UniProtKB - Q11205 (SIA4B_RAT)
Protein
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
Gene
St3gal2
Organism
Rattus norvegicus (Rat)
Status
Functioni
A beta-galactoside alpha2-3 sialyltransferase primarily involved in terminal sialylation of ganglio and globo series glycolipids (PubMed:8144500). 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 gangliosides to form GD1a and GM1b, respectively (PubMed:8144500). Together with ST3GAL3, primarily responsible for biosynthesis of brain gangliosides that function as ligand for myelin-associated glycoprotein MAG on axons, regulating MAG expression and axonal myelin stability and regeneration (By similarity). 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 similarity1 Publication
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+1 PublicationEC:2.4.99.41 PublicationThis reaction proceeds in the forward1 Publication 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 forward1 Publication 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 forwardBy similarity direction.
: 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.1 PublicationView 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: RGD
- monosialoganglioside sialyltransferase activity Source: RGD
- sialyltransferase activity Source: RGD
GO - Biological processi
- glycolipid biosynthetic process Source: RGD
- glycoprotein biosynthetic process Source: RGD
- lipid glycosylation Source: RGD
- oligosaccharide biosynthetic process Source: RGD
- protein glycosylation Source: RGD
- protein sialylation Source: RGD
- sialylation Source: RGD
Keywordsi
Molecular function | Glycosyltransferase, Transferase |
Biological process | Lipid metabolism |
Enzyme and pathway databases
BRENDAi | 2.4.99.2, 5301 2.4.99.4, 5301 |
Reactomei | R-RNO-2022854, Keratan sulfate biosynthesis R-RNO-4085001, Sialic acid metabolism R-RNO-977068, Termination of O-glycan biosynthesis |
UniPathwayi | UPA00378 |
Protein family/group databases
CAZyi | GT29, Glycosyltransferase Family 29 |
Chemistry databases
SwissLipidsi | SLP:000001414 |
Names & Taxonomyi
Protein namesi | Recommended name: CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2 (EC:2.4.99.41 Publication)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 | Name:St3gal2 Synonyms:Siat4b, Siat5 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 68413, St3gal2 |
Subcellular locationi
Golgi apparatus
- Golgi stack membrane By similarity; Single-pass type II membrane protein
Extracellular region or secreted
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, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000149261 | 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
PaxDbi | Q11205 |
PRIDEi | Q11205 |
PTM databases
GlyGeni | Q11205, 1 site |
Interactioni
Subunit structurei
Homodimer; disulfide-linked. Homodimer formation occurs in the endoplasmic reticulum.
By similarityProtein-protein interaction databases
STRINGi | 10116.ENSRNOP00000024248 |
Chemistry databases
BindingDBi | Q11205 |
Family & Domainsi
Sequence similaritiesi
Belongs to the glycosyltransferase 29 family.Curated
Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG2692, Eukaryota |
InParanoidi | Q11205 |
OrthoDBi | 891104at2759 |
PhylomeDBi | Q11205 |
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
Q11205-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKCSLRVWFL SMAFLLVFIM SLLFTYSHHS MATLPYLDSG TLGGTHRVKL
60 70 80 90 100
VPGYTGQQRL VKEGLSGKSC TCSRCMGDAG TSEWFDSHFD SNISPVWTRD
110 120 130 140 150
NMNLTPDVQR 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 EAHIIDILAK ASKIEVYRGN
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketG3V8B2 | G3V8B2_RAT | CMP-N-acetylneuraminate-beta-galact... | St3gal2 rCG_51602 | 350 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X76988 mRNA Translation: CAA54293.1 |
PIRi | B54420 |
RefSeqi | NP_113883.2, NM_031695.2 |
Genome annotation databases
GeneIDi | 64442 |
KEGGi | rno:64442 |
UCSCi | RGD:68413, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X76988 mRNA Translation: CAA54293.1 |
PIRi | B54420 |
RefSeqi | NP_113883.2, NM_031695.2 |
3D structure databases
SMRi | Q11205 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000024248 |
Chemistry databases
BindingDBi | Q11205 |
ChEMBLi | CHEMBL3638362 |
SwissLipidsi | SLP:000001414 |
Protein family/group databases
CAZyi | GT29, Glycosyltransferase Family 29 |
PTM databases
GlyGeni | Q11205, 1 site |
Proteomic databases
PaxDbi | Q11205 |
PRIDEi | Q11205 |
Genome annotation databases
GeneIDi | 64442 |
KEGGi | rno:64442 |
UCSCi | RGD:68413, rat |
Organism-specific databases
CTDi | 6483 |
RGDi | 68413, St3gal2 |
Phylogenomic databases
eggNOGi | KOG2692, Eukaryota |
InParanoidi | Q11205 |
OrthoDBi | 891104at2759 |
PhylomeDBi | Q11205 |
Enzyme and pathway databases
UniPathwayi | UPA00378 |
BRENDAi | 2.4.99.2, 5301 2.4.99.4, 5301 |
Reactomei | R-RNO-2022854, Keratan sulfate biosynthesis R-RNO-4085001, Sialic acid metabolism R-RNO-977068, Termination of O-glycan biosynthesis |
Miscellaneous databases
PROi | PR:Q11205 |
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_RAT | |
Accessioni | Q11205Primary (citable) accession number: Q11205 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | December 2, 2020 | |
This is version 125 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families