SIA4B_RAT
ID SIA4B_RAT Reviewed; 350 AA.
AC Q11205;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2;
DE Short=Alpha 2,3-ST 2;
DE Short=Beta-galactoside alpha-2,3-sialyltransferase 2;
DE EC=2.4.99.4 {ECO:0000269|PubMed:8144500};
DE AltName: Full=Gal-NAc6S;
DE AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase {ECO:0000303|PubMed:8144500};
DE AltName: Full=Monosialoganglioside sialyltransferase;
DE EC=2.4.99.2 {ECO:0000305|PubMed:8144500};
DE AltName: Full=ST3Gal II;
DE Short=ST3GalII;
DE AltName: Full=ST3GalA.2;
DE AltName: Full=Sialyltransferase 4B;
DE Short=SIAT4-B;
GN Name=St3gal2; Synonyms=Siat4b, Siat5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC TISSUE=Brain;
RX PubMed=8144500; DOI=10.1016/s0021-9258(17)36985-5;
RA Lee Y.-C., Kojima N., Wada E., Kurosawa N., Nakaoka T., Hamamoto T.,
RA Tsuji S.;
RT "Cloning and expression of cDNA for a new type of Gal beta 1,3GalNAc alpha
RT 2,3-sialyltransferase.";
RL J. Biol. Chem. 269:10028-10033(1994).
CC -!- FUNCTION: A beta-galactoside alpha2-3 sialyltransferase primarily
CC involved in terminal sialylation of ganglio and globo series
CC glycolipids (PubMed:8144500). Catalyzes the transfer of sialic acid (N-
CC acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-
CC Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates
CC through an alpha2-3 linkage. Sialylates GM1/GM1a, GA1/asialo-GM1
CC gangliosides to form GD1a and GM1b, respectively (PubMed:8144500).
CC Together with ST3GAL3, primarily responsible for biosynthesis of brain
CC gangliosides that function as ligand for myelin-associated glycoprotein
CC MAG on axons, regulating MAG expression and axonal myelin stability and
CC regeneration (By similarity). Responsible for the sialylation of the
CC pluripotent stem cell- and cancer stem cell-associated antigen SSEA3,
CC forming SSEA4 (By similarity). Sialylates with low efficiency
CC asialofetuin, presumably onto O-glycosidically linked Galbeta-(1->3)-
CC GalNAc-O-Ser (PubMed:8144500). {ECO:0000250|UniProtKB:Q11204,
CC ECO:0000250|UniProtKB:Q16842, ECO:0000269|PubMed:8144500}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:21616,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133470, ChEBI:CHEBI:139596; EC=2.4.99.4;
CC Evidence={ECO:0000269|PubMed:8144500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617;
CC Evidence={ECO:0000305|PubMed:8144500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 (d18:1(4E)) =
CC CMP + ganglioside GD1a (d18:1(4E)) + H(+); Xref=Rhea:RHEA:18021,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:77709, ChEBI:CHEBI:78445; EC=2.4.99.2;
CC Evidence={ECO:0000305|PubMed:8144500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022;
CC Evidence={ECO:0000305|PubMed:8144500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1
CC (d18:1(4E)/18:0) = CMP + ganglioside GD1a (18:1(4E)/18:0) + H(+);
CC Xref=Rhea:RHEA:48248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:73110, ChEBI:CHEBI:90153;
CC Evidence={ECO:0000269|PubMed:8144500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48249;
CC Evidence={ECO:0000305|PubMed:8144500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 = CMP +
CC ganglioside GM1b + H(+); Xref=Rhea:RHEA:48244, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:88069,
CC ChEBI:CHEBI:90151; Evidence={ECO:0000269|PubMed:8144500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48245;
CC Evidence={ECO:0000305|PubMed:8144500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GA1 (d18:1(4E)) =
CC CMP + ganglioside GM1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47560,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27938, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568;
CC Evidence={ECO:0000305|PubMed:8144500};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561;
CC Evidence={ECO:0000305|PubMed:8144500};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + globoside GalGb4Cer = CMP +
CC globoside MSGG + H(+); Xref=Rhea:RHEA:65372, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140623,
CC ChEBI:CHEBI:140691; Evidence={ECO:0000250|UniProtKB:Q16842};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65373;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:8144500}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:8144500}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homodimer formation occurs in the
CC endoplasmic reticulum. {ECO:0000250|UniProtKB:Q16842}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q16842}; Single-pass type II membrane protein.
CC Secreted. Note=Membrane-bound form distributed along the Golgi
CC cisternae, mainly in proximal compartments (By similarity). Secreted
CC into the body fluid. {ECO:0000250|UniProtKB:Q16842}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- PTM: N-glycosylated; necessary for proper exit from endoplasmic
CC reticulum and trafficking to the Golgi apparatus.
CC {ECO:0000250|UniProtKB:Q16842}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; X76988; CAA54293.1; -; mRNA.
DR PIR; B54420; B54420.
DR RefSeq; NP_113883.2; NM_031695.2.
DR AlphaFoldDB; Q11205; -.
DR SMR; Q11205; -.
DR STRING; 10116.ENSRNOP00000024248; -.
DR BindingDB; Q11205; -.
DR ChEMBL; CHEMBL3638362; -.
DR SwissLipids; SLP:000001414; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q11205; 1 site.
DR PaxDb; Q11205; -.
DR PRIDE; Q11205; -.
DR GeneID; 64442; -.
DR KEGG; rno:64442; -.
DR UCSC; RGD:68413; rat.
DR CTD; 6483; -.
DR RGD; 68413; St3gal2.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q11205; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; Q11205; -.
DR BRENDA; 2.4.99.4; 5301.
DR Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-RNO-4085001; Sialic acid metabolism.
DR Reactome; R-RNO-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q11205; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047288; F:monosialoganglioside sialyltransferase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:RGD.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; IDA:UniProtKB.
DR GO; GO:0010707; P:globoside biosynthetic process via lactosylceramide; ISS:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; ISO:RGD.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; ISO:RGD.
DR GO; GO:0030259; P:lipid glycosylation; ISO:RGD.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; ISO:RGD.
DR GO; GO:0006486; P:protein glycosylation; IDA:RGD.
DR GO; GO:1990743; P:protein sialylation; ISO:RGD.
DR GO; GO:0097503; P:sialylation; ISO:RGD.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR InterPro; IPR012163; Sialyl_trans.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR PIRSF; PIRSF005557; Sialyl_trans; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Secreted; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="CMP-N-acetylneuraminate-beta-galactosamide-alpha-
FT 2,3-sialyltransferase 2"
FT /id="PRO_0000149261"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..350
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 70..75
FT /evidence="ECO:0000250"
FT DISULFID 72..149
FT /evidence="ECO:0000250"
FT DISULFID 152..291
FT /evidence="ECO:0000250"
SQ SEQUENCE 350 AA; 40166 MW; 87E6494FB02D0BE1 CRC64;
MKCSLRVWFL SMAFLLVFIM SLLFTYSHHS MATLPYLDSG TLGGTHRVKL VPGYTGQQRL
VKEGLSGKSC TCSRCMGDAG TSEWFDSHFD SNISPVWTRD NMNLTPDVQR WWMMLQPQFK
SHNTNEVLEK LFQIVPGENP YRFRDPQQCR RCAVVGNSGN LRGSGYGQEV DSHNFIMRMN
QAPTVGFEKD VGSRTTHHFM YPESAKNLPA NVSFVLVPFK ALDLMWIASA LSTGQIRFTY
APVKSFLRVD KEKVQIYNPA FFKYIHDRWT EHHGRYPSTG MLVLFFALHV CDEVNVYGFG
ADSRGNWHHY WENNRYAGEF RKTGVHDADF EAHIIDILAK ASKIEVYRGN
