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Protein

Type 2 lactosamine alpha-2,3-sialyltransferase

Gene

ST3GAL6

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Involved in the synthesis of sialyl-paragloboside, a precursor of sialyl-Lewis X determinant. Has a alpha-2,3-sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on glycoproteins and glycolipids. Has a restricted substrate specificity, it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide or asialo-GM1 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase

Protein family/group databases

CAZyiGT29 Glycosyltransferase Family 29

Names & Taxonomyi

Protein namesi
Recommended name:
Type 2 lactosamine alpha-2,3-sialyltransferase (EC:2.4.99.-)
Alternative name(s):
CMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VI
ST3Gal VI
Short name:
ST3GalVI
Sialyltransferase 10
Gene namesi
Name:ST3GAL6
Synonyms:SIAT10
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 4CytoplasmicSequence analysis4
Transmembranei5 – 25Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini26 – 331LumenalSequence analysisAdd BLAST306

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003315061 – 331Type 2 lactosamine alpha-2,3-sialyltransferaseAdd BLAST331

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi129N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi181N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi282N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi295N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi308N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi327N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ5RE85

Interactioni

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000015216

Structurei

3D structure databases

SMRiQ5RE85
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2692 Eukaryota
ENOG410XT8P LUCA
HOGENOMiHOG000000682
HOVERGENiHBG056676
InParanoidiQ5RE85
KOiK03792

Family and domain databases

Gene3Di3.90.1480.20, 1 hit
InterProiView protein in InterPro
IPR001675 Glyco_trans_29
IPR038578 GT29-like_sf
IPR012163 Sialyl_trans
PfamiView protein in Pfam
PF00777 Glyco_transf_29, 1 hit
PIRSFiPIRSF005557 Sialyl_trans, 1 hit

Sequencei

Sequence statusi: Complete.

Q5RE85-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRGYLVAIFL SAVFLYYVLH CILWGTNVYW AAPVEMKRRN KIQPCLSKPA
60 70 80 90 100
FASLLRFHQF HPFLCAADFR KIASLYGSDK FDLPYGMRTS AEYFRLALSK
110 120 130 140 150
LQSCDLFDEF DNIPCKKCVV VGNGGVLKNK TLGEKIDSYD VIIRMNNGPV
160 170 180 190 200
LGHEEEVGRR TTFRLFYPES VFSDPIHNDP NTTVILTAFK PHDLRWLLEL
210 220 230 240 250
LMGDKINTNG FWKKPALNLI YKPYQIRILD PFIIRTAAYE LLHFPKVFPK
260 270 280 290 300
NQKPKHPTTG IIAITLAFYI CHEVHLAGFK YNFSDLKSPL HYYGNATMSL
310 320 330
MNKNAYHNVT AEQLFLKDII EKNLVINLTQ D
Length:331
Mass (Da):38,186
Last modified:December 21, 2004 - v1
Checksum:iCC118B5D90652A79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857649 mRNA Translation: CAH89922.1
RefSeqiNP_001124903.1, NM_001131431.1
UniGeneiPab.14695

Genome annotation databases

GeneIDi100171770
KEGGipon:100171770

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857649 mRNA Translation: CAH89922.1
RefSeqiNP_001124903.1, NM_001131431.1
UniGeneiPab.14695

3D structure databases

SMRiQ5RE85
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000015216

Protein family/group databases

CAZyiGT29 Glycosyltransferase Family 29

Proteomic databases

PRIDEiQ5RE85

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100171770
KEGGipon:100171770

Organism-specific databases

CTDi10402

Phylogenomic databases

eggNOGiKOG2692 Eukaryota
ENOG410XT8P LUCA
HOGENOMiHOG000000682
HOVERGENiHBG056676
InParanoidiQ5RE85
KOiK03792

Family and domain databases

Gene3Di3.90.1480.20, 1 hit
InterProiView protein in InterPro
IPR001675 Glyco_trans_29
IPR038578 GT29-like_sf
IPR012163 Sialyl_trans
PfamiView protein in Pfam
PF00777 Glyco_transf_29, 1 hit
PIRSFiPIRSF005557 Sialyl_trans, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSIA10_PONAB
AccessioniPrimary (citable) accession number: Q5RE85
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: December 21, 2004
Last modified: April 25, 2018
This is version 55 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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