SIA7D_MOUSE
ID SIA7D_MOUSE Reviewed; 360 AA.
AC Q9R2B6; O88725; Q9JHP0; Q9QUP9; Q9R2B5;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-acetyl-galactosaminide alpha-2,6-sialyltransferase;
DE EC=2.4.99.7 {ECO:0000269|PubMed:10207017, ECO:0000269|PubMed:10601645};
DE AltName: Full=NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc-alpha-2,6-sialyltransferase;
DE AltName: Full=ST6GalNAc IV {ECO:0000303|PubMed:10207017, ECO:0000303|PubMed:10601645};
DE Short=ST6GalNAcIV;
DE AltName: Full=Sialyltransferase 7D;
DE Short=SIAT7-D;
GN Name=St6galnac4; Synonyms=Siat7d;
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, ALTERNATIVE SPLICING, 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 [GENOMIC DNA] OF 299-360.
RC STRAIN=C57BL/6J;
RX PubMed=10731711; DOI=10.1093/oxfordjournals.jbchem.a022621;
RA Takashima S., Kurosawa N., Tachida Y., Inoue M., Tsuji S.;
RT "Comparative analysis of the genomic structures and promoter activities of
RT mouse Siaa2,3Galb1,3GalNAc GalNAca2,6-sialyltransferase genes (ST6GalNAc
RT III and IV): characterization of their Sp1 binding.";
RL J. Biochem. 127:399-409(2000).
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 (PubMed:10207017, PubMed:10601645). Prefers O-glycans to
CC glycoproteins or glycolipids (PubMed:10207017).
CC {ECO:0000269|PubMed:10207017, 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 ECO:0000269|PubMed:10601645};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53897;
CC Evidence={ECO:0000305|PubMed:10207017, ECO:0000305|PubMed:10601645};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + N-acetyl-alpha-neuraminosyl-
CC (2->3)-beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine = CMP + H(+)
CC + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-[N-
CC acetyl-alpha-neuraminosyl-(2->6)]-N-acetyl-D-galactosamine;
CC Xref=Rhea:RHEA:65288, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:156406, ChEBI:CHEBI:156407;
CC Evidence={ECO:0000269|PubMed:10207017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65289;
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:0000269|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=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:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1; Synonyms=Long 2;
CC IsoId=Q9R2B6-1; Sequence=Displayed;
CC Name=2; Synonyms=Long 1;
CC IsoId=Q9R2B6-2; Sequence=VSP_001788;
CC Name=3; Synonyms=Short;
CC IsoId=Q9R2B6-3; Sequence=VSP_001787;
CC -!- TISSUE SPECIFICITY: High expression in brain and colon and to a lesser
CC extent in lung, heart, kidney, spleen and thymus.
CC {ECO:0000269|PubMed:10207017}.
CC -!- DEVELOPMENTAL STAGE: Developmentally regulated.
CC {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 IV;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_653";
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DR EMBL; Y15780; CAB43514.1; -; mRNA.
DR EMBL; Y15780; CAB43515.1; -; mRNA.
DR EMBL; Y15779; CAB43507.1; -; mRNA.
DR EMBL; Y15779; CAB43508.1; -; mRNA.
DR EMBL; AJ007310; CAA07446.1; -; mRNA.
DR EMBL; Y19057; CAB93948.1; -; Genomic_DNA.
DR CCDS; CCDS15921.1; -. [Q9R2B6-3]
DR RefSeq; NP_001263354.1; NM_001276425.1.
DR RefSeq; NP_035503.1; NM_011373.3.
DR AlphaFoldDB; Q9R2B6; -.
DR SMR; Q9R2B6; -.
DR STRING; 10090.ENSMUSP00000099882; -.
DR SwissLipids; SLP:000000785; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q9R2B6; 1 site.
DR iPTMnet; Q9R2B6; -.
DR PhosphoSitePlus; Q9R2B6; -.
DR PaxDb; Q9R2B6; -.
DR PRIDE; Q9R2B6; -.
DR ProteomicsDB; 257170; -. [Q9R2B6-1]
DR ProteomicsDB; 257171; -. [Q9R2B6-2]
DR ProteomicsDB; 257172; -. [Q9R2B6-3]
DR DNASU; 20448; -.
DR GeneID; 20448; -.
DR KEGG; mmu:20448; -.
DR CTD; 27090; -.
DR MGI; MGI:1341894; St6galnac4.
DR eggNOG; KOG2692; Eukaryota.
DR InParanoid; Q9R2B6; -.
DR OrthoDB; 817470at2759; -.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20448; 4 hits in 75 CRISPR screens.
DR ChiTaRS; St6galnac4; mouse.
DR PRO; PR:Q9R2B6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9R2B6; protein.
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:0001574; P:ganglioside biosynthetic process; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lipid metabolism; Membrane; Reference proteome;
KW Sialic acid; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..360
FT /note="Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3-N-
FT acetyl-galactosaminide alpha-2,6-sialyltransferase"
FT /id="PRO_0000149279"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..94
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..360
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 134..283
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_001787"
FT VAR_SEQ 1..28
FT /note="MEHVVTCWRLKLLSWPVFLIWICLSLAS -> MSSEQRILSPQRTPIRSF
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001788"
SQ SEQUENCE 360 AA; 40773 MW; 7CF4101B8FDA369A CRC64;
MEHVVTCWRL KLLSWPVFLI WICLSLASVS LISWDQLPAF LIPSTGDSSL QTAKSRDSMK
APGRLLLLTL CILTFSAVCV FLCCWACLPL CLATCLDRHL PAAPRSTVPG PLHFSGYSSV
PDGKPLIREL CHSCAVVSNS GQMLGSGLGA QIDGAECVLR MNQAPTVGFE EDVGQRTTLR
VISHTSVPLL LRNYSHYFQH ARDTLYVVWG QGRHMDRVLG GRTYRTLLQL TRMYPGLQVY
TFTERMMAYC DQIFQDETGK NRRQSGSFLS TGWFTMIPAL ELCEEIVVYG MVSDSYCSEK
SPRSVPYHYF EKGRLDECQM YRLHEQAPRS AHRFITEKAV FSRWAKKRPI VFAHPSWRAK
