SIA8A_XENTR
ID SIA8A_XENTR Reviewed; 345 AA.
AC Q6DNG6;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase {ECO:0000250|UniProtKB:Q92185};
DE EC=2.4.99.8 {ECO:0000250|UniProtKB:Q6ZXA0};
DE AltName: Full=Alpha-2,8-sialyltransferase 8A;
DE AltName: Full=Ganglioside GD3 synthase {ECO:0000250|UniProtKB:Q6ZXA0};
DE AltName: Full=Sialyltransferase 8A;
DE Short=SIAT8-A;
DE AltName: Full=Sialyltransferase St8Sia I;
DE Short=ST8SiaI;
GN Name=st8sia1; Synonyms=st8siaI {ECO:0000312|EMBL:AAI70804.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAT67042.2}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17333390; DOI=10.1007/s11010-006-9406-1;
RA Rimoldi S., Papis E., Bernardini G., Prati M., Gornati R.;
RT "Molecular cloning and expression of alpha2,8-sialyltransferase (ST8Sia I,
RT GD3 Synthase) in Xenopus.";
RL Mol. Cell. Biochem. 301:143-153(2007).
RN [2] {ECO:0000312|EMBL:AAI70804.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Glycosphingolipids
CC are required for convergence extension movements during early
CC development (By similarity). Can catalyze the addition of a second
CC alpha-2,8- sialic acid to GD3 to form GT3 (By similarity). Can use
CC GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and
CC GQ1b respectively (By similarity). {ECO:0000250|UniProtKB:Q6ZXA0,
CC ECO:0000250|UniProtKB:Q92185}.
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:0000250|UniProtKB:Q6ZXA0};
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:0000250|UniProtKB:Q6ZXA0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41761;
CC Evidence={ECO:0000250|UniProtKB:Q6ZXA0};
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:0000250|UniProtKB:Q92185};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41765;
CC Evidence={ECO:0000250|UniProtKB:Q92185};
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:0000250|UniProtKB:Q92185};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41769;
CC Evidence={ECO:0000250|UniProtKB:Q92185};
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:0000250|UniProtKB:Q92185};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41773;
CC Evidence={ECO:0000250|UniProtKB:Q92185};
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:0000250|UniProtKB:Q92185};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47577;
CC Evidence={ECO:0000250|UniProtKB:Q92185};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q6ZXA0}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q6ZXA0}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q6ZXA0}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000255}.
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DR EMBL; AY652775; AAT67042.2; -; mRNA.
DR EMBL; BC170804; AAI70804.1; -; mRNA.
DR EMBL; BC170806; AAI70806.1; -; mRNA.
DR RefSeq; NP_001003659.1; NM_001003659.1.
DR AlphaFoldDB; Q6DNG6; -.
DR SMR; Q6DNG6; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GeneID; 444887; -.
DR KEGG; xtr:444887; -.
DR CTD; 6489; -.
DR Xenbase; XB-GENE-5824739; st8sia1.
DR InParanoid; Q6DNG6; -.
DR BRENDA; 2.4.99.8; 8483.
DR Reactome; R-XTR-4085001; Sialic acid metabolism.
DR UniPathway; UPA00222; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
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:0001574; P:ganglioside biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
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:0006486; P:protein glycosylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Signal-anchor; Sphingolipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..345
FT /note="Alpha-N-acetylneuraminide alpha-2,8-
FT sialyltransferase"
FT /id="PRO_0000376860"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..345
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 310
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 176..178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 262..264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 126..275
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 140..335
FT /evidence="ECO:0000250|UniProtKB:O43173"
SQ SEQUENCE 345 AA; 39831 MW; 222B64EA41A2C62F CRC64;
MKLQGSRMWL CPRTRLPVGA SALGFLILCW LYVFPGYRLP GHKEMVREVL RFGPGWRKNR
TEMDSFRKLL QDCCDPPHLF SLTKVNTPLG ENLWFDGEFF HSLTIDNSTR SLFPQDTPFK
LPLKRCSVVG NGGILKNSRC GEQIDEADFV MRCNLPPLSR EYTEDVGTRT QLVTVNPSII
DKRYQNLLWS RKSFVENLRV YQQSYVYMPA FSTKRGTDPS LRVYYTLADF GTNQTVLFAN
PNFLRNVGKF WKSRGIHSKR LSTGLFMVSA ALSLCEEVTI YGFWPFQMDL GGRYISHHYY
DNTLPLSGVH AMPEEFLQLW LLHKSGVLQM QLDQCKKDVS SQKPH
