SIA8A_XENLA
ID SIA8A_XENLA Reviewed; 359 AA.
AC Q6ZXA0; A0T095; Q6WRU1; Q6WRU2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase {ECO:0000250|UniProtKB:Q92185};
DE EC=2.4.99.8 {ECO:0000269|PubMed:17333390, ECO:0000269|PubMed:18095347};
DE AltName: Full=Alpha-2,8-sialyltransferase 8A {ECO:0000303|PubMed:15843597};
DE AltName: Full=Ganglioside GD3 synthase {ECO:0000303|PubMed:18095347};
DE Short=XlGD3 synthase;
DE AltName: Full=Sialyltransferase 8A;
DE Short=SIAT8-A;
DE AltName: Full=Sialyltransferase St8Sia I;
DE Short=ST8SiaI;
GN Name=st8sia1; Synonyms=siat8a {ECO:0000312|EMBL:CAG28695.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAG28695.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] {ECO:0000305, ECO:0000312|EMBL:AAQ16163.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 19-359 (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [3] {ECO:0000305, ECO:0000312|EMBL:ABK58605.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, PATHWAY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18095347; DOI=10.1002/dvdy.21406;
RA Luque M.E., Crespo P.M., Monaco M.E., Aybar M.J., Daniotti J.L.,
RA Sanchez S.S.;
RT "Cloning and functional characterization of two key enzymes of
RT glycosphingolipid biosynthesis in the amphibian Xenopus laevis.";
RL Dev. Dyn. 237:112-123(2008).
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:17333390, PubMed:18095347).
CC Glycosphingolipids are required for convergence extension movements
CC during early development (PubMed:18095347). Can catalyze the addition
CC of a second alpha-2,8- sialic acid to GD3 to form GT3 (By similarity).
CC Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c,
CC GT1a and GQ1b respectively (By similarity).
CC {ECO:0000250|UniProtKB:Q92185, ECO:0000269|PubMed:17333390,
CC ECO:0000269|PubMed:18095347}.
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:17333390, ECO:0000269|PubMed:18095347};
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:17333390, ECO:0000269|PubMed:18095347};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41761;
CC Evidence={ECO:0000305|PubMed:17333390};
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.
CC {ECO:0000269|PubMed:18095347, ECO:0000305}.
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:18095347}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:17333390, ECO:0000269|PubMed:18095347}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:17333390,
CC ECO:0000269|PubMed:18095347}. Note=PubMed:18095347 report localization
CC in the endoplasmic reticulum. {ECO:0000269|PubMed:17333390,
CC ECO:0000269|PubMed:18095347}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:15843597, ECO:0000269|PubMed:17333390};
CC Synonyms=ST8Sia I_long {ECO:0000269|PubMed:17333390};
CC IsoId=Q6ZXA0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:17333390}; Synonyms=ST8Sia I_short
CC {ECO:0000269|PubMed:17333390};
CC IsoId=Q6ZXA0-2; Sequence=VSP_053115;
CC Name=3 {ECO:0000269|PubMed:18095347};
CC IsoId=Q6ZXA0-3; Sequence=VSP_053116;
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal blastopore lip and in the
CC presumptive neuroectoderm in stage 11 embryos. During gastrulation,
CC strongly expressed in the involuting mesoderm. At stages 13 and 16,
CC expressed in the neural plate and neural fold, paraxial mesoderm and
CC notochord. At stages 19 and 22 (neural tube and early tailbud),
CC strongly expressed in the neural tube and notochord. At the tadpole
CC stage, expressed in the head region, branchial arches and otic and
CC optic primordia. Also localized in the notochord and weakly expressed
CC in the somites. In adults, expressed in the brain and ovary. Isoform 2
CC (short) is expressed at a low level in the adult testis and muscle, and
CC at a high level in the skin. Isoform 1 (long) is expressed at a high
CC level in the adult lung and kidney. Both isoforms 1 and 2 are expressed
CC in the gut and liver. {ECO:0000269|PubMed:17333390,
CC ECO:0000269|PubMed:18095347}.
CC -!- DEVELOPMENTAL STAGE: Expressed zygotically from the beginning of
CC gastrulation, with expression increasing at stage 12. Expression then
CC persists until stage 35 and declines afterwards.
CC {ECO:0000269|PubMed:17333390, ECO:0000269|PubMed:18095347}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000255}.
CC -!- CAUTION: PubMed:18095347 report an endoplasmic reticulum localization
CC and a lack of enzymatic activity, which could be a result of impaired
CC N-glycosylation. {ECO:0000305}.
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DR EMBL; AJ704562; CAG28695.1; -; mRNA.
DR EMBL; AY272056; AAQ16162.1; -; mRNA.
DR EMBL; AY272057; AAQ16163.1; -; mRNA.
DR EMBL; EF067919; ABK58605.1; -; mRNA.
DR RefSeq; NP_001083088.1; NM_001089619.1. [Q6ZXA0-1]
DR AlphaFoldDB; Q6ZXA0; -.
DR SMR; Q6ZXA0; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GeneID; 398735; -.
DR KEGG; xla:398735; -.
DR CTD; 398735; -.
DR Xenbase; XB-GENE-5824746; st8sia1.L.
DR OrthoDB; 825014at2759; -.
DR BRENDA; 2.4.99.8; 6725.
DR UniPathway; UPA00222; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 398735; Expressed in brain and 18 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA: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; IDA:UniProtKB.
DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IDA:UniProtKB.
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 InterPro; IPR012163; Sialyl_trans.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR PIRSF; PIRSF005557; Sialyl_trans; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Alpha-N-acetylneuraminide alpha-2,8-
FT sialyltransferase"
FT /id="PRO_0000376859"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..359
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 324
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 190..192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT BINDING 276..278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..289
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT DISULFID 154..349
FT /evidence="ECO:0000250|UniProtKB:O43173"
FT VAR_SEQ 1..128
FT /note="MWGRWRGAGGRRGVAQPVIPQMKLLGGRVPLGASALGLLIVCWFYIFPGGER
FT LPGHKEMIRQVLQFGPRWGRNRSSGDSFRKLLQDCCDPPRLFSMTKANTALGENLWYDG
FT EFFQSLTIDNTTRSLFP -> MERGGRSERGRTAGDSADEAVGGAGAARCQCPGASHCL
FT LVLHLPRGGATPGTQRNDPAGSTVRPEMGEKPEQRRLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17333390"
FT /id="VSP_053115"
FT VAR_SEQ 167..197
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18095347"
FT /id="VSP_053116"
FT CONFLICT 58
FT /note="E -> Q (in Ref. 2; AAQ16163)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="T -> S (in Ref. 2; AAQ16163)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="T -> S (in Ref. 2; AAQ16162)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="F -> L (in Ref. 2; AAQ16163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40811 MW; 087442A04C092D2D CRC64;
MWGRWRGAGG RRGVAQPVIP QMKLLGGRVP LGASALGLLI VCWFYIFPGG ERLPGHKEMI
RQVLQFGPRW GRNRSSGDSF RKLLQDCCDP PRLFSMTKAN TALGENLWYD GEFFQSLTID
NTTRSLFPQD TPIKLPLKRC SVVGNGGILK NSRCGEQIDE ADFVMRCNLP PLSREYTDDV
GTKTQLVTVN PSIIDKRFQN LLWSRKSFVE SVSVYKQSYV YMPAFSTKRG TDPSLRVYYT
LEDFGTNQTV LFANPNFLRN VGKFWKSKGV HSKRLSTGLF MVSAALSLCE EVTIYGFWPF
QMDLGGRHIS HHYYDNMLPL SGVHAMPEEF LQLWHLHKSG VLQMQLDQCK KDVSSKKPH
