Q64687 · SIA8A_MOUSE
- ProteinAlpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- GeneSt8sia1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids355 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphingolipds that contain one or more residues of sialic acid (PubMed:8910600).
Can catalyze the addition of a second alpha-2,8- sialic acid to GD3 to form GT3 (PubMed:8910600).
Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b respectively (PubMed:8910600).
Can catalyze the addition of a second alpha-2,8- sialic acid to GD3 to form GT3 (PubMed:8910600).
Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b respectively (PubMed:8910600).
Catalytic activity
- an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl derivative + CMP + H+
- a ganglioside GM3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GD3 (d18:1(4E)) + CMP + H+This reaction proceeds in the forward direction.
- a ganglioside GD3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GT3 (d18:1(4E)) + CMP + H+This reaction proceeds in the forward direction.
- a ganglioside GD1a (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GT1a (d18:1(4E)) + CMP + H+This reaction proceeds in the forward direction.
- a ganglioside GT1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GQ1b (d18:1(4E)) + CMP + H+This reaction proceeds in the forward direction.
- a ganglioside GM1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GD1c (d18:1(4E)) + CMP + H+This reaction proceeds in the forward direction.
- a ganglioside GD3 + CMP-N-acetyl-beta-neuraminate = a ganglioside GT3 + CMP + H+This reaction proceeds in the forward direction.
- [alpha-N-acetylneuraminyl-(2->8)](n)-alpha-N-acetylneuraminyl-(2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + CMP-N-acetyl-beta-neuraminate = [alpha-N-acetylneuraminyl-(2->8)](n+1)-alpha-N-acetylneuraminyl-(2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + CMP + H+This reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.03 mM | ganglioside GM3 | |||||
5 mM | ganglioside GD3 | |||||
5 mM | ganglioside GD1a | |||||
2 mM | ganglioside GT1b |
Pathway
Protein modification; protein glycosylation.
Lipid metabolism; sphingolipid metabolism.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 142 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 165 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 273 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 274 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 275 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 295 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 309 | CMP-N-acetyl-beta-neuraminate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 321 | Proton donor/acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi membrane | |
Molecular Function | alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity | |
Biological Process | cell population proliferation | |
Biological Process | cellular response to heat | |
Biological Process | epithelial cell proliferation | |
Biological Process | positive regulation of epithelial cell proliferation | |
Biological Process | protein glycosylation | |
Biological Process | sphingolipid metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ64687
- 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 | 1-28 | Cytoplasmic | ||||
Sequence: MSPCGRALHTSRGAMAMLARKFPRTRLP | ||||||
Transmembrane | 29-47 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: VGASALCVVVLCWLYIFPV | ||||||
Topological domain | 48-355 | Lumenal | ||||
Sequence: YRLPNEKEIVQGVLAQRTAWRTNQTSASLFRRQMEDCCDPAHLFAMTKMNSPMGKSLWYDGELLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKMSGCGRQIDEANFVMRCNLPPLSSEYTRDVGSKTQLVTANPSIIRQRFENLLWSRKKFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLKDVGANQTVLFANPNFLRNIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVSIYGFWPFSVNMQGDPISHHYYDNVLPFSGYHAMPEEFLQLWYLHKIGALRMQLDPCEEPSPQPTS |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000149283 | 1-355 | Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase | |||
Sequence: MSPCGRALHTSRGAMAMLARKFPRTRLPVGASALCVVVLCWLYIFPVYRLPNEKEIVQGVLAQRTAWRTNQTSASLFRRQMEDCCDPAHLFAMTKMNSPMGKSLWYDGELLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKMSGCGRQIDEANFVMRCNLPPLSSEYTRDVGSKTQLVTANPSIIRQRFENLLWSRKKFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLKDVGANQTVLFANPNFLRNIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVSIYGFWPFSVNMQGDPISHHYYDNVLPFSGYHAMPEEFLQLWYLHKIGALRMQLDPCEEPSPQPTS | ||||||
Glycosylation | 70 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 118 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 137↔286 | |||||
Sequence: CAVVGNGGILKMSGCGRQIDEANFVMRCNLPPLSSEYTRDVGSKTQLVTANPSIIRQRFENLLWSRKKFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLKDVGANQTVLFANPNFLRNIGKFWKSRGIHAKRLSTGLFLVSAALGLC | ||||||
Disulfide bond | 151↔346 | |||||
Sequence: CGRQIDEANFVMRCNLPPLSSEYTRDVGSKTQLVTANPSIIRQRFENLLWSRKKFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLKDVGANQTVLFANPNFLRNIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVSIYGFWPFSVNMQGDPISHHYYDNVLPFSGYHAMPEEFLQLWYLHKIGALRMQLDPC | ||||||
Glycosylation | 213 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 244 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length355
- Mass (Da)40,324
- Last updated2011-07-27 v2
- Checksum220BD56BBEE6E6C6
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0N4SVL1 | A0A0N4SVL1_MOUSE | St8sia1 | 101 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 50 | in Ref. 1; CAA59014 | ||||
Sequence: L → P | ||||||
Sequence conflict | 64 | in Ref. 1; CAA59014 | ||||
Sequence: R → S | ||||||
Sequence conflict | 294 | in Ref. 1; CAA59014 | ||||
Sequence: F → S | ||||||
Sequence conflict | 318 | in Ref. 1; CAA59014 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X84235 EMBL· GenBank· DDBJ | CAA59014.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466572 EMBL· GenBank· DDBJ | EDL10653.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC024821 EMBL· GenBank· DDBJ | AAH24821.1 EMBL· GenBank· DDBJ | mRNA |