SIA4C_RAT
ID SIA4C_RAT Reviewed; 333 AA.
AC P61131;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
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 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].
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.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7798936; DOI=10.1046/j.1471-4159.1995.64010385.x;
RA Freischuetz B., Saito M., Rahmann H., Yu R.K.;
RT "Characterization of sialyltransferase-IV activity and its involvement in
RT the c-pathway of brain ganglioside metabolism.";
RL J. Neurochem. 64:385-393(1995).
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 (Probable).
CC Synthesizes ganglioside LM1 (IV3Neu5Ac-nLc4Cer), a major structural
CC component of peripheral nerve myelin (By similarity).
CC {ECO:0000250|UniProtKB:Q11206, ECO:0000250|UniProtKB:Q91Y74,
CC ECO:0000305|PubMed:7798936}.
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:0000305|PubMed:7798936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47589;
CC Evidence={ECO:0000305|PubMed:7798936};
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 Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; AJ626825; CAF25183.1; -; mRNA.
DR EMBL; BC089057; AAH89057.1; -; mRNA.
DR RefSeq; NP_976082.1; NM_203337.2.
DR RefSeq; XP_006242851.1; XM_006242789.3.
DR RefSeq; XP_008764282.1; XM_008766060.1.
DR AlphaFoldDB; P61131; -.
DR SMR; P61131; -.
DR STRING; 10116.ENSRNOP00000013243; -.
DR SwissLipids; SLP:000001443; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; P61131; 4 sites.
DR PaxDb; P61131; -.
DR GeneID; 363040; -.
DR KEGG; rno:363040; -.
DR UCSC; RGD:1303068; rat.
DR CTD; 6484; -.
DR RGD; 1303068; St3gal4.
DR VEuPathDB; HostDB:ENSRNOG00000009850; -.
DR eggNOG; KOG2692; Eukaryota.
DR HOGENOM; CLU_032020_1_0_1; -.
DR InParanoid; P61131; -.
DR OMA; KSPPLCM; -.
DR OrthoDB; 891104at2759; -.
DR PhylomeDB; P61131; -.
DR TreeFam; TF354325; -.
DR Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-RNO-4085001; Sialic acid metabolism.
DR Reactome; R-RNO-9037629; Lewis blood group biosynthesis.
DR Reactome; R-RNO-975577; N-Glycan antennae elongation.
DR Reactome; R-RNO-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:P61131; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000009850; Expressed in ovary and 20 other tissues.
DR Genevisible; P61131; RN.
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; ISO:RGD.
DR GO; GO:0047288; F:monosialoganglioside sialyltransferase activity; IDA:RGD.
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:0050890; P:cognition; ISO:RGD.
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: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; ISO: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; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..333
FT /note="CMP-N-acetylneuraminate-beta-galactosamide-alpha-
FT 2,3-sialyltransferase 4"
FT /id="PRO_0000149265"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..333
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..273
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 38043 MW; 8D086A0F73C79791 CRC64;
MTSKSHWKLL ALALVLVVVM VWYSISREDR YIEFFYFPVS EKKEPCFQGE AERQASKIFG
NHSREQPIFL QLKDYFWVKT PSAYELPFGT KGSEDLLLRV LAITSYSIPE SIQSLECRRC
VVVGNGHRLK NSSLGGVINK YDVVIRLNNA PVAGYEGDVG SKTTIRLFYP ESAHFDPKIE
NNPDTLLVLV AFKAMDFHWI ETILSDKKRV RKGFWKQPPL IWDVNPKQIR ILNPFFMEIA
ADKLLSLPIQ QPRKIKQKPT TGLLAITLAL HLCDLVHIAG FGYPDAYNKK QTIHYYEQIT
LKSMAGSGHN VSQEAVAIKR MLEMGAVKNL TYF
