
Expressed in the salivary glands from embryonic stage 12 onwards (PubMed:16251381).
During embryonic stages 12-13, still expressed in the amnioserosa region (PubMed:16251381).
In third instar larvae, expressed ubiquitously in wing, with increased expression in the notum and ventral wing pouch, leg and haltere imaginal disks (PubMed:16251381).
In eye-antennal imaginal disk, expressed in the presumptive eye region only (PubMed:16251381).
Isoform A: Expressed in trachea, midgut, salivary gland, hindgut, central nervous system and Malpighian tubules (PubMed:30158631).
Isoform B: Specifically expressed in the salivary gland (PubMed:30158631).
Expressed through embryonic and larval stages (PubMed:16251381).
During embryonic stages 9-11, expressed in the developing anterior midgut and amnioserosa (PubMed:16251381).
Expressed in the salivary glands from embryonic stage 12 onwards (PubMed:16251381).
During embryonic stages 12-13, still expressed in the amnioserosa region (PubMed:16251381).
In third instar larvae, expressed ubiquitously in wing, with increased expression in the notum and ventral wing pouch, leg and haltere imaginal disks (PubMed:16251381).
In eye-antennal imaginal disk, expressed in the presumptive eye region only (PubMed:16251381).
Isoform A: Expressed in trachea, midgut, salivary gland, hindgut, central nervous system and Malpighian tubules (PubMed:30158631).
Isoform B: Specifically expressed in the salivary gland (PubMed:30158631).
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 84-154 | Disordered | ||||
Sequence: NVIGGGGQKQAHDEADIPPTVGKHKADLQAERMRKKAAEQPKKKPQEDSKKVIDPPANFEENPGELGKPVR | ||||||
Compositional bias | 99-138 | Basic and acidic residues | ||||
Sequence: DIPPTVGKHKADLQAERMRKKAAEQPKKKPQEDSKKVIDP | ||||||
Region | 208-317 | Catalytic subdomain A | ||||
Sequence: LPKTDVIICFHNEAWTVLLRTVHSVLDRSPEHLIGKIILVDDYSDMPHLKRQLEDYFAAYPKVQIIRGQKREGLIRARILGANHAKSPVLTYLDSHCECTEGWLEPLLDR | ||||||
Region | 378-440 | Catalytic subdomain B | ||||
Sequence: PVYSPTMAGGLFSIDREFFDRLGTYDSGFDIWGGENLELSFKTWMCGGTLEIVPCSHVGHIFR | ||||||
Domain | 521-643 | Ricin B-type lectin | ||||
Sequence: AHGEIRNLGYGGRTCLDAPAGKKHQKKAVGTYPCHRQGGNQYWMLSKAGEIRRDDSCLDYAGKDVTLFGCHGGKGNQFWTYRENTKQLHHGTSGKCLAISESKDKLLMEECSASLSRQQWTLE |
Domain
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is involved in catalytic reaction and UDP-Gal binding.
The alpha subunit loop in the ricin B-type lectin domain regulates substrate specificity and modulates the substrate access to the active site. In isoform A, the alpha subunit loop is composed of positively charged residues and acts on negatively charged substrates. In isoform B, the alpha subunit loop is composed of negatively charged residues and acts on positively charged substrates.
Sequence similarities
Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q8MRC9-1
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.
- NameA
- SynonymsD
- Length650
- Mass (Da)73,193
- Last updated2004-08-16 v2
- ChecksumAC847736AD1C07CA
Q8MRC9-2
- NameB
- SynonymsC
- Differences from canonical
- 526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG
Q8MRC9-3
- NameE
Q8MRC9-4
- NameF
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_034632 | 1-383 | in isoform E | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_034633 | 2-22 | in isoform F | |||
Sequence: AFIWRRRSTTIVKLVAFALAI → NFYLSSWHCQVTQSGLVAGLE | ||||||
Alternative sequence | VSP_034634 | 23-273 | in isoform F | |||
Sequence: Missing | ||||||
Compositional bias | 99-138 | Basic and acidic residues | ||||
Sequence: DIPPTVGKHKADLQAERMRKKAAEQPKKKPQEDSKKVIDP | ||||||
Sequence conflict | 145 | in Ref. 3; AAM51988 | ||||
Sequence: N → D | ||||||
Sequence conflict | 454 | in Ref. 3; AAM51988 | ||||
Sequence: L → P | ||||||
Sequence conflict | 472 | in Ref. 3; AAM51988 | ||||
Sequence: Y → C | ||||||
Alternative sequence | VSP_034635 | 526-556 | in isoform B, isoform E and isoform F | |||
Sequence: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE013599 EMBL· GenBank· DDBJ | AAF57964.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF57966.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | ABV53822.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | ABV53823.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | ABV53824.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY121661 EMBL· GenBank· DDBJ | AAM51988.1 EMBL· GenBank· DDBJ | mRNA | ||
BT029588 EMBL· GenBank· DDBJ | ABL75647.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BT029630 EMBL· GenBank· DDBJ | ABL75689.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |