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Protein

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

Gene

ST3GAL1

Organism
Gallus gallus (Chicken)
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 sitei107 – 1071SubstrateBy similarity
Binding sitei149 – 1491SubstrateBy similarity
Binding sitei172 – 1721SubstrateBy similarity
Binding sitei232 – 2321SubstrateBy similarity
Binding sitei268 – 2681SubstrateBy similarity
Binding sitei272 – 2721Substrate; via amide nitrogenBy similarity
Binding sitei292 – 2921Substrate; via amide nitrogenBy similarity
Binding sitei301 – 3011SubstrateBy similarity
Binding sitei318 – 3181SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiR-GGA-2022854. Keratan sulfate biosynthesis.
R-GGA-4085001. Sialic acid metabolism.
R-GGA-977068. Termination of O-glycan biosynthesis.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

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
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 2

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010CytoplasmicSequence analysis
Transmembranei11 – 2818Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini29 – 342314LumenalSequence 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 – 342342CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1PRO_0000149257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi61 ↔ 66By similarity
Disulfide bondi63 ↔ 141By similarity
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence analysis
Disulfide bondi144 ↔ 283By similarity
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence analysis
Glycosylationi229 – 2291N-linked (GlcNAc...)Sequence analysis
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence analysis
Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence analysis
Glycosylationi325 – 3251N-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

PaxDbiQ11200.
PRIDEiQ11200.

Expressioni

Developmental stagei

Expressed in early embryonic stages.

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000026083.

Structurei

3D structure databases

ProteinModelPortaliQ11200.
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.
GeneTreeiENSGT00760000119095.
HOGENOMiHOG000126811.
HOVERGENiHBG054227.
InParanoidiQ11200.
KOiK00780.
OMAiTWFPKQM.
OrthoDBiEOG7C8GH8.
PhylomeDBiQ11200.
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.

Q11200-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTVRKRNVK VFTFAFVLIT VTSFLLNYKH QVTMTTWDPK HIISQFSEQV
60 70 80 90 100
RKLIKFPRRP CSCSTCISEL GHSLWFDQRF NSTMQPFLTS QNALIPEDSY
110 120 130 140 150
RWWLKLQGEK SPKNINDTLK ELFGIIPGDR DPLQERGTFS CRRCAVVGNS
160 170 180 190 200
GNLRQSQYGQ DIDSHDFVLR MNRAPTIGYE SDVGSKTTHH FVYPESYKEL
210 220 230 240 250
AENVSMIVIP FKTLDLRWIV TALTTGTINF TYVPVPRKIK VRKEKVLIYN
260 270 280 290 300
PSFIKYVYEN WLQNHGRYPS TGLLSVIFAL HVCDEVNVYG FGADSKGHWH
310 320 330 340
HYWENNASAG AFRQTGVHDG DFEFNVTLTL ASIEKIKFFK GR
Length:342
Mass (Da):39,540
Last modified:October 1, 1996 - v1
Checksum:i59E657652F4FE949
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80503 mRNA. Translation: CAA56666.1.
PIRiS55675.
RefSeqiNP_990548.1. NM_205217.1.
XP_015138567.1. XM_015283081.1.
UniGeneiGga.3672.

Genome annotation databases

EnsembliENSGALT00000026131; ENSGALP00000026083; ENSGALG00000016210.
GeneIDi396140.
KEGGigga:396140.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80503 mRNA. Translation: CAA56666.1.
PIRiS55675.
RefSeqiNP_990548.1. NM_205217.1.
XP_015138567.1. XM_015283081.1.
UniGeneiGga.3672.

3D structure databases

ProteinModelPortaliQ11200.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000026083.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Proteomic databases

PaxDbiQ11200.
PRIDEiQ11200.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000026131; ENSGALP00000026083; ENSGALG00000016210.
GeneIDi396140.
KEGGigga:396140.

Organism-specific databases

CTDi6482.

Phylogenomic databases

eggNOGiKOG2692. Eukaryota.
ENOG410XT8P. LUCA.
GeneTreeiENSGT00760000119095.
HOGENOMiHOG000126811.
HOVERGENiHBG054227.
InParanoidiQ11200.
KOiK00780.
OMAiTWFPKQM.
OrthoDBiEOG7C8GH8.
PhylomeDBiQ11200.
TreeFamiTF354325.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-GGA-2022854. Keratan sulfate biosynthesis.
R-GGA-4085001. Sialic acid metabolism.
R-GGA-977068. Termination of O-glycan biosynthesis.

Miscellaneous databases

NextBioi20816197.
PROiQ11200.

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. "Molecular cloning and expression of chick Gal beta 1,3GalNAc alpha 2,3-sialyltransferase."
    Kurosawa N., Hamamoto T., Inoue M., Tsuji S.
    Biochim. Biophys. Acta 1244:216-222(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryonic brain.

Entry informationi

Entry nameiSIA4A_CHICK
AccessioniPrimary (citable) accession number: Q11200
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 16, 2016
This is version 107 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. 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.