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   27-MAR-2024, entry version 168.
DE   RecName: Full=Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase {ECO:0000305};
DE            EC=2.4.3.8 {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 {ECO:0000312|MGI:MGI:106011}; 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 glycosphingolipds 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=2.4.3.8;
CC         Evidence={ECO:0000269|PubMed:8910600};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GM3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = a ganglioside GD3 (d18:1(4E)) + CMP + 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=a ganglioside GD3 (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = a ganglioside GT3 (d18:1(4E)) + CMP + 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=a ganglioside GD1a (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = a ganglioside GT1a (d18:1(4E)) + CMP + 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=a ganglioside GT1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = a ganglioside GQ1b (d18:1(4E)) + CMP + 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=a ganglioside GM1b (d18:1(4E)) + CMP-N-acetyl-beta-neuraminate
CC         = a ganglioside GD1c (d18:1(4E)) + CMP + 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ganglioside GD3 + CMP-N-acetyl-beta-neuraminate = a
CC         ganglioside GT3 + CMP + H(+); Xref=Rhea:RHEA:77295,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:79214, ChEBI:CHEBI:79216;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77296;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[alpha-N-acetylneuraminyl-(2->8)](n)-alpha-N-acetylneuraminyl-
CC         (2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-
CC         D-glucosyl-(1<->1)-ceramide + CMP-N-acetyl-beta-neuraminate = [alpha-
CC         N-acetylneuraminyl-(2->8)](n+1)-alpha-N-acetylneuraminyl-(2->8)-
CC         alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-
CC         glucosyl-(1<->1)-ceramide + CMP + H(+); Xref=Rhea:RHEA:77371,
CC         Rhea:RHEA-COMP:18881, Rhea:RHEA-COMP:18935, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:197322;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77372;
CC         Evidence={ECO:0000250|UniProtKB:Q92185};
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";
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; 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   GlyCosmos; Q64687; 4 sites, 1 glycan.
DR   GlyGen; Q64687; 4 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q64687; -.
DR   PhosphoSitePlus; Q64687; -.
DR   SwissPalm; Q64687; -.
DR   MaxQB; Q64687; -.
DR   PaxDb; 10090-ENSMUSP00000032421; -.
DR   ProteomicsDB; 257235; -.
DR   Antibodypedia; 12441; 83 antibodies from 20 providers.
DR   DNASU; 20449; -.
DR   Ensembl; ENSMUST00000032421.4; ENSMUSP00000032421.4; ENSMUSG00000030283.8.
DR   GeneID; 20449; -.
DR   KEGG; mmu:20449; -.
DR   UCSC; uc009epv.1; mouse.
DR   AGR; MGI:106011; -.
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; MAGLAWK; -.
DR   OrthoDB; 5348004at2759; -.
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; 1 hit in 79 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 150 other cell types or tissues.
DR   ExpressionAtlas; Q64687; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.1480.20; Glycosyl transferase family 29; 1.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   InterPro; IPR012163; Sialyl_trans.
DR   PANTHER; PTHR11987; ALPHA-2,8-SIALYLTRANSFERASE; 1.
DR   PANTHER; PTHR11987:SF3; ALPHA-N-ACETYLNEURAMINIDE ALPHA-2,8-SIALYLTRANSFERASE; 1.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   PIRSF; PIRSF005557; Sialyl_trans; 1.
DR   Genevisible; Q64687; MM.
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         142
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         165
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         273
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         274
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         275
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         295
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
FT                   /evidence="ECO:0000250|UniProtKB:O43173"
FT   BINDING         309
FT                   /ligand="CMP-N-acetyl-beta-neuraminate"
FT                   /ligand_id="ChEBI:CHEBI:57812"
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
//