St3gal1
entrez
20442
canonical
uniprot
P54751
canonical
ensembl
ENSMUSG00000013846
resolver
ensp
ENSMUSP00000090307
resolver
ensp
ENSMUSP00000154853
resolver
ensp
ENSMUSP00000155359
resolver
ensp
ENSMUSP00000357466
resolver
enst
ENSMUST00000092640
resolver
enst
ENSMUST00000229028
resolver
enst
ENSMUST00000229213
resolver
genesymbol
St3gal1
resolver
genesymbol_syn
Siat4
resolver
genesymbol_syn
Siat4a
resolver
uniprot
Q11202
resolver
uniprot
Q544T4
resolver
uniprot_entry
Q544T4_MOUSE
resolver
uniprot_entry
SIA4A_MOUSE
resolver
uniprot_sec
Q11202
resolver
amino_acid_sequence
MRRKTLKYLTFFLLFIFLTSFVLNYSNTGVPSAWFPKQMLLELSENFRRFIKSQPCTCRHCISQDKVSYWFDQRFNKTMQPLLTVHNALMEEDTYRWWLRLQRERKPNNLSDTVKELFRLVPGNVDPMLNKRLVGCRRCAVVGNSGNLKDSSYGPEIDSHDFVLRMNKAPTVGFEADVGSRTTHHLVYPESFRELGENVNMVLVPFKTTDLQWVISATTTGTITHTYVPVPPKIKVKQEKILIYHPAFIKYVFDNWLQGHGRYPSTGILSIIFSIHICDEVDLYGFGADSKGNWHHYWENNPSAGAFRKTGVHDGDFEYNITTTLAAINKIRIFKGR
uniprot
proteins
ec_number
2.4.3.2
uniprot
proteins
ec_number
2.4.3.4
uniprot
proteins
function
FUNCTION: A beta-galactoside alpha2->3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids (PubMed:8375377, PubMed:9184827). Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through an alpha2-3 linkage (PubMed:10755614, PubMed:8144500, PubMed:8375377, PubMed:9184827). Adds sialic acid to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, which is a major structure of mucin-type O-glycans. As part of a homeostatic mechanism that regulates CD8-positive T cell numbers, sialylates core 1 O-glycans of T cell glycoproteins, SPN/CD43 and PTPRC/CD45. Prevents premature apoptosis of thymic CD8-positive T cells prior to peripheral emigration, whereas in the secondary lymphoid organs controls the survival of CD8-positive memory T cells generated following a successful immune response (PubMed:10755614). Transfers sialic acid to asialofetuin, presumably onto Galbeta-(1->3)-GalNAc-O-Ser (PubMed:8375377). Sialylates GM1a, GA1 and GD1b gangliosides to form GD1a, GM1b and GT1b, respectively (PubMed:8144500, PubMed:8375377, PubMed:9184827). {ECO:0000269|PubMed:10755614, ECO:0000269|PubMed:8144500, ECO:0000269|PubMed:8375377, ECO:0000269|PubMed:9184827}.
uniprot
proteins
mass_dalton
39073
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:10755614}.; PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:8375377}.
uniprot
proteins
post_translational_modification
PTM: The soluble form derives from the membrane form by proteolytic processing.
uniprot
proteins
protein_family
Glycosyltransferase 29 family
uniprot
proteins
pubmed
10755614
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
8144500
uniprot
proteins
pubmed
8375377
uniprot
proteins
pubmed
9184827
uniprot
proteins
sequence_length
337
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q11201}; Single-pass type II membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q11201}; Single-pass type II membrane protein {ECO:0000255}. Secreted. Note=Membrane-bound form in medial and trans cisternae of Golgi (By similarity). Secreted into the body fluid. {ECO:0000250|UniProtKB:Q11201}.
uniprot
proteins
transmembrane_region
TRANSMEM 5..25; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins