SIA4B_PANTR
ID SIA4B_PANTR Reviewed; 350 AA.
AC Q6KB58;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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:0000250|UniProtKB:Q16842};
DE AltName: Full=Gal-NAc6S;
DE AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase;
DE AltName: Full=Monosialoganglioside sialyltransferase;
DE EC=2.4.99.2 {ECO:0000250|UniProtKB:Q16842};
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;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Harduin-Lepers A., Martinez-Duncker I., Mollicone R., Delannoy P.,
RA Oriol R.;
RT "Phylogeny of sialyltransferases.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A beta-galactoside alpha2-3 sialyltransferase primarily
CC involved in terminal sialylation of ganglio and globo series
CC glycolipids. Catalyzes the transfer of sialic acid (N-acetyl-neuraminic
CC acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor
CC Galbeta-(1->3)-GalNAc-terminated glycoconjugates through an alpha2-3
CC linkage. Sialylates GM1/GM1a, GA1/asialo-GM1 and GD1b gangliosides to
CC form GD1a, GM1b and GT1b, respectively (By similarity). Together with
CC ST3GAL3, primarily responsible for biosynthesis of brain GD1a and GT1b
CC that function as ligands for myelin-associated glycoprotein MAG on
CC axons, regulating MAG expression and axonal myelin stability and
CC regeneration. Via GT1b regulates TLR2 signaling in spinal cord
CC microglia in response to nerve injury (By similarity). Responsible for
CC the sialylation of the pluripotent stem cell- and cancer stem cell-
CC associated antigen SSEA3, forming SSEA4 (By similarity). Sialylates
CC with low efficiency asialofetuin, presumably onto O-glycosidically
CC linked Galbeta-(1->3)-GalNAc-O-Ser (By similarity).
CC {ECO:0000250|UniProtKB:Q11204, ECO:0000250|UniProtKB:Q16842}.
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:0000250|UniProtKB:Q16842};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1 = CMP +
CC ganglioside GD1a + H(+); Xref=Rhea:RHEA:48260, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82637,
CC ChEBI:CHEBI:82639; Evidence={ECO:0000250|UniProtKB:Q16842};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48261;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
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:0000250|UniProtKB:Q16842};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
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:0000250|UniProtKB:Q16842};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48249;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
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:0000250|UniProtKB:Q16842};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48245;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
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:0000250|UniProtKB:Q16842};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1b = CMP +
CC ganglioside GT1b + H(+); Xref=Rhea:RHEA:48240, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:82939,
CC ChEBI:CHEBI:82940; Evidence={ECO:0000250|UniProtKB:Q16842};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48241;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1b (d18:1(4E)) =
CC CMP + ganglioside GT1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47572,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78452, ChEBI:CHEBI:87785;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47573;
CC Evidence={ECO:0000250|UniProtKB:Q16842};
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:0000250|UniProtKB:Q16842}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:Q16842}.
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 {ECO:0000255}. Secreted {ECO:0000250}. Note=Membrane-bound form
CC distributed along the Golgi cisternae, mainly in proximal compartments
CC (By similarity). Secreted into the body fluid. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q16842}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000250}.
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; AJ744804; CAG32840.1; -; mRNA.
DR RefSeq; NP_001032384.1; NM_001037307.1.
DR AlphaFoldDB; Q6KB58; -.
DR SMR; Q6KB58; -.
DR STRING; 9598.ENSPTRP00000014180; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q6KB58; -.
DR GeneID; 454214; -.
DR KEGG; ptr:454214; -.
DR CTD; 6483; -.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q6KB58; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; 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:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047288; F:monosialoganglioside sialyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; ISS:UniProtKB.
DR GO; GO:0010707; P:globoside biosynthetic process via lactosylceramide; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript 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_0000149260"
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; 40074 MW; FCE9932A2D9CB73A CRC64;
MKCSLRVWFL SVAFLLVFIM SLLFTYSHHS MATLPYLDSG ALDGTHRVKL VPGYAGLQRL
SKERLSGKSC ACRRCMGDAG ASDWFDSHFD GNISPVWTRE NMDLPPDVQR WWMMLQPQFK
SHNTNEVLEK LFQIVPGENP YRFRDPHQCR RCAVVGNSGN LRGSGYGQDV DGHNFIMRMN
QAPTVGFEQD VGSRTTHHFM YPESAKNLPA NVSFVLVPFK ALDLLWIASA LSTGQIRFTY
APVKSFLRVD KEKVQIYNPA FFKYIHDRWT EHHGRYPSTG MLVLFFALHV CDEVNVYGFG
ADSRGNWHHY WENNRYAGEF RKTGVHDADF EVHIIDMLAK ASKIEVYGGN
