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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)DescriptionActionsGraphical viewLength
Binding sitei108Substrate1
Binding sitei150Substrate1
Binding sitei173Substrate1
Binding sitei233Substrate1
Binding sitei269Substrate1
Binding sitei273Substrate; via amide nitrogen1
Binding sitei293Substrate; via amide nitrogen1
Binding sitei302Substrate1
Binding sitei319Substrate1

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 databases

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)DescriptionActionsGraphical viewLength
Topological domaini1 – 11CytoplasmicSequence analysisAdd BLAST11
Transmembranei12 – 27Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST16
Topological domaini28 – 343LumenalSequence analysisAdd BLAST316

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001492561 – 343CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1Add BLAST343

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi28N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi62 ↔ 671 Publication
Disulfide bondi64 ↔ 1421 Publication
Glycosylationi82N-linked (GlcNAc...)Sequence analysis1
Glycosylationi117N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi145 ↔ 2841 Publication
Glycosylationi326N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ02745.
PeptideAtlasiQ02745.
PRIDEiQ02745.

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

1343
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi63 – 66Combined sources4
Beta strandi71 – 73Combined sources3
Helixi75 – 80Combined sources6
Turni91 – 93Combined sources3
Helixi98 – 105Combined sources8
Turni106 – 108Combined sources3
Helixi116 – 123Combined sources8
Turni124 – 126Combined sources3
Turni133 – 136Combined sources4
Helixi137 – 139Combined sources3
Beta strandi144 – 148Combined sources5
Helixi152 – 154Combined sources3
Helixi160 – 164Combined sources5
Beta strandi166 – 172Combined sources7
Helixi181 – 184Combined sources4
Beta strandi189 – 194Combined sources6
Beta strandi206 – 209Combined sources4
Helixi214 – 223Combined sources10
Turni224 – 226Combined sources3
Beta strandi231 – 235Combined sources5
Helixi244 – 246Combined sources3
Beta strandi247 – 250Combined sources4
Helixi252 – 261Combined sources10
Beta strandi267 – 269Combined sources3
Helixi272 – 283Combined sources12
Beta strandi285 – 291Combined sources7
Beta strandi317 – 319Combined sources3
Helixi321 – 333Combined sources13
Beta strandi336 – 340Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WMLX-ray1.90A46-343[»]
2WNBX-ray1.55A46-343[»]
2WNFX-ray1.25A46-343[»]
SMRiQ02745.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WMLX-ray1.90A46-343[»]
2WNBX-ray1.55A46-343[»]
2WNFX-ray1.25A46-343[»]
SMRiQ02745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000029883.

Chemistry databases

SwissLipidsiSLP:000001385.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Proteomic databases

PaxDbiQ02745.
PeptideAtlasiQ02745.
PRIDEiQ02745.

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: November 2, 2016
This is version 111 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.