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Protein

Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase

Gene

st8sia1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the production of gangliosides GD3 and GT3 from GM3; gangliosides are a subfamily of complex glycosphingolipids that contain one or more residues of sialic acid. Glycosphingolipids are required for convergence extension movements during early development.2 Publications

Catalytic activityi

CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-R = CMP + alpha-N-acetylneuraminyl-(2->8)-alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-R.1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Pathwayi: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei168 – 1681SubstrateBy similarity
Active sitei324 – 3241Proton donor/acceptorBy similarity

GO - Molecular functioni

  • alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity Source: UniProtKB

GO - Biological processi

  • ganglioside biosynthetic process Source: UniProtKB
  • glycosphingolipid biosynthetic process Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
  • protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BRENDAi2.4.99.8. 6725.
UniPathwayiUPA00222.
UPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-N-acetylneuraminide alpha-2,8-sialyltransferaseBy similarity (EC:2.4.99.8)
Alternative name(s):
Alpha-2,8-sialyltransferase 8A1 Publication
Ganglioside GD3 synthase1 Publication
Short name:
XlGD3 synthase
Sialyltransferase 8A
Short name:
SIAT8-A
Sialyltransferase St8Sia I
Short name:
ST8SiaI
Gene namesi
Name:st8sia1
Synonyms:siat8aImported
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-5824746. st8sia1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2828CytoplasmicSequence analysisAdd
BLAST
Transmembranei29 – 4921Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini50 – 359310LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi membrane Source: UniProtKB
  • integral component of Golgi membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Alpha-N-acetylneuraminide alpha-2,8-sialyltransferasePRO_0000376859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence analysis
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence analysis
Disulfide bondi140 ↔ 289By similarity
Disulfide bondi154 ↔ 349By similarity
Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed in the dorsal blastopore lip and in the presumptive neuroectoderm in stage 11 embryos. During gastrulation, strongly expressed in the involuting mesoderm. At stages 13 and 16, expressed in the neural plate and neural fold, paraxial mesoderm and notochord. At stages 19 and 22 (neural tube and early tailbud), strongly expressed in the neural tube and notochord. At the tadpole stage, expressed in the head region, branchial arches and otic and optic primordia. Also localized in the notochord and weakly expressed in the somites. In adults, expressed in the brain and ovary. Isoform 2 (short) is expressed at a low level in the adult testis and muscle, and at a high level in the skin. Isoform 1 (long) is expressed at a high level in the adult lung and kidney. Both isoforms 1 and 2 are expressed in the gut and liver.2 Publications

Developmental stagei

Expressed zygotically from the beginning of gastrulation, with expression increasing at stage 12. Expression then persists until stage 35 and declines afterwards.2 Publications

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 1923Substrate bindingBy similarity
Regioni276 – 2783Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Sequence analysis

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK03371.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFiPIRSF005557. Sialyl_trans. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 12 Publications (identifier: Q6ZXA0-1) [UniParc]FASTAAdd to basket

Also known as: ST8Sia I_long1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWGRWRGAGG RRGVAQPVIP QMKLLGGRVP LGASALGLLI VCWFYIFPGG
60 70 80 90 100
ERLPGHKEMI RQVLQFGPRW GRNRSSGDSF RKLLQDCCDP PRLFSMTKAN
110 120 130 140 150
TALGENLWYD GEFFQSLTID NTTRSLFPQD TPIKLPLKRC SVVGNGGILK
160 170 180 190 200
NSRCGEQIDE ADFVMRCNLP PLSREYTDDV GTKTQLVTVN PSIIDKRFQN
210 220 230 240 250
LLWSRKSFVE SVSVYKQSYV YMPAFSTKRG TDPSLRVYYT LEDFGTNQTV
260 270 280 290 300
LFANPNFLRN VGKFWKSKGV HSKRLSTGLF MVSAALSLCE EVTIYGFWPF
310 320 330 340 350
QMDLGGRHIS HHYYDNMLPL SGVHAMPEEF LQLWHLHKSG VLQMQLDQCK

KDVSSKKPH
Length:359
Mass (Da):40,811
Last modified:July 5, 2004 - v1
Checksum:i087442A04C092D2D
GO
Isoform 21 Publication (identifier: Q6ZXA0-2) [UniParc]FASTAAdd to basket

Also known as: ST8Sia I_short1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: MWGRWRGAGG...IDNTTRSLFP → MERGGRSERG...GEKPEQRRLL

Show »
Length:307
Mass (Da):34,248
Checksum:i436A2AA7D7D0E71D
GO
Isoform 31 Publication (identifier: Q6ZXA0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     167-197: Missing.

Show »
Length:328
Mass (Da):37,355
Checksum:i64BE48A4856841F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581E → Q in AAQ16163 (PubMed:17333390).Curated
Sequence conflicti122 – 1221T → S in AAQ16163 (PubMed:17333390).Curated
Sequence conflicti246 – 2461T → S in AAQ16162 (PubMed:17333390).Curated
Sequence conflicti264 – 2641F → L in AAQ16163 (PubMed:17333390).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 128128MWGRW…RSLFP → MERGGRSERGRTAGDSADEA VGGAGAARCQCPGASHCLLV LHLPRGGATPGTQRNDPAGS TVRPEMGEKPEQRRLL in isoform 2. 1 PublicationVSP_053115Add
BLAST
Alternative sequencei167 – 19731Missing in isoform 3. 1 PublicationVSP_053116Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ704562 mRNA. Translation: CAG28695.1.
AY272056 mRNA. Translation: AAQ16162.1.
AY272057 mRNA. Translation: AAQ16163.1.
EF067919 mRNA. Translation: ABK58605.1.
RefSeqiNP_001083088.1. NM_001089619.1. [Q6ZXA0-1]
UniGeneiXl.29879.

Genome annotation databases

GeneIDi398735.
KEGGixla:398735.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ704562 mRNA. Translation: CAG28695.1.
AY272056 mRNA. Translation: AAQ16162.1.
AY272057 mRNA. Translation: AAQ16163.1.
EF067919 mRNA. Translation: ABK58605.1.
RefSeqiNP_001083088.1. NM_001089619.1. [Q6ZXA0-1]
UniGeneiXl.29879.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi398735.
KEGGixla:398735.

Organism-specific databases

CTDi6489.
XenbaseiXB-GENE-5824746. st8sia1.

Phylogenomic databases

KOiK03371.

Enzyme and pathway databases

UniPathwayiUPA00222.
UPA00378.
BRENDAi2.4.99.8. 6725.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFiPIRSF005557. Sialyl_trans. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach."
    Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.
    Glycobiology 15:805-817(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Molecular cloning and expression of alpha2,8-sialyltransferase (ST8Sia I, GD3 Synthase) in Xenopus."
    Rimoldi S., Papis E., Bernardini G., Prati M., Gornati R.
    Mol. Cell. Biochem. 301:143-153(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 19-359 (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "Cloning and functional characterization of two key enzymes of glycosphingolipid biosynthesis in the amphibian Xenopus laevis."
    Luque M.E., Crespo P.M., Monaco M.E., Aybar M.J., Daniotti J.L., Sanchez S.S.
    Dev. Dyn. 237:112-123(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiSIA8A_XENLA
AccessioniPrimary (citable) accession number: Q6ZXA0
Secondary accession number(s): A0T095, Q6WRU1, Q6WRU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

PubMed:18095347 report an endoplasmic reticulum localization and a lack of enzymatic activity, which could be a result of impaired N-glycosylation.Curated

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.