St8sia3
entrez
20451
canonical
uniprot
Q64689
canonical
ensembl
ENSMUSG00000056812
resolver
ensp
ENSMUSP00000025477
resolver
ensp
ENSMUSP00000158392
resolver
ensp
ENSMUSP00000263582
resolver
enst
ENSMUST00000025477
resolver
enst
ENSMUST00000237770
resolver
genesymbol
St8sia3
resolver
genesymbol_syn
Siat8c
resolver
uniprot
Q6DIB7
resolver
uniprot
Q9CUJ6
resolver
uniprot_entry
Q9CUJ6_MOUSE
resolver
uniprot_entry
SIA8C_MOUSE
resolver
uniprot_sec
Q6DIB7
resolver
amino_acid_sequence
MRNCKMARVASVLGLVMLSVALLILSLISYVSLKKENIFTTPKYASPGAPRMYMFHAGFRSQFALKFLDQSFVPITNSLTHELQEKPSKWTFNRTAFLHQRQEILQHVDVIKNFSLTKSSVRIGQLMHYDYSSHKYVFSISNNFRSLLPDVSPIMNKRYNVCAVVGNSGILTGSQCGQEIDKSDFVFRCNFAPTEAFHKDVGRKTNLTTFNPSILEKYYNNLLTIQDRNNFFLSLKKLDGAILWIPAFFFHTSATVTRTLVDFFVEHRGQLKVQLAWPGNIMQHVNRYWKNKHLSPKRLSTGILMYTLASAICEEIHLYGFWPFGFDPNTREDLPYHYYDKKGTKFTTKWQESHQLPAEFQLLYRMHGEGLTKLTLSHCA
uniprot
proteins
ec_number
2.4.3.-
uniprot
proteins
ec_number
2.4.3.8
uniprot
proteins
function
FUNCTION: Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto a terminal alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid of an acceptor, such as N-linked oligosaccharides of glycoproteins and glycolipids through alpha-2,8-linkages (PubMed:7782326). Forms oligosialic and polysialic acid on various sialylated N-acetyllactosamine oligosaccharides of glycoproteins, including FETUB N-glycans, a2-HS-glycoprotein (AHSG) and alpha 2,3-sialylated glycosphingolipids, such as alpha 2,3-sialylparagloboside and ganglioside GM3 and to a lesser extent NCAM1 N-glycans (PubMed:7782326). However, it is much more specific to N-linked oligosaccharides of glycoproteins than glycosphingolipids (PubMed:7782326). 2,3-sialylparagloboside served as the best acceptor substrate among the glycolipids (PubMed:7782326). alpha-Neu5Ac-(2->8)-alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-6S-D-GlcNAc and monosialyl and disialyl N-acetyllactosamines are the best acceptor substrates among glycoproteins (By similarity). May play critical role in the striatum by mediating the formation of disialylated and trisialylated terminal glycotopes on N- and O-glycans of specific striatal proteins, regulating their distribution in lipid rafts, affecting their interaction with other binding partners, and subsequently modulating striatal functions (PubMed:31455764). {ECO:0000250|UniProtKB:O43173, ECO:0000269|PubMed:31455764, ECO:0000269|PubMed:7782326}.
uniprot
proteins
mass_dalton
43942
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:7782326}.
uniprot
proteins
protein_family
Glycosyltransferase 29 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
31455764
uniprot
proteins
pubmed
7782326
uniprot
proteins
sequence_length
380
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O43173}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O43173}.
uniprot
proteins
transmembrane_region
TRANSMEM 18..33; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins