SIA4C_PANTR
ID SIA4C_PANTR Reviewed; 328 AA.
AC P61130;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4;
DE Short=Alpha 2,3-ST 4;
DE Short=Beta-galactoside alpha-2,3-sialyltransferase 4;
DE EC=2.4.99.2 {ECO:0000250|UniProtKB:Q11206};
DE EC=2.4.99.4 {ECO:0000250|UniProtKB:Q11206};
DE AltName: Full=Alpha 2,3-sialyltransferase IV;
DE AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase;
DE AltName: Full=Gal-beta-1,4-GlcNAc-alpha-2,3-sialyltransferase;
DE AltName: Full=N-acetyllactosaminide alpha-2,3-sialyltransferase;
DE EC=2.4.99.6 {ECO:0000250|UniProtKB:Q11206};
DE AltName: Full=ST3Gal IV;
DE Short=ST3GalIV;
DE AltName: Full=Sialyltransferase 4C;
DE Short=SIAT4-C;
GN Name=ST3GAL4; Synonyms=SIAT4C;
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 (JAN-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)-
CC GalNAc- and Galbeta-(1->4)-GlcNAc-terminated glycoconjugates through an
CC alpha2-3 linkage (By similarity). Plays a major role in hemostasis.
CC Responsible for sialylation of plasma VWF/von Willebrand factor,
CC preventing its recognition by asialoglycoprotein receptors (ASGPR) and
CC subsequent clearance. Regulates ASGPR-mediated clearance of platelets
CC (By similarity). Participates in the biosynthesis of the sialyl Lewis X
CC epitopes, both on O- and N-glycans, which are recognized by SELE/E-
CC selectin, SELP/P-selectin and SELL/L-selectin. Essential for selectin-
CC mediated rolling and adhesion of leukocytes during extravasation (By
CC similarity). Contributes to adhesion and transendothelial migration of
CC neutrophils likely through terminal sialylation of CXCR2 (By
CC similarity). In glycosphingolipid biosynthesis, sialylates GM1 and GA1
CC gangliosides to form GD1a and GM1b, respectively (By similarity).
CC Metabolizes brain c-series ganglioside GT1c forming GQ1c (By
CC similarity). Synthesizes ganglioside LM1 (IV3Neu5Ac-nLc4Cer), a major
CC structural component of peripheral nerve myelin (By similarity).
CC {ECO:0000250|UniProtKB:P61131, ECO:0000250|UniProtKB:Q11206,
CC ECO:0000250|UniProtKB:Q91Y74}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-
CC galactosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:52380,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:136588, ChEBI:CHEBI:136589; EC=2.4.99.2;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52381;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
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:Q11206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21617;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-
CC glucosaminyl derivative + CMP + H(+); Xref=Rhea:RHEA:52316,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:136545; EC=2.4.99.6;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52317;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
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:Q11206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18022;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
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:Q11206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47561;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GT1c (d18:1(4E)) =
CC CMP + ganglioside GQ1c (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47588,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:87789, ChEBI:CHEBI:87791;
CC Evidence={ECO:0000250|UniProtKB:P61131};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47589;
CC Evidence={ECO:0000250|UniProtKB:P61131};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer + CMP-N-acetyl-beta-neuraminate = a
CC neolactoside IV(3)-alpha-NeuAc-nLc4Cer + CMP + H(+);
CC Xref=Rhea:RHEA:65432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:90376, ChEBI:CHEBI:90390;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65433;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer(d18:1(4E)) + CMP-N-acetyl-beta-
CC neuraminate = a neolactoside IV(3)-alpha-NeuAc-nLc4Cer(d18:1(4E)) +
CC CMP + H(+); Xref=Rhea:RHEA:18913, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17006, ChEBI:CHEBI:57812, ChEBI:CHEBI:58665,
CC ChEBI:CHEBI:60377; EC=2.4.99.6;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18914;
CC Evidence={ECO:0000250|UniProtKB:Q11206};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q11206}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:Q11206}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Secreted {ECO:0000250}. Note=Membrane-bound form in trans cisternae of
CC Golgi. Secreted into the body fluid. {ECO:0000250}.
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; AJ626824; CAF25182.1; -; mRNA.
DR RefSeq; NP_001032390.1; NM_001037313.1.
DR AlphaFoldDB; P61130; -.
DR SMR; P61130; -.
DR STRING; 9598.ENSPTRP00000007620; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; P61130; -.
DR GeneID; 466845; -.
DR KEGG; ptr:466845; -.
DR CTD; 6484; -.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; P61130; -.
DR OrthoDB; 891104at2759; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0047288; F:monosialoganglioside sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0008118; F:N-acetyllactosaminide alpha-2,3-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004513; F:neolactotetraosylceramide alpha-2,3-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISS:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
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..328
FT /note="CMP-N-acetylneuraminate-beta-galactosamide-alpha-
FT 2,3-sialyltransferase 4"
FT /id="PRO_0000149264"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..328
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..268
FT /evidence="ECO:0000250"
SQ SEQUENCE 328 AA; 37274 MW; 38B319C82223CD31 CRC64;
MCPAGWKLLA MLALVLVVMV WYSISREDSF YFPIPEKKEP CLQGEAESKA SKLFGNYSRD
QPIFLRLEDY FWVKTPSAYE LPYGTKGSED LLLRVLAITS SSIRKNIQSL RCRRCVVVGN
GHRLRNSSLG DAINKYDVVI RLNNAPVAGY EGDVGSKTTM RLFYPESAHF DPKVENNPDT
LLVLVAFKAM DFHWIETILS DKKRVRKGFW KQPPLIWDVN PKQIRILNPF FMEIAADKLL
SLPMQQPRKI KQKPTTGLLA ITLALHLCDL VHIAGFGYPD AYNKKQTIHY YEQITLKSMA
GSGHNVSQEA LAIKRMLEMG AVKNLTSF
