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Protein

CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4

Gene

St3gal4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, and NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids.1 Publication

Catalytic activityi

CMP-N-acetyl-beta-neuraminate + a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-R = CMP + an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-R.1 Publication
CMP-N-acetyl-beta-neuraminate + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R = CMP + N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R.1 Publication

Kineticsi

Relative Vmax is 2:5:1 for Gal-beta-1,3-GlcNAc, Gal-beta-1,4-GlcNAc and Gal-beta-1,3-GalNAc as substrate, respectively.1 Publication
  1. KM=0.75 mM for Gal-beta-1,3-GlcNAc1 Publication
  2. KM=0.22 mM for Gal-beta-1,4-GlcNAc1 Publication
  3. KM=3.0 mM for Gal-beta-1,3-GalNAc1 Publication

    pH dependencei

    Optimum pH is 6.4.1 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.

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionGlycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.99.4 3474
    ReactomeiR-MMU-2022854 Keratan sulfate biosynthesis
    R-MMU-4085001 Sialic acid metabolism
    R-MMU-975577 N-Glycan antennae elongation
    R-MMU-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 4 (EC:2.4.99.21 Publication, EC:2.4.99.61 Publication)
    Short name:
    Alpha 2,3-ST 4
    Short name:
    Beta-galactoside alpha-2,3-sialyltransferase 4
    Alternative name(s):
    Alpha 2,3-sialyltransferase IV
    Gal-beta-1,4-GalNAc-alpha-2,3-sialyltransferase
    ST3Gal IV
    Short name:
    ST3GalIV
    Sialyltransferase 4C
    Short name:
    SIAT4-C
    Gene namesi
    Name:St3gal4
    Synonyms:Siat4c
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 9

    Organism-specific databases

    MGIiMGI:1316743 St3gal4

    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 – 8CytoplasmicSequence analysis8
    Transmembranei9 – 26Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST18
    Topological domaini27 – 333LumenalSequence analysisAdd BLAST307

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001492631 – 333CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4Add BLAST333

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi61N-linked (GlcNAc...) asparagineSequence analysis1
    Disulfide bondi120 ↔ 273By similarity
    Glycosylationi131N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi310N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi329N-linked (GlcNAc...) asparagineSequence analysis1

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    EPDiQ91Y74
    MaxQBiQ91Y74
    PaxDbiQ91Y74
    PRIDEiQ91Y74

    PTM databases

    iPTMnetiQ91Y74
    PhosphoSitePlusiQ91Y74

    Expressioni

    Tissue specificityi

    Found in high levels in all tissues tested.1 Publication

    Gene expression databases

    BgeeiENSMUSG00000032038
    ExpressionAtlasiQ91Y74 baseline and differential
    GenevisibleiQ91Y74 MM

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000034537

    Structurei

    3D structure databases

    ProteinModelPortaliQ91Y74
    SMRiQ91Y74
    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
    HOGENOMiHOG000000682
    HOVERGENiHBG056676
    InParanoidiQ91Y74
    KOiK03494
    OMAiIHYYEQI
    OrthoDBiEOG091G098L
    PhylomeDBiQ91Y74
    TreeFamiTF354325

    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.

    Q91Y74-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTSKSHWKLL ALALVLVVVM VWYSISREDR YIEFFYFPIS EKKEPCFQGE
    60 70 80 90 100
    AERQASKIFG NRSREQPIFL QLKDYFWVKT PSTYELPFGT KGSEDLLLRV
    110 120 130 140 150
    LAITSYSIPE SIKSLECRRC VVVGNGHRLR NSSLGGVINK YDVVIRLNNA
    160 170 180 190 200
    PVAGYEGDVG SKTTIRLFYP ESAHFDPKIE NNPDTLLVLV AFKAMDFHWI
    210 220 230 240 250
    ETILSDKKRV RKGFWKQPPL IWDVNPKQVR ILNPFFMEIA ADKLLSLPIQ
    260 270 280 290 300
    QPRKIKQKPT TGLLAITLAL HLCDLVHIAG FGYPDASNKK QTIHYYEQIT
    310 320 330
    LKSMAGSGHN VSQEAIAIKR MLEMGAVKNL TYF
    Length:333
    Mass (Da):38,058
    Last modified:December 1, 2001 - v1
    Checksum:i4EAB2F09502B54F4
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti131N → T in CAA65076 (PubMed:9184827).Curated1
    Sequence conflicti262G → V in CAA65076 (PubMed:9184827).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X95809 mRNA Translation: CAA65076.1
    AB061305 mRNA Translation: BAB47508.1
    BC050773 mRNA Translation: AAH50773.1
    CCDSiCCDS22956.1
    RefSeqiNP_033204.2, NM_009178.4
    XP_011240735.1, XM_011242433.1
    UniGeneiMm.275973

    Genome annotation databases

    EnsembliENSMUST00000034537; ENSMUSP00000034537; ENSMUSG00000032038
    GeneIDi20443
    KEGGimmu:20443
    UCSCiuc009osm.1 mouse

    Similar proteinsi

    Entry informationi

    Entry nameiSIA4C_MOUSE
    AccessioniPrimary (citable) accession number: Q91Y74
    Secondary accession number(s): P97354, Q61325
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: December 1, 2001
    Last modified: March 28, 2018
    This is version 125 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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health