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Protein

CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1

Gene

ST3GAL1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

It may be responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found on sugar chains O-linked to Thr or Ser and also as a terminal sequence on certain gangliosides. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values. The short isoform seems to be catalytically inactive.1 Publication

Catalytic activityi

CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R.1 Publication

Pathwayi: protein glycosylation

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei108 – 1081Substrate
Binding sitei150 – 1501Substrate
Binding sitei173 – 1731Substrate
Binding sitei233 – 2331Substrate
Binding sitei269 – 2691Substrate
Binding sitei273 – 2731Substrate; via amide nitrogen
Binding sitei293 – 2931Substrate; via amide nitrogen
Binding sitei302 – 3021Substrate
Binding sitei319 – 3191Substrate

GO - Molecular functioni

  • beta-galactoside (CMP) alpha-2,3-sialyltransferase activity Source: UniProtKB

GO - Biological processi

  • ganglioside biosynthetic process Source: GO_Central
  • N-acetylneuraminate metabolic process Source: UniProtKB
  • oligosaccharide metabolic process Source: GO_Central
  • protein N-linked glycosylation Source: UniProtKB
  • protein N-linked glycosylation via asparagine Source: GO_Central
  • sialylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Chemistry

SwissLipidsiSLP:000001385.

Names & Taxonomyi

Protein namesi
Recommended name:
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 (EC:2.4.99.4)
Short name:
Alpha 2,3-ST 1
Short name:
Beta-galactoside alpha-2,3-sialyltransferase 1
Alternative name(s):
Gal-NAc6S
Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase
ST3Gal I
Short name:
ST3GalI
ST3GalA.1
ST3O
Sialyltransferase 4A
Short name:
SIAT4-A
Gene namesi
Name:ST3GAL1
Synonyms:SIAT4A
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence analysisAdd
BLAST
Transmembranei12 – 2716Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini28 – 343316LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 343343CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1PRO_0000149256Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...)Sequence analysis
Disulfide bondi62 ↔ 671 Publication
Disulfide bondi64 ↔ 1421 Publication
Glycosylationi82 – 821N-linked (GlcNAc...)Sequence analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi145 ↔ 2841 Publication
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

The soluble form derives from the membrane form by proteolytic processing.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ02745.
PeptideAtlasiQ02745.

Expressioni

Tissue specificityi

The long isoform is abundant in salivary gland, liver, lung, and colon mucosa. Both long and short forms are detected in submaxillary salivary glands.

Interactioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000029883.

Structurei

Secondary structure

1
343
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi63 – 664Combined sources
Beta strandi71 – 733Combined sources
Helixi75 – 806Combined sources
Turni91 – 933Combined sources
Helixi98 – 1058Combined sources
Turni106 – 1083Combined sources
Helixi116 – 1238Combined sources
Turni124 – 1263Combined sources
Turni133 – 1364Combined sources
Helixi137 – 1393Combined sources
Beta strandi144 – 1485Combined sources
Helixi152 – 1543Combined sources
Helixi160 – 1645Combined sources
Beta strandi166 – 1727Combined sources
Helixi181 – 1844Combined sources
Beta strandi189 – 1946Combined sources
Beta strandi206 – 2094Combined sources
Helixi214 – 22310Combined sources
Turni224 – 2263Combined sources
Beta strandi231 – 2355Combined sources
Helixi244 – 2463Combined sources
Beta strandi247 – 2504Combined sources
Helixi252 – 26110Combined sources
Beta strandi267 – 2693Combined sources
Helixi272 – 28312Combined sources
Beta strandi285 – 2917Combined sources
Beta strandi317 – 3193Combined sources
Helixi321 – 33313Combined sources
Beta strandi336 – 3405Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WMLX-ray1.90A46-343[»]
2WNBX-ray1.55A46-343[»]
2WNFX-ray1.25A46-343[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02745.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
HOGENOMiHOG000126811.
HOVERGENiHBG054227.
InParanoidiQ02745.
KOiK00780.

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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q02745-1) [UniParc]FASTAAdd to basket

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
MAPMRKKSTL KLLTLLVLFI FLTSFFLNYS HTVVTTAWFP KQMVIELSEN
60 70 80 90 100
FKKLMKYPYR PCTCTRCIEE QRVSAWFDER FNRSMQPLLT AKNAHLEEDT
110 120 130 140 150
YKWWLRLQRE KQPNNLNDTI RELFQVVPGN VDPLLEKRLV SCRRCAVVGN
160 170 180 190 200
SGNLKESYYG PQIDSHDFVL RMNKAPTEGF EADVGSKTTH HFVYPESFRE
210 220 230 240 250
LAQEVSMILV PFKTTDLEWV ISATTTGRIS HTYVPVPAKI KVKKEKILIY
260 270 280 290 300
HPAFIKYVFD RWLQGHGRYP STGILSVIFS LHICDEVDLY GFGADSKGNW
310 320 330 340
HHYWENNPSA GAFRKTGVHD GDFESNVTTI LASINKIRIF KGR
Length:343
Mass (Da):39,769
Last modified:February 1, 1994 - v1
Checksum:i1840274CEDA0E46D
GO
Isoform Short (identifier: Q02745-2)
Sequence is not available
Note: Seems to lack a 40 residues internal segment.
Length:
Mass (Da):

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97753 mRNA. Translation: AAA31125.1.
PIRiA45073.
RefSeqiNP_001004047.1. NM_001004047.1. [Q02745-1]
UniGeneiSsc.31458.
Ssc.4856.
Ssc.55798.

Genome annotation databases

GeneIDi445537.
KEGGissc:445537.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97753 mRNA. Translation: AAA31125.1.
PIRiA45073.
RefSeqiNP_001004047.1. NM_001004047.1. [Q02745-1]
UniGeneiSsc.31458.
Ssc.4856.
Ssc.55798.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WMLX-ray1.90A46-343[»]
2WNBX-ray1.55A46-343[»]
2WNFX-ray1.25A46-343[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000029883.

Chemistry

SwissLipidsiSLP:000001385.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Proteomic databases

PaxDbiQ02745.
PeptideAtlasiQ02745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi445537.
KEGGissc:445537.

Organism-specific databases

CTDi6482.

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
HOGENOMiHOG000126811.
HOVERGENiHBG054227.
InParanoidiQ02745.
KOiK00780.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

EvolutionaryTraceiQ02745.

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...

Entry informationi

Entry nameiSIA4A_PIG
AccessioniPrimary (citable) accession number: Q02745
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 6, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.