UniProtKB - Q11204 (SIA4B_MOUSE)
Protein
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
Gene
St3gal2
Organism
Mus musculus (Mouse)
Status
Functioni
A beta-galactoside alpha2-3 sialyltransferase primarily involved in terminal sialylation of ganglio and globo series glycolipids (PubMed:8144500, 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. Sialylates GM1/GM1a, GA1/asialo-GM1 and GD1b gangliosides to form GD1a, GM1b and GT1b, respectively (PubMed:8144500, PubMed:9184827). Together with ST3GAL3, primarily responsible for biosynthesis of brain GD1a and GT1b that function as ligands for myelin-associated glycoprotein MAG on axons, regulating MAG expression and axonal myelin stability and regeneration (PubMed:22735313). Via GT1b regulates TLR2 signaling in spinal cord microglia in response to nerve injury (PubMed:32030804). Responsible for the sialylation of the pluripotent stem cell- and cancer stem cell-associated antigen SSEA3, forming SSEA4 (By similarity). Sialylates with low efficiency asialofetuin, presumably onto O-glycosidically linked Galbeta-(1->3)-GalNAc-O-Ser (PubMed:8144500).By similarity4 Publications
Catalytic activityi
- a β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl derivative + CMP-N-acetyl-β-neuraminate = an N-acetyl-α-neuraminyl-(2→3)-β-D-galactosyl-(1→3)-N-acetyl-α-D-galactosaminyl derivative + CMP + H+2 PublicationsEC:2.4.99.42 PublicationsThis reaction proceeds in the forward2 Publications direction.
- CMP-N-acetyl-β-neuraminate + ganglioside GM1 (d18:1(4E)) = CMP + ganglioside GD1a (d18:1(4E)) + H+1 PublicationEC:2.4.99.21 PublicationThis reaction proceeds in the forward1 Publication direction.
- CMP-N-acetyl-β-neuraminate + ganglioside GM1 (d18:1(4E)/18:0) = CMP + ganglioside GD1a (18:1(4E)/18:0) + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward2 Publications direction.
- CMP-N-acetyl-β-neuraminate + ganglioside GA1 (d18:1(4E)) = CMP + ganglioside GM1b (d18:1(4E)) + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
Kineticsi
Vmax is 10 fold higher with Gal-beta-1,3-GalNAc than with Gal-beta-1,3-GlcNAc as substrate.1 Publication
- KM=2.3 mM for Gal-beta-1,3-GlcNAc1 Publication
- KM=0.16 mM for Gal-beta-1,3-GalNAc1 Publication
- KM=0.63 mM for Gal-beta-1,3-GalNAc1 Publication
- KM=0.83 mM for GM11 Publication
- KM=0.67 mM for asialo-GM11 Publication
pH dependencei
Optimum pH is 6.4.1 Publication
: protein glycosylation Pathwayi
This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 PublicationView all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.
Pathwayi: Glycolipid biosynthesis
This protein is involved in Glycolipid biosynthesis.2 PublicationsView all proteins of this organism that are known to be involved in Glycolipid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 116 | SubstrateBy similarity | 1 | |
Binding sitei | 157 | SubstrateBy similarity | 1 | |
Binding sitei | 180 | SubstrateBy similarity | 1 | |
Binding sitei | 240 | SubstrateBy similarity | 1 | |
Binding sitei | 276 | SubstrateBy similarity | 1 | |
Binding sitei | 280 | Substrate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 300 | Substrate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 309 | SubstrateBy similarity | 1 | |
Binding sitei | 326 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- beta-galactoside (CMP) alpha-2,3-sialyltransferase activity Source: MGI
- monosialoganglioside sialyltransferase activity Source: MGI
- sialyltransferase activity Source: MGI
GO - Biological processi
- glycolipid biosynthetic process Source: MGI
- glycoprotein biosynthetic process Source: MGI
- lipid glycosylation Source: MGI
- oligosaccharide biosynthetic process Source: MGI
- protein glycosylation Source: MGI
- protein sialylation Source: MGI
- sialylation Source: MGI
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Biological process | Lipid metabolism |
Enzyme and pathway databases
Reactomei | R-MMU-2022854, Keratan sulfate biosynthesis R-MMU-4085001, Sialic acid metabolism R-MMU-977068, Termination of O-glycan biosynthesis |
UniPathwayi | UPA00378 |
Protein family/group databases
CAZyi | GT29, Glycosyltransferase Family 29 |
Chemistry databases
SwissLipidsi | SLP:000001389 |
Names & Taxonomyi
Protein namesi | Recommended name: CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2 (EC:2.4.99.42 Publications)Short name: Alpha 2,3-ST 2 Short name: Beta-galactoside alpha-2,3-sialyltransferase 2 Alternative name(s): Gal-NAc6S Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase1 Publication Monosialoganglioside sialyltransferase (EC:2.4.99.21 Publication) ST3Gal II Short name: ST3GalII ST3GalA.2 Sialyltransferase 4B Short name: SIAT4-B |
Gene namesi | |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:99427, St3gal2 |
Subcellular locationi
Extracellular region or secreted
Golgi apparatus
- Golgi stack membrane By similarity; Single-pass type II membrane protein
Note: Membrane-bound form distributed along the Golgi cisternae, mainly in proximal compartments (By similarity). Secreted into the body fluid.By similarity
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Golgi apparatus
- Golgi cisterna membrane Source: UniProtKB-SubCell
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 6 | CytoplasmicSequence analysis | 6 | |
Transmembranei | 7 – 27 | Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST | 21 | |
Topological domaini | 28 – 350 | LumenalSequence analysisAdd BLAST | 323 |
Keywords - Cellular componenti
Golgi apparatus, Membrane, SecretedPathology & Biotechi
Disruption phenotypei
No visible phenotype under physiological conditions; due to the redundancy with ST3GAL3. Simultaneous knockdown of ST3GAL2 and ST3GAL3 results in markedly fewer offspring and impaired nervous system function at weaning (PubMed:22735313). Knockout mice show reduced nerve injury-induced neuropathic pain in response to noxious stimuli (hyperalgesia) and to normally innocuous stimuli (allodynia) (PubMed:32030804).2 Publications
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000149259 | 1 – 350 | CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2Add BLAST | 350 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 70 ↔ 75 | By similarity | ||
Disulfide bondi | 72 ↔ 149 | By similarity | ||
Disulfide bondi | 152 ↔ 291 | By similarity | ||
Glycosylationi | 211 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Post-translational modificationi
The soluble form derives from the membrane form by proteolytic processing.
N-glycosylated; necessary for proper exit from endoplasmic reticulum and trafficking to the Golgi apparatus.By similarity
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
MaxQBi | Q11204 |
PaxDbi | Q11204 |
PRIDEi | Q11204 |
PTM databases
GlyGeni | Q11204, 1 site |
PhosphoSitePlusi | Q11204 |
Expressioni
Tissue specificityi
Strongly expressed in brain and liver and to a lesser extent in heart and kidney. Scarcely detectable in lung, pancreas, spleen and submaxillary gland (PubMed:8144500). Expressed in L5 dorsal root ganglion (DRG) neurons (at protein level) (PubMed:32030804).2 Publications
Inductioni
Up-regulated in DRG neurons in response to nerve injury.1 Publication
Gene expression databases
Bgeei | ENSMUSG00000031749, Expressed in cerebellum and 277 other tissues |
ExpressionAtlasi | Q11204, baseline and differential |
Genevisiblei | Q11204, MM |
Interactioni
Subunit structurei
Homodimer; disulfide-linked. Homodimer formation occurs in the endoplasmic reticulum.
By similarityProtein-protein interaction databases
STRINGi | 10090.ENSMUSP00000034197 |
Miscellaneous databases
RNActi | Q11204, protein |
Family & Domainsi
Sequence similaritiesi
Belongs to the glycosyltransferase 29 family.Curated
Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG2692, Eukaryota |
GeneTreei | ENSGT00940000156356 |
HOGENOMi | CLU_032020_2_0_1 |
InParanoidi | Q11204 |
OMAi | YIHDHWT |
OrthoDBi | 891104at2759 |
TreeFami | TF354325 |
Family and domain databases
Gene3Di | 3.90.1480.20, 1 hit |
InterProi | View protein in InterPro IPR001675, Glyco_trans_29 IPR038578, GT29-like_sf IPR012163, Sialyl_trans |
Pfami | View protein in Pfam PF00777, Glyco_transf_29, 1 hit |
PIRSFi | PIRSF005557, Sialyl_trans, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
Q11204-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKCSLRVWFL SMAFLLVFIM SLLFTYSHHS MATLPYLDSG ALGGTHRVKL
60 70 80 90 100
VPGYSGLQRL GKEGLLGRNC ACSRCMGDAS TSEWFDSHFD GNISPVWTRD
110 120 130 140 150
NMNLPPDVQR WWMMLQPQFK SHNTNEVLEK LFQIVPGENP YRFRDPQQCR
160 170 180 190 200
RCAVVGNSGN LRGSGYGQEV DSHNFIMRMN QAPTVGFEKD VGSRTTHHFM
210 220 230 240 250
YPESAKNLPA NVSFVLVPFK ALDLMWIASA LSTGQIRFTY APVKSFLRVD
260 270 280 290 300
KEKVQIYNPA FFKYIHDRWT EHHGRYPSTG MLVLFFALHV CDEVNVYGFG
310 320 330 340 350
ADSRGNWHHY WENNRYAGEF RKTGVHDADF EAHIIDMLAK ASKIEVYRGN
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketD3Z3V2 | D3Z3V2_MOUSE | CMP-N-acetylneuraminate-beta-galact... | St3gal2 | 303 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 309 – 310 | HY → RH in CAA54294 (PubMed:8144500).Curated | 2 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X76989 mRNA Translation: CAA54294.1 AK053827 mRNA Translation: BAC35543.1 AK131653 mRNA Translation: BAE20742.1 CH466525 Genomic DNA Translation: EDL11478.1 BC066064 mRNA Translation: AAH66064.1 |
CCDSi | CCDS22667.1 |
PIRi | A54420 |
RefSeqi | NP_033205.2, NM_009179.3 XP_006530849.1, XM_006530786.2 XP_006530850.1, XM_006530787.2 XP_006530851.1, XM_006530788.1 XP_017168113.1, XM_017312624.1 |
Genome annotation databases
Ensembli | ENSMUST00000034197; ENSMUSP00000034197; ENSMUSG00000031749 |
GeneIDi | 20444 |
KEGGi | mmu:20444 |
UCSCi | uc009nlk.2, mouse |
Similar proteinsi
Cross-referencesi
Web resourcesi
Functional Glycomics Gateway - GTase ST3Gal II |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X76989 mRNA Translation: CAA54294.1 AK053827 mRNA Translation: BAC35543.1 AK131653 mRNA Translation: BAE20742.1 CH466525 Genomic DNA Translation: EDL11478.1 BC066064 mRNA Translation: AAH66064.1 |
CCDSi | CCDS22667.1 |
PIRi | A54420 |
RefSeqi | NP_033205.2, NM_009179.3 XP_006530849.1, XM_006530786.2 XP_006530850.1, XM_006530787.2 XP_006530851.1, XM_006530788.1 XP_017168113.1, XM_017312624.1 |
3D structure databases
SMRi | Q11204 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10090.ENSMUSP00000034197 |
Chemistry databases
SwissLipidsi | SLP:000001389 |
Protein family/group databases
CAZyi | GT29, Glycosyltransferase Family 29 |
PTM databases
GlyGeni | Q11204, 1 site |
PhosphoSitePlusi | Q11204 |
Proteomic databases
MaxQBi | Q11204 |
PaxDbi | Q11204 |
PRIDEi | Q11204 |
Protocols and materials databases
Antibodypediai | 2529, 135 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000034197; ENSMUSP00000034197; ENSMUSG00000031749 |
GeneIDi | 20444 |
KEGGi | mmu:20444 |
UCSCi | uc009nlk.2, mouse |
Organism-specific databases
CTDi | 6483 |
MGIi | MGI:99427, St3gal2 |
Phylogenomic databases
eggNOGi | KOG2692, Eukaryota |
GeneTreei | ENSGT00940000156356 |
HOGENOMi | CLU_032020_2_0_1 |
InParanoidi | Q11204 |
OMAi | YIHDHWT |
OrthoDBi | 891104at2759 |
TreeFami | TF354325 |
Enzyme and pathway databases
UniPathwayi | UPA00378 |
Reactomei | R-MMU-2022854, Keratan sulfate biosynthesis R-MMU-4085001, Sialic acid metabolism R-MMU-977068, Termination of O-glycan biosynthesis |
Miscellaneous databases
BioGRID-ORCSi | 20444, 0 hits in 17 CRISPR screens |
ChiTaRSi | St3gal2, mouse |
PROi | PR:Q11204 |
RNActi | Q11204, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000031749, Expressed in cerebellum and 277 other tissues |
ExpressionAtlasi | Q11204, baseline and differential |
Genevisiblei | Q11204, MM |
Family and domain databases
Gene3Di | 3.90.1480.20, 1 hit |
InterProi | View protein in InterPro IPR001675, Glyco_trans_29 IPR038578, GT29-like_sf IPR012163, Sialyl_trans |
Pfami | View protein in Pfam PF00777, Glyco_transf_29, 1 hit |
PIRSFi | PIRSF005557, Sialyl_trans, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SIA4B_MOUSE | |
Accessioni | Q11204Primary (citable) accession number: Q11204 Secondary accession number(s): Q8BPL0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | July 27, 2011 | |
Last modified: | December 2, 2020 | |
This is version 148 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families