SIA8A_MOUSE
ID SIA8A_MOUSE Reviewed; 355 AA.
AC Q64687; Q8K1C1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase;
DE EC=2.4.99.8 {ECO:0000269|PubMed:8910600};
DE AltName: Full=Alpha-2,8-sialyltransferase 8A;
DE AltName: Full=Ganglioside GD3 synthase;
DE AltName: Full=Ganglioside GT3 synthase;
DE AltName: Full=Sialyltransferase 8A;
DE Short=SIAT8-A;
DE AltName: Full=Sialyltransferase St8Sia I;
DE Short=ST8SiaI;
GN Name=St8sia1; Synonyms=Siat8, Siat8a;
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, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Brain;
RX PubMed=8910600; DOI=10.1074/jbc.271.46.29366;
RA Kono M., Yoshida Y., Kojima N., Tsuji S.;
RT "Molecular cloning and expression of a fifth type of alpha2,8-
RT sialyltransferase (ST8Sia V). Its substrate specificity is similar to that
RT of SAT-V/III, which synthesize GD1c, GT1a, GQ1b and GT3.";
RL J. Biol. Chem. 271:29366-29371(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP IDENTIFICATION.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the addition of sialic acid in alpha 2,8-linkage to
CC the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3;
CC gangliosides are a subfamily of complex glycosphinglolipds that contain
CC one or more residues of sialic acid (PubMed:8910600). Can catalyze the
CC addition of a second alpha-2,8- sialic acid to GD3 to form GT3
CC (PubMed:8910600). Can use GM1b, GD1a and GT1b as acceptor substrates to
CC synthesize GD1c, GT1a and GQ1b respectively (PubMed:8910600).
CC {ECO:0000269|PubMed:8910600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl
CC derivative + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-
CC neuraminyl-(2->8)-N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl
CC derivative + CMP + H(+); Xref=Rhea:RHEA:19313, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:140308,
CC ChEBI:CHEBI:140309; EC=2.4.99.8;
CC Evidence={ECO:0000269|PubMed:8910600};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM3 (d18:1(4E)) =
CC CMP + ganglioside GD3 (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41760,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60065,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78436;
CC Evidence={ECO:0000269|PubMed:8910600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41761;
CC Evidence={ECO:0000305|PubMed:8910600};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD3 (d18:1(4E)) =
CC CMP + ganglioside GT3 (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41764,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78436, ChEBI:CHEBI:78438;
CC Evidence={ECO:0000269|PubMed:8910600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41765;
CC Evidence={ECO:0000305|PubMed:8910600};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GD1a (d18:1(4E)) =
CC CMP + ganglioside GT1a (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41768,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78445, ChEBI:CHEBI:78447;
CC Evidence={ECO:0000269|PubMed:8910600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41769;
CC Evidence={ECO:0000305|PubMed:8910600};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GT1b (d18:1(4E)) =
CC CMP + ganglioside GQ1b (d18:1(4E)) + H(+); Xref=Rhea:RHEA:41772,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78452, ChEBI:CHEBI:78455;
CC Evidence={ECO:0000269|PubMed:8910600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41773;
CC Evidence={ECO:0000305|PubMed:8910600};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP-N-acetyl-beta-neuraminate + ganglioside GM1b (d18:1(4E)) =
CC CMP + ganglioside GD1c (d18:1(4E)) + H(+); Xref=Rhea:RHEA:47576,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC ChEBI:CHEBI:78568, ChEBI:CHEBI:87787;
CC Evidence={ECO:0000269|PubMed:8910600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47577;
CC Evidence={ECO:0000305|PubMed:8910600};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.03 mM for ganglioside GM3 {ECO:0000269|PubMed:8910600};
CC KM=5 mM for ganglioside GD3 {ECO:0000269|PubMed:8910600};
CC KM=5 mM for ganglioside GD1a {ECO:0000269|PubMed:8910600};
CC KM=2 mM for ganglioside GT1b {ECO:0000269|PubMed:8910600};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia I;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_656";
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DR EMBL; X84235; CAA59014.1; -; mRNA.
DR EMBL; CH466572; EDL10653.1; -; Genomic_DNA.
DR EMBL; BC024821; AAH24821.1; -; mRNA.
DR CCDS; CCDS20689.1; -.
DR RefSeq; NP_035504.2; NM_011374.2.
DR AlphaFoldDB; Q64687; -.
DR SMR; Q64687; -.
DR STRING; 10090.ENSMUSP00000032421; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyConnect; 2125; 1 N-Linked glycan (1 site).
DR GlyGen; Q64687; 4 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q64687; -.
DR MaxQB; Q64687; -.
DR PaxDb; Q64687; -.
DR PRIDE; Q64687; -.
DR ProteomicsDB; 257235; -.
DR Antibodypedia; 12441; 70 antibodies from 20 providers.
DR DNASU; 20449; -.
DR Ensembl; ENSMUST00000032421; ENSMUSP00000032421; ENSMUSG00000030283.
DR GeneID; 20449; -.
DR KEGG; mmu:20449; -.
DR UCSC; uc009epv.1; mouse.
DR CTD; 6489; -.
DR MGI; MGI:106011; St8sia1.
DR VEuPathDB; HostDB:ENSMUSG00000030283; -.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT01030000234535; -.
DR HOGENOM; CLU_048583_1_0_1; -.
DR InParanoid; Q64687; -.
DR OMA; NSPMGKN; -.
DR OrthoDB; 825014at2759; -.
DR PhylomeDB; Q64687; -.
DR TreeFam; TF323961; -.
DR BRENDA; 2.4.99.8; 3474.
DR Reactome; R-MMU-4085001; Sialic acid metabolism.
DR UniPathway; UPA00222; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 20449; 0 hits in 74 CRISPR screens.
DR ChiTaRS; St8sia1; mouse.
DR PRO; PR:Q64687; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q64687; protein.
DR Bgee; ENSMUSG00000030283; Expressed in urogenital fold and 146 other tissues.
DR ExpressionAtlas; Q64687; baseline and differential.
DR Genevisible; Q64687; MM.
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:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:MGI.
DR GO; GO:0006486; P:protein glycosylation; ISO:MGI.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
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 biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Signal-anchor; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..355
FT /note="Alpha-N-acetylneuraminide alpha-2,8-
FT sialyltransferase"
FT /id="PRO_0000149283"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..47
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..355
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 321
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 187..189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 273..275
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 137..286
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 151..346
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CONFLICT 50
FT /note="L -> P (in Ref. 1; CAA59014)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="R -> S (in Ref. 1; CAA59014)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="F -> S (in Ref. 1; CAA59014)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="S -> T (in Ref. 1; CAA59014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 40324 MW; 220BD56BBEE6E6C6 CRC64;
MSPCGRALHT SRGAMAMLAR KFPRTRLPVG ASALCVVVLC WLYIFPVYRL PNEKEIVQGV
LAQRTAWRTN QTSASLFRRQ MEDCCDPAHL FAMTKMNSPM GKSLWYDGEL LYSFTIDNST
YSLFPQATPF QLPLKKCAVV GNGGILKMSG CGRQIDEANF VMRCNLPPLS SEYTRDVGSK
TQLVTANPSI IRQRFENLLW SRKKFVDNMK IYNHSYIYMP AFSMKTGTEP SLRVYYTLKD
VGANQTVLFA NPNFLRNIGK FWKSRGIHAK RLSTGLFLVS AALGLCEEVS IYGFWPFSVN
MQGDPISHHY YDNVLPFSGY HAMPEEFLQL WYLHKIGALR MQLDPCEEPS PQPTS
