SIA7C_RAT
ID SIA7C_RAT Reviewed; 305 AA.
AC Q64686;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3;
DE EC=2.4.99.7 {ECO:0000269|PubMed:8631773};
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase III;
DE AltName: Full=ST6GalNAc III {ECO:0000303|PubMed:8631773};
DE Short=ST6GalNAcIII;
DE AltName: Full=STY;
DE AltName: Full=Sialyltransferase 7C;
DE Short=SIAT7-C;
GN Name=St6galnac3; Synonyms=Siat7c;
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 TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8631773; DOI=10.1074/jbc.271.13.7450;
RA Sjoberg E.R., Kitagawa H., Glushka J., van Halbeek H., Paulson J.C.;
RT "Molecular cloning of a developmentally regulated N-acetylgalactosamine
RT alpha2,6-sialyltransferase specific for sialylated glycoconjugates.";
RL J. Biol. Chem. 271:7450-7459(1996).
CC -!- FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or
CC NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-
CC beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an
CC alpha-2,6-linkage. Produces branched type disialyl structures by
CC transfer of a sialyl group onto a GalNAc residue inside the backbone
CC core chains. ST6GalNAcIII prefers glycolipids to glycoproteins,
CC predominantly catalyzing the biosynthesis of ganglioside GD1alpha from
CC GM1b (PubMed:8631773). GD1alpha is a critical molecule in the
CC communication and interaction between neuronal cells and their
CC supportive cells, particularly in brain tissues, and functions as an
CC adhesion molecule in the process of metastasis (By similarity).
CC Sialylation of glycoproteins or glycosphingolipids is very important in
CC tumor development, neuronal development, nerve repair, immunological
CC processes and regulation of hormone sensitivity (By similarity).
CC {ECO:0000250|UniProtKB:Q8NDV1, ECO:0000250|UniProtKB:Q9QYJ1,
CC ECO:0000269|PubMed:8631773}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative +
CC CMP-N-acetyl-beta-neuraminate = an alpha-Neu5Ac-(2->3)-beta-D-Gal-
CC (1->3)-[alpha-Neu5Ac-(2->6)]-D-GlcNAc-R + CMP + H(+);
CC Xref=Rhea:RHEA:53896, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:146021, ChEBI:CHEBI:149714;
CC EC=2.4.99.7; Evidence={ECO:0000269|PubMed:8631773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53897;
CC Evidence={ECO:0000305|PubMed:8631773};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b = a
CC ganglioside GD1alpha + CMP + H(+); Xref=Rhea:RHEA:48316,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:90151, ChEBI:CHEBI:90246;
CC Evidence={ECO:0000269|PubMed:8631773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48317;
CC Evidence={ECO:0000305|PubMed:8631773};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) =
CC a ganglioside GD1alpha (d18:1(4E)) + CMP + H(+);
CC Xref=Rhea:RHEA:41968, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78568, ChEBI:CHEBI:78569;
CC Evidence={ECO:0000250|UniProtKB:Q9WUV2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41969;
CC Evidence={ECO:0000250|UniProtKB:Q9WUV2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + globoside MSGG = CMP +
CC globoside DSGG + H(+); Xref=Rhea:RHEA:56088, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140623,
CC ChEBI:CHEBI:140624; Evidence={ECO:0000250|UniProtKB:Q8NDV1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56089;
CC Evidence={ECO:0000250|UniProtKB:Q8NDV1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc]-L-
CC Ser-[protein] + CMP-N-acetyl-beta-neuraminate = 3-O-{alpha-Neu5Ac-
CC (2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-alpha-D-GalNAc}-L-Ser-
CC [protein] + CMP + H(+); Xref=Rhea:RHEA:65280, Rhea:RHEA-COMP:16760,
CC Rhea:RHEA-COMP:16761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:156395, ChEBI:CHEBI:156397;
CC Evidence={ECO:0000250|UniProtKB:Q8NDV1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65281;
CC Evidence={ECO:0000250|UniProtKB:Q8NDV1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-alpha-D-GalNAc]-L-
CC Thr-[protein] + CMP-N-acetyl-beta-neuraminate = 3-O-{alpha-Neu5Ac-
CC (2->3)-beta-D-Gal-(1->3)-[alpha-Neu5Ac-(2->6)]-alpha-D-GalNAc}-L-Thr-
CC [protein] + CMP + H(+); Xref=Rhea:RHEA:65284, Rhea:RHEA-COMP:16762,
CC Rhea:RHEA-COMP:16763, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:156396, ChEBI:CHEBI:156398;
CC Evidence={ECO:0000250|UniProtKB:Q8NDV1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65285;
CC Evidence={ECO:0000250|UniProtKB:Q8NDV1};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:8631773}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:8631773}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In adults it is highly expressed in spleen,
CC followed by kidney and lesser in lung. Not found in liver and skeletal
CC muscle. In newborns it is abundantly expressed in brain and kidney.
CC {ECO:0000269|PubMed:8631773}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; L29554; AAC42086.1; -; mRNA.
DR RefSeq; NP_061996.1; NM_019123.1.
DR AlphaFoldDB; Q64686; -.
DR STRING; 10116.ENSRNOP00000068331; -.
DR BindingDB; Q64686; -.
DR ChEMBL; CHEMBL2198; -.
DR SwissLipids; SLP:000001429; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q64686; 2 sites.
DR PaxDb; Q64686; -.
DR GeneID; 29758; -.
DR KEGG; rno:29758; -.
DR CTD; 256435; -.
DR RGD; 3677; St6galnac3.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q64686; -.
DR OrthoDB; 817470at2759; -.
DR PhylomeDB; Q64686; -.
DR Reactome; R-RNO-4085001; Sialic acid metabolism.
DR Reactome; R-RNO-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q64686; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047290; F:(alpha-N-acetylneuraminyl-2,3-beta-galactosyl-1,3)-N-acetyl-galactosaminide 6-alpha-sialyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0001665; F:alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase activity; IBA:GO_Central.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:RGD.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IBA:GO_Central.
DR GO; GO:0009100; P:glycoprotein metabolic process; ISO:RGD.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; ISO:RGD.
DR GO; GO:0006677; P:glycosylceramide metabolic process; ISO:RGD.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IDA:RGD.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR Pfam; PF00777; Glyco_transf_29; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Sialic acid; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..305
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 3"
FT /id="PRO_0000149277"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..305
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 80..229
FT /evidence="ECO:0000250"
SQ SEQUENCE 305 AA; 35150 MW; 9077F6547D359AE9 CRC64;
MACILKRKPA LAVSFIALCI LLLAMRLAND VTFPLLLNCF GQPKTKWIPL SYTLRQPLQT
HYGYINVRTQ EPLQLNCNHC AVVSNSGQMV GQKVGEEIDR ASCIWRMNNA PTKGFEEDVG
YMTMVRVVSH TSVPLLLKNP DYFFKEASTT IYVIWGPFRN MRKDGNGIVY NMLKKTVDAY
PDAQIYVTTE QRMTYCDGVF KDETGKDRVQ SGSYLSTGWF TFILAMDACY SIHVYGMINE
TYCTTEGYRK VPYHYYEQGK DECNEYLLHE HAPYGGHRFI TEKKVFAKWA KKHRIVFTHP
NWTVS
