SIA7F_BOVIN
ID SIA7F_BOVIN Reviewed; 332 AA.
AC Q08E15; Q704S2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 6;
DE EC=2.4.99.- {ECO:0000250|UniProtKB:Q969X2};
DE AltName: Full=GalNAc alpha-2,6-sialyltransferase VI;
DE AltName: Full=ST6GalNAc VI;
DE Short=ST6GalNAcVI;
DE AltName: Full=Sialyltransferase 7F;
DE Short=SIAT7-F;
GN Name=ST6GALNAC6; Synonyms=SIAT7F;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15843597; DOI=10.1093/glycob/cwi063;
RA Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.;
RT "The animal sialyltransferases and sialyltransferase-related genes: a
RT phylogenetic approach.";
RL Glycobiology 15:805-817(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or
CC NeuAc) from CMP-NeuAc onto glycoproteins and glycolipids, forming an
CC alpha-2,6-linkage. Produces branched type disialyl structures by
CC transfer of a sialyl group onto the GalNAc or GlcNAc residue inside
CC backbone core chains having a terminal sialic acid with an alpha-2,3-
CC linkage on Gal. ST6GalNAcVI prefers glycolipids to glycoproteins,
CC predominantly catalyzing the biosynthesis of ganglioside GD1alpha from
CC GM1b. Besides GMb1, MSGG and other glycolipids, it shows activity
CC towards sialyl Lc4Cer generating disialyl Lc4Cer, which can lead to the
CC synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-
CC associated antigen (By similarity). Also has activity toward GD1a and
CC GT1b, and can generate DSGG (disialylgalactosylgloboside) from MSGG
CC (monosialylgalactosylgloboside) (By similarity).
CC {ECO:0000250|UniProtKB:Q969X2, ECO:0000250|UniProtKB:Q9JM95}.
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:Q969X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41969;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + N-acetyl-alpha-neuraminosyl-
CC (2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-
CC enine = CMP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->3)-[N-acetyl-alpha-neuraminosyl-(2->6)]-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-N-acyl-sphing-4-enine; Xref=Rhea:RHEA:47884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:88073, ChEBI:CHEBI:88079;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47885;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
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:Q969X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56089;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1a (d18:1(4E)) =
CC CMP + ganglioside GT1aalpha (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41972,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78445, ChEBI:CHEBI:78571;
CC Evidence={ECO:0000250|UniProtKB:Q9JM95};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41973;
CC Evidence={ECO:0000250|UniProtKB:Q9JM95};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GT1b (d18:1(4E)) =
CC CMP + ganglioside GQ1b alpha (d18:1(4E)) + H(+);
CC Xref=Rhea:RHEA:41976, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78452, ChEBI:CHEBI:78572;
CC Evidence={ECO:0000250|UniProtKB:Q9JM95};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41977;
CC Evidence={ECO:0000250|UniProtKB:Q9JM95};
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:Q969X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65281;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
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:Q969X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65285;
CC Evidence={ECO:0000250|UniProtKB:Q969X2};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ620949; CAF06586.1; -; mRNA.
DR EMBL; BC123467; AAI23468.1; -; mRNA.
DR RefSeq; NP_001001151.2; NM_001001151.2.
DR RefSeq; XP_010808690.1; XM_010810388.2.
DR AlphaFoldDB; Q08E15; -.
DR STRING; 9913.ENSBTAP00000053714; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR PaxDb; Q08E15; -.
DR PRIDE; Q08E15; -.
DR GeneID; 407222; -.
DR KEGG; bta:407222; -.
DR CTD; 30815; -.
DR eggNOG; KOG2692; Eukaryota.
DR HOGENOM; CLU_061099_3_0_1; -.
DR InParanoid; Q08E15; -.
DR OrthoDB; 817470at2759; -.
DR TreeFam; TF323961; -.
DR Proteomes; UP000009136; 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: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:InterPro.
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 2: Evidence at transcript 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..332
FT /note="Alpha-N-acetylgalactosaminide alpha-2,6-
FT sialyltransferase 6"
FT /id="PRO_0000314794"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..332
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..255
FT /evidence="ECO:0000250"
FT CONFLICT 330
FT /note="S -> F (in Ref. 1; CAF06586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 38034 MW; 990B326431CD62D3 CRC64;
MACPRPLSQC DHTPLPGPPA GHWPLPLSRR RREMKSNKEQ RSAVFVILFA LITILILYSS
SSANEVFHYG SLRGRTRRPV NLRKWSITDG YIPILGNKTL PSRCGQCVIV TSSSHLLGTK
LGPEIERAEC TIRMNDAPTT GYSADVGNKT TFRVVAHSSV FHVLRRPQEF VNRTPETVFI
FWGPPNKMQK PQGSLVRVIQ RAGLVFPNME AYAISLSRMR QFDDLFRSET GKDREKSHSW
LSTGWFTMVI AVELCDHVHV YGMVPPDYCS LRPHLQRMPY HYYEPKGPDE CVTYIQNENS
RKGNHHRFIT EKRVFSSWAQ LYGITFSHPS WT
