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Protein

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

Gene

St3gal1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.

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.

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 sitei102 – 1021SubstrateBy similarity
Binding sitei144 – 1441SubstrateBy similarity
Binding sitei167 – 1671SubstrateBy similarity
Binding sitei227 – 2271SubstrateBy similarity
Binding sitei263 – 2631SubstrateBy similarity
Binding sitei267 – 2671Substrate; via amide nitrogenBy similarity
Binding sitei287 – 2871Substrate; via amide nitrogenBy similarity
Binding sitei296 – 2961SubstrateBy similarity
Binding sitei313 – 3131SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  • N-acetylneuraminate metabolic process Source: UniProtKB
  • protein glycosylation Source: MGI
  • protein N-linked glycosylation Source: UniProtKB
  • protein phosphorylation Source: MGI
  • sialylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.99.4. 3474.
ReactomeiR-MMU-2022854. Keratan sulfate biosynthesis.
R-MMU-4085001. Sialic acid metabolism.
R-MMU-977068. Termination of O-glycan biosynthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Chemistry

SwissLipidsiSLP:000001413.

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:Siat4, Siat4a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:98304. St3gal1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence analysis
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini26 – 337312LumenalSequence 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 – 337337CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1PRO_0000149254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 61By similarity
Disulfide bondi58 ↔ 136By similarity
Glycosylationi76 – 761N-linked (GlcNAc...)Sequence analysis
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence analysis
Disulfide bondi139 ↔ 278By similarity
Glycosylationi320 – 3201N-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

EPDiP54751.
PaxDbiP54751.
PRIDEiP54751.

Expressioni

Tissue specificityi

Highly expressed in submaxillary gland and to a much lesser extent in liver, lung, kidney, heart and brain.

Gene expression databases

BgeeiP54751.
ExpressionAtlasiP54751. baseline and differential.
GenevisibleiP54751. MM.

Interactioni

Protein-protein interaction databases

IntActiP54751. 1 interaction.
MINTiMINT-4134677.
STRINGi10090.ENSMUSP00000090307.

Structurei

3D structure databases

ProteinModelPortaliP54751.
SMRiP54751. Positions 54-337.
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.
HOGENOMiHOG000126811.
HOVERGENiHBG054227.
InParanoidiP54751.
KOiK00780.
OMAiTWFPKQM.
OrthoDBiEOG7C8GH8.
PhylomeDBiP54751.
TreeFamiTF354325.

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.

Sequencei

Sequence statusi: Complete.

P54751-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRKTLKYLT FFLLFIFLTS FVLNYSNTGV PSAWFPKQML LELSENFRRF
60 70 80 90 100
IKSQPCTCRH CISQDKVSYW FDQRFNKTMQ PLLTVHNALM EEDTYRWWLR
110 120 130 140 150
LQRERKPNNL SDTVKELFRL VPGNVDPMLN KRLVGCRRCA VVGNSGNLKD
160 170 180 190 200
SSYGPEIDSH DFVLRMNKAP TVGFEADVGS RTTHHLVYPE SFRELGENVN
210 220 230 240 250
MVLVPFKTTD LQWVISATTT GTITHTYVPV PPKIKVKQEK ILIYHPAFIK
260 270 280 290 300
YVFDNWLQGH GRYPSTGILS IIFSIHICDE VDLYGFGADS KGNWHHYWEN
310 320 330
NPSAGAFRKT GVHDGDFEYN ITTTLAAINK IRIFKGR
Length:337
Mass (Da):39,073
Last modified:October 1, 1996 - v1
Checksum:iCB54929D1EC047D1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73523 mRNA. Translation: CAA51919.1.
BC084730 mRNA. Translation: AAH84730.1.
CCDSiCCDS27511.1.
PIRiS36824.
RefSeqiNP_033203.1. NM_009177.4.
XP_006520727.1. XM_006520664.2.
XP_006520728.1. XM_006520665.2.
XP_011243830.1. XM_011245528.1.
XP_011243831.1. XM_011245529.1.
UniGeneiMm.248334.
Mm.442417.
Mm.461082.

Genome annotation databases

EnsembliENSMUST00000092640; ENSMUSP00000090307; ENSMUSG00000013846.
GeneIDi20442.
KEGGimmu:20442.
UCSCiuc007wba.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

ST3Gal I

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73523 mRNA. Translation: CAA51919.1.
BC084730 mRNA. Translation: AAH84730.1.
CCDSiCCDS27511.1.
PIRiS36824.
RefSeqiNP_033203.1. NM_009177.4.
XP_006520727.1. XM_006520664.2.
XP_006520728.1. XM_006520665.2.
XP_011243830.1. XM_011245528.1.
XP_011243831.1. XM_011245529.1.
UniGeneiMm.248334.
Mm.442417.
Mm.461082.

3D structure databases

ProteinModelPortaliP54751.
SMRiP54751. Positions 54-337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP54751. 1 interaction.
MINTiMINT-4134677.
STRINGi10090.ENSMUSP00000090307.

Chemistry

SwissLipidsiSLP:000001413.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Proteomic databases

EPDiP54751.
PaxDbiP54751.
PRIDEiP54751.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000092640; ENSMUSP00000090307; ENSMUSG00000013846.
GeneIDi20442.
KEGGimmu:20442.
UCSCiuc007wba.1. mouse.

Organism-specific databases

CTDi6482.
MGIiMGI:98304. St3gal1.

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
HOGENOMiHOG000126811.
HOVERGENiHBG054227.
InParanoidiP54751.
KOiK00780.
OMAiTWFPKQM.
OrthoDBiEOG7C8GH8.
PhylomeDBiP54751.
TreeFamiTF354325.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.99.4. 3474.
ReactomeiR-MMU-2022854. Keratan sulfate biosynthesis.
R-MMU-4085001. Sialic acid metabolism.
R-MMU-977068. Termination of O-glycan biosynthesis.

Miscellaneous databases

ChiTaRSiSt3gal1. mouse.
NextBioi298484.
PROiP54751.
SOURCEiSearch...

Gene expression databases

BgeeiP54751.
ExpressionAtlasiP54751. baseline and differential.
GenevisibleiP54751. MM.

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

« Hide 'large scale' publications
  1. "Molecular cloning and expression of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase from mouse brain."
    Lee Y.-C., Kurosawa N., Hamamoto T., Nakaoka T., Tsuji S.
    Eur. J. Biochem. 216:377-385(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.

Entry informationi

Entry nameiSIA4A_MOUSE
AccessioniPrimary (citable) accession number: P54751
Secondary accession number(s): Q11202
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 130 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.