SIA7C_MOUSE
ID SIA7C_MOUSE Reviewed; 305 AA.
AC Q9WUV2; Q9JHP5;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 3;
DE EC=2.4.99.7 {ECO:0000269|PubMed:10207017};
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase III;
DE AltName: Full=ST6GalNAc III {ECO:0000303|PubMed:10207017, ECO:0000303|PubMed:10601645};
DE Short=ST6GalNAcIII;
DE AltName: Full=STY;
DE AltName: Full=Sialyltransferase 7C;
DE Short=SIAT7-C;
GN Name=St6galnac3; Synonyms=Siat7c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=10207017; DOI=10.1074/jbc.274.17.11958;
RA Lee Y.-C., Kaufman M., Kitazume-Kawaguchi S., Kono M., Takashima S.,
RA Kurosawa N., Liu H., Pircher H., Tsuji S.;
RT "Molecular cloning and functional expression of two members of mouse NeuAc-
RT alpha-2,3Gal-beta-1,3GalNAc GalNAc-alpha2,6-sialyltransferase family,
RT ST6GalNAc III and IV.";
RL J. Biol. Chem. 274:11958-11967(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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=10601645; DOI=10.1016/s0014-5793(99)01605-1;
RA Ikehara Y., Shimizu N., Kono M., Nishihara S., Nakanishi H., Kitamura T.,
RA Narimatsu H., Tsuji S., Tatematsu M.;
RT "A novel glycosyltransferase with a polyglutamine repeat; a new candidate
RT for GD1alpha synthase (ST6GalNAc V).";
RL FEBS Lett. 463:92-96(1999).
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:10207017, PubMed:10601645). GD1alpha is a critical
CC molecule in the communication and interaction between neuronal cells
CC and their supportive cells, particularly in brain tissues, and
CC functions as an adhesion molecule in the process of metastasis (By
CC similarity). Sialylation of glycoproteins or glycosphingolipids is very
CC important in tumor development, neuronal development, nerve repair,
CC immunological processes and regulation of hormone sensitivity (By
CC similarity). {ECO:0000250|UniProtKB:Q8NDV1,
CC ECO:0000250|UniProtKB:Q9QYJ1, ECO:0000269|PubMed:10207017,
CC ECO:0000269|PubMed:10601645}.
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:10207017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53897;
CC Evidence={ECO:0000305|PubMed:10207017};
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:0000269|PubMed:10207017, ECO:0000305|PubMed:10601645};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41969;
CC Evidence={ECO:0000305|PubMed:10207017, ECO:0000305|PubMed:10601645};
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:0000269|PubMed:10207017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65281;
CC Evidence={ECO:0000305|PubMed:10207017};
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:0000269|PubMed:10207017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65285;
CC Evidence={ECO:0000305|PubMed:10207017};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:10207017, ECO:0000305|PubMed:10601645}.
CC -!- PATHWAY: Glycolipid biosynthesis. {ECO:0000305|PubMed:10207017,
CC ECO:0000305|PubMed:10601645}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In adult tissues, high expression in brain, lung
CC and heart and to a lesser extent in kidney, mammary gland, spleen,
CC testis and thymus. {ECO:0000269|PubMed:10207017}.
CC -!- DEVELOPMENTAL STAGE: In brain, expression reaches maximum levels at day
CC 12 of the embryonic stage. Keeps almost similar levels during mouse
CC development. {ECO:0000269|PubMed:10207017}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST6GalNAc
CC III;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_652";
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DR EMBL; Y11342; CAA72181.2; -; mRNA.
DR EMBL; Y11343; CAB95031.1; -; Genomic_DNA.
DR EMBL; Y11344; CAB95031.1; JOINED; Genomic_DNA.
DR EMBL; Y11345; CAB95031.1; JOINED; Genomic_DNA.
DR EMBL; Y11346; CAB95031.1; JOINED; Genomic_DNA.
DR EMBL; BC058387; AAH58387.1; -; mRNA.
DR CCDS; CCDS38677.1; -.
DR RefSeq; NP_035502.1; NM_011372.2.
DR AlphaFoldDB; Q9WUV2; -.
DR SMR; Q9WUV2; -.
DR STRING; 10090.ENSMUSP00000068598; -.
DR SwissLipids; SLP:000000783; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q9WUV2; 2 sites.
DR PhosphoSitePlus; Q9WUV2; -.
DR MaxQB; Q9WUV2; -.
DR PaxDb; Q9WUV2; -.
DR PRIDE; Q9WUV2; -.
DR ProteomicsDB; 257234; -.
DR Antibodypedia; 33477; 53 antibodies from 15 providers.
DR DNASU; 20447; -.
DR Ensembl; ENSMUST00000200397; ENSMUSP00000143747; ENSMUSG00000052544.
DR GeneID; 20447; -.
DR KEGG; mmu:20447; -.
DR UCSC; uc008rtw.1; mouse.
DR CTD; 256435; -.
DR MGI; MGI:1341828; St6galnac3.
DR VEuPathDB; HostDB:ENSMUSG00000052544; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000159735; -.
DR HOGENOM; CLU_061099_2_2_1; -.
DR InParanoid; Q9WUV2; -.
DR OMA; PGAKWIP; -.
DR OrthoDB; 817470at2759; -.
DR PhylomeDB; Q9WUV2; -.
DR TreeFam; TF352818; -.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20447; 2 hits in 74 CRISPR screens.
DR ChiTaRS; St6galnac3; mouse.
DR PRO; PR:Q9WUV2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9WUV2; protein.
DR Bgee; ENSMUSG00000052544; Expressed in lumbar subsegment of spinal cord and 192 other tissues.
DR ExpressionAtlas; Q9WUV2; baseline and differential.
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:0005654; C:nucleoplasm; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IBA:GO_Central.
DR GO; GO:0009100; P:glycoprotein metabolic process; ISO:MGI.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; ISO:MGI.
DR GO; GO:0006677; P:glycosylceramide metabolic process; ISO:MGI.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; ISO:MGI.
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_0000149276"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..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; 35414 MW; 63C7498615BF6A3F CRC64;
MACILKRKPV LVVSFIALCI LLLAMRLVND ATFPLLLNCF GQPKTKWIPL PYTFRQPLRT
HYGYINVRTQ EPLQLNCNHC AIVSNSGQMV GQKVGEEIDH ASCIWRMNNA PTKGFEEDVG
YMTMVRVVSH TSVPLLLKNP DYFFKEASRT IYVIWGPFRN MRKDGNGIVY NMLKKTVDAY
PDAQIYVTTE QQMTHCDRVF KDETGKDRVQ SGSYLSTGWF TFILAMDACY SIHVYGMINE
TYCKTEGYRK VPYHYYEQGK DECNEYLLHE HAPYGGHRFI TEKKVFAKWA KKHRIVFTHP
NWTLS
