Q9WUV2 · SIA7C_MOUSE
- ProteinAlpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3
- GeneSt6galnac3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids305 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. ST6GalNAcIII prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b (PubMed:10207017, PubMed:10601645).
GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity).
Sialylation of glycoproteins or glycosphingolipids is very important in tumor development, neuronal development, nerve repair, immunological processes and regulation of hormone sensitivity (By similarity).
GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity).
Sialylation of glycoproteins or glycosphingolipids is very important in tumor development, neuronal development, nerve repair, immunological processes and regulation of hormone sensitivity (By similarity).
Catalytic activity
- an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative + CMP-N-acetyl-beta-neuraminate = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-D-GlcNAc-R + CMP + H+This reaction proceeds in the forward direction.
- a ganglioside GM1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GD1alpha (d18:1(4E)) + CMP + H+This reaction proceeds in the forward direction.
- a globoside MSGG + CMP-N-acetyl-beta-neuraminate = a globoside DSGG + CMP + H+This reaction proceeds in the forward direction.
- 3-O-[alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc]-L-Ser-[protein] + CMP-N-acetyl-beta-neuraminate = 3-O-{alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-alpha-D-GalNAc}-L-Ser-[protein] + CMP + H+This reaction proceeds in the forward direction.
- 3-O-[alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc]-L-Thr-[protein] + CMP-N-acetyl-beta-neuraminate = 3-O-{alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-alpha-D-GalNAc}-L-Thr-[protein] + CMP + H+This reaction proceeds in the forward direction.
Pathway
Protein modification; protein glycosylation.
Glycolipid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi membrane | |
Cellular Component | nucleoplasm | |
Molecular Function | alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity | |
Molecular Function | alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide 6-alpha-sialyltransferase activity | |
Molecular Function | sialyltransferase activity | |
Biological Process | ganglioside biosynthetic process | |
Biological Process | glycosylceramide metabolic process | |
Biological Process | oligosaccharide metabolic process | |
Biological Process | protein glycosylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameAlpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9WUV2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-8 | Cytoplasmic | ||||
Sequence: MACILKRK | ||||||
Transmembrane | 9-28 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: PVLVVSFIALCILLLAMRLV | ||||||
Topological domain | 29-305 | Lumenal | ||||
Sequence: NDATFPLLLNCFGQPKTKWIPLPYTFRQPLRTHYGYINVRTQEPLQLNCNHCAIVSNSGQMVGQKVGEEIDHASCIWRMNNAPTKGFEEDVGYMTMVRVVSHTSVPLLLKNPDYFFKEASRTIYVIWGPFRNMRKDGNGIVYNMLKKTVDAYPDAQIYVTTEQQMTHCDRVFKDETGKDRVQSGSYLSTGWFTFILAMDACYSIHVYGMINETYCKTEGYRKVPYHYYEQGKDECNEYLLHEHAPYGGHRFITEKKVFAKWAKKHRIVFTHPNWTLS |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000149276 | 1-305 | Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3 | |||
Sequence: MACILKRKPVLVVSFIALCILLLAMRLVNDATFPLLLNCFGQPKTKWIPLPYTFRQPLRTHYGYINVRTQEPLQLNCNHCAIVSNSGQMVGQKVGEEIDHASCIWRMNNAPTKGFEEDVGYMTMVRVVSHTSVPLLLKNPDYFFKEASRTIYVIWGPFRNMRKDGNGIVYNMLKKTVDAYPDAQIYVTTEQQMTHCDRVFKDETGKDRVQSGSYLSTGWFTFILAMDACYSIHVYGMINETYCKTEGYRKVPYHYYEQGKDECNEYLLHEHAPYGGHRFITEKKVFAKWAKKHRIVFTHPNWTLS | ||||||
Disulfide bond | 80↔229 | |||||
Sequence: CAIVSNSGQMVGQKVGEEIDHASCIWRMNNAPTKGFEEDVGYMTMVRVVSHTSVPLLLKNPDYFFKEASRTIYVIWGPFRNMRKDGNGIVYNMLKKTVDAYPDAQIYVTTEQQMTHCDRVFKDETGKDRVQSGSYLSTGWFTFILAMDAC | ||||||
Glycosylation | 239 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 301 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
In adult tissues, high expression in brain, lung and heart and to a lesser extent in kidney, mammary gland, spleen, testis and thymus.
Developmental stage
In brain, expression reaches maximum levels at day 12 of the embryonic stage. Keeps almost similar levels during mouse development.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length305
- Mass (Da)35,414
- Last updated2001-03-01 v2
- Checksum63C7498615BF6A3F
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0H2UKC4 | A0A0H2UKC4_MOUSE | St6galnac3 | 196 | ||
A0A0G2JF56 | A0A0G2JF56_MOUSE | St6galnac3 | 125 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y11342 EMBL· GenBank· DDBJ | CAA72181.2 EMBL· GenBank· DDBJ | mRNA | ||
Y11343 EMBL· GenBank· DDBJ | CAB95031.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11344 EMBL· GenBank· DDBJ | CAB95031.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11345 EMBL· GenBank· DDBJ | CAB95031.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y11346 EMBL· GenBank· DDBJ | CAB95031.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC058387 EMBL· GenBank· DDBJ | AAH58387.1 EMBL· GenBank· DDBJ | mRNA |