SIA4A_PANTR
ID SIA4A_PANTR Reviewed; 340 AA.
AC Q6KB59;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1;
DE Short=Alpha 2,3-ST 1;
DE Short=Beta-galactoside alpha-2,3-sialyltransferase 1;
DE EC=2.4.99.4 {ECO:0000250|UniProtKB:Q11201};
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:Q11201};
DE AltName: Full=SIATFL;
DE AltName: Full=ST3Gal I;
DE Short=ST3GalI;
DE AltName: Full=ST3GalA.1;
DE AltName: Full=ST3O;
DE AltName: Full=Sialyltransferase 4A;
DE Short=SIAT4-A;
GN Name=ST3GAL1; Synonyms=SIAT4, SIAT4A;
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 involved in
CC terminal sialylation of glycoproteins and glycolipids. Catalyzes the
CC transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the
CC nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-
CC terminated glycoconjugates through an alpha2-3 linkage. Adds sialic
CC acid to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, which is
CC a major structure of mucin-type O-glycans. As part of a homeostatic
CC mechanism that regulates CD8-positive T cell numbers, sialylates core 1
CC O-glycans of T cell glycoproteins, SPN/CD43 and PTPRC/CD45. Prevents
CC premature apoptosis of thymic CD8-positive T cells prior to peripheral
CC emigration, whereas in the secondary lymphoid organs controls the
CC survival of CD8-positive memory T cells generated following a
CC successful immune response. Transfers sialic acid to asialofetuin,
CC presumably onto Galbeta-(1->3)-GalNAc-O-Ser. Sialylates GM1a, GA1 and
CC GD1b gangliosides to form GD1a, GM1b and GT1b, respectively.
CC {ECO:0000250|UniProtKB:P54751, ECO:0000250|UniProtKB:Q11201}.
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:Q11201};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617;
CC Evidence={ECO:0000250|UniProtKB:Q11201};
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:Q11201};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48261;
CC Evidence={ECO:0000250|UniProtKB:Q11201};
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:Q11201};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022;
CC Evidence={ECO:0000250|UniProtKB:Q11201};
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:P54751};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48249;
CC Evidence={ECO:0000250|UniProtKB:P54751};
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:Q11201};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48245;
CC Evidence={ECO:0000250|UniProtKB:Q11201};
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:Q02745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561;
CC Evidence={ECO:0000250|UniProtKB:Q02745};
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:P54751};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48241;
CC Evidence={ECO:0000250|UniProtKB:P54751};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P54751, ECO:0000250|UniProtKB:Q11201}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:P54751,
CC ECO:0000250|UniProtKB:Q11201}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q11201}; Single-pass type II membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q11201}; Single-pass type II membrane protein
CC {ECO:0000255}. Secreted. Note=Membrane-bound form in medial and trans
CC cisternae of Golgi (By similarity). Secreted into the body fluid.
CC {ECO:0000250|UniProtKB:Q11201}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; AJ744803; CAG32839.1; -; mRNA.
DR RefSeq; NP_001009037.1; NM_001009037.1.
DR AlphaFoldDB; Q6KB59; -.
DR SMR; Q6KB59; -.
DR STRING; 9598.ENSPTRP00000054506; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q6KB59; -.
DR GeneID; 450114; -.
DR KEGG; ptr:450114; -.
DR CTD; 6482; -.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q6KB59; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:1990675; C:Golgi medial cisterna membrane; ISS:UniProtKB.
DR GO; GO:1990676; C:Golgi trans cisterna 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:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
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:0010706; P:ganglioside biosynthetic process via lactosylceramide; ISS:UniProtKB.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:1990743; P:protein sialylation; ISS:UniProtKB.
DR GO; GO:0097503; P:sialylation; ISS:UniProtKB.
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..340
FT /note="CMP-N-acetylneuraminate-beta-galactosamide-alpha-
FT 2,3-sialyltransferase 1"
FT /id="PRO_0000149255"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..340
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..64
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT DISULFID 61..139
FT /evidence="ECO:0000250|UniProtKB:Q02745"
FT DISULFID 142..281
FT /evidence="ECO:0000250|UniProtKB:Q02745"
SQ SEQUENCE 340 AA; 39059 MW; E225885CC83EB501 CRC64;
MVTLRKRTLK VLTFLVLFIF LTSFFLNYSH TMVATTWFPK QMVLELSENL KRLIKHRPCT
CTHCIGQRKL SAWFDERFNQ TVQPLLTAQN ALLEDDTYRW WLRLQREKKP NNLNDTIKEL
FRVVPGNVDP MLEKRSVGCR RCAVVGNSGN LRESSYGPEI DSHDFVLRMN KAPTAGFEAD
VGTKTTHHLV YPESFRELGD NVSMILVPFK TIDLEWVVSA ITTGTISHTY TPVLVKIRVK
QDKILIYHPA FIKYVFDNWL QGHGRYPSTG ILSVIFSMHV CDEVDLYGFG ADSKGNWHHY
WENNPSAGAF RKTGVHDADF ESNVTATLAA INKIRIFKGR
