Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q80WV3

- CHST2_MOUSE

UniProt

Q80WV3 - CHST2_MOUSE

Protein

Carbohydrate sulfotransferase 2

Gene

Chst2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues within keratan-like structures on N-linked glycans and within mucin-associated glycans that can ultimately serve as SELL ligands. SELL ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation. Participates in biosynthesis of the SELL ligand sialyl 6-sulfo Lewis X and in lymphocyte homing to Peyer patches. Has no activity toward O-linked sugars. Its substrate specificity may be influenced by its subcellular location. Sulfates GlcNAc residues at terminal, non-reducing ends of oligosaccharide chains.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi173 – 1797PAPSBy similarity
    Nucleotide bindingi332 – 3409PAPSBy similarity

    GO - Molecular functioni

    1. N-acetylglucosamine 6-O-sulfotransferase activity Source: Ensembl
    2. sulfotransferase activity Source: MGI

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW
    2. inflammatory response Source: UniProtKB-KW
    3. N-acetylglucosamine metabolic process Source: MGI
    4. sulfur compound metabolic process Source: Ensembl

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Inflammatory response

    Enzyme and pathway databases

    ReactomeiREACT_198578. Keratan sulfate biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbohydrate sulfotransferase 2 (EC:2.8.2.-)
    Alternative name(s):
    Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 2
    Short name:
    GST-2
    N-acetylglucosamine 6-O-sulfotransferase 1
    Short name:
    GlcNAc6ST-1
    Short name:
    Gn6st-1
    Gene namesi
    Name:Chst2
    Synonyms:Gst2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1891160. Chst2.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: InterPro
    2. integral component of membrane Source: UniProtKB-KW
    3. trans-Golgi network Source: Ensembl

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice are impaired in the elaboration of sialyl 6-sulfo Lewis X in HEV. Lymphocyte homing to peripheral lymph nodes, mesenteric lymph nodes, and Peyer patches are significantly reduced.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 530530Carbohydrate sulfotransferase 2PRO_0000085187Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ80WV3.
    PRIDEiQ80WV3.

    PTM databases

    PhosphoSiteiQ80WV3.

    Expressioni

    Tissue specificityi

    In brain, it is expressed in pyramidal cells in the CA3 subregion of the hippocampus, cerebellar nucleus and Purkinje cells.2 Publications

    Gene expression databases

    ArrayExpressiQ80WV3.
    BgeeiQ80WV3.
    CleanExiMM_CHST2.
    GenevestigatoriQ80WV3.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Homodimerization is not essential for enzyme activity By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ80WV3.
    SMRiQ80WV3. Positions 417-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5454CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini76 – 530455LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei55 – 7521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG67451.
    GeneTreeiENSGT00530000062902.
    HOGENOMiHOG000261614.
    HOVERGENiHBG050949.
    InParanoidiQ80WV3.
    KOiK04745.
    OMAiMGGPADY.
    OrthoDBiEOG7RZ5S0.
    TreeFamiTF342871.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR016469. Carbohydrate_sulfotransferase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
    SUPFAMiSSF52540. SSF52540. 3 hits.

    Sequencei

    Sequence statusi: Complete.

    Q80WV3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRSSPRALP PGALPRPLPA APAAVQRALL PPWPRRAGRR WPASPLGMKV    50
    FRRKALVLCA GYALLLVLTM LNLLDYKWHK EPLQQCNPDG PLGAAVGAAG 100
    AGWGRPGSPP AAPPRAHSRM DPRTPYRPPA AGVGAVPAAA AGSAGAAASL 150
    GNATRGTRGG GDKRQLVYVF TTWRSGSSFF GELFNQNPEV FFLYEPVWHV 200
    WQKLYPGDAV SLQGAARDML SALYRCDLSV FQLYSPAGSG GRNLTTLGIF 250
    GAATNKVVCS SPLCPAYRKE VVGLVDDRVC KKCPPQRLAR FEEECRKYRT 300
    LVIKGVRVFD VAVLAPLLKD PALDLKVIHL VRDPRAVASS RIRSRHGLIR 350
    ESLQVVRSRD PRAHRMPFLE AAGHKLGAKK EGMGGPADYH ALGAMEVICN 400
    SMAKTLQTAL QPPDWLQGHY LVVRYEDLVG DPVKTLRRVY DFVGLLVSPE 450
    MEQFALNMTS GSGSSSKPFV VSARNATQAA NAWRTALTFQ QIKQVEEFCY 500
    QPMAVLGYER VNSPEEVKDL SKTLLRKPRL 530
    Length:530
    Mass (Da):57,828
    Last modified:July 27, 2011 - v3
    Checksum:i275363BF15440730
    GO

    Sequence cautioni

    The sequence AAH51963.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA32137.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA32139.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD16775.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti301 – 3011L → V in BAA32137. (PubMed:9712885)Curated
    Sequence conflicti301 – 3011L → V in BAA32139. (PubMed:9712885)Curated
    Sequence conflicti301 – 3011L → V in BAA32138. (PubMed:9712885)Curated
    Sequence conflicti301 – 3011L → V in BAD16775. (PubMed:15175329)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011451 mRNA. Translation: BAA32137.1. Different initiation.
    AB011452 mRNA. Translation: BAA32138.1.
    AB011452 mRNA. Translation: BAA32139.1. Different initiation.
    AB125058 Genomic DNA. Translation: BAD16775.1. Different initiation.
    AC144813 Genomic DNA. No translation available.
    BC051963 mRNA. Translation: AAH51963.2. Different initiation.
    CCDSiCCDS52888.1.
    RefSeqiNP_061233.2. NM_018763.2.
    UniGeneiMm.212446.

    Genome annotation databases

    EnsembliENSMUST00000036267; ENSMUSP00000040775; ENSMUSG00000033350.
    GeneIDi54371.
    KEGGimmu:54371.
    UCSCiuc009raz.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB011451 mRNA. Translation: BAA32137.1 . Different initiation.
    AB011452 mRNA. Translation: BAA32138.1 .
    AB011452 mRNA. Translation: BAA32139.1 . Different initiation.
    AB125058 Genomic DNA. Translation: BAD16775.1 . Different initiation.
    AC144813 Genomic DNA. No translation available.
    BC051963 mRNA. Translation: AAH51963.2 . Different initiation.
    CCDSi CCDS52888.1.
    RefSeqi NP_061233.2. NM_018763.2.
    UniGenei Mm.212446.

    3D structure databases

    ProteinModelPortali Q80WV3.
    SMRi Q80WV3. Positions 417-501.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q80WV3.

    Proteomic databases

    PaxDbi Q80WV3.
    PRIDEi Q80WV3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000036267 ; ENSMUSP00000040775 ; ENSMUSG00000033350 .
    GeneIDi 54371.
    KEGGi mmu:54371.
    UCSCi uc009raz.2. mouse.

    Organism-specific databases

    CTDi 9435.
    MGIi MGI:1891160. Chst2.

    Phylogenomic databases

    eggNOGi NOG67451.
    GeneTreei ENSGT00530000062902.
    HOGENOMi HOG000261614.
    HOVERGENi HBG050949.
    InParanoidi Q80WV3.
    KOi K04745.
    OMAi MGGPADY.
    OrthoDBi EOG7RZ5S0.
    TreeFami TF342871.

    Enzyme and pathway databases

    Reactomei REACT_198578. Keratan sulfate biosynthesis.

    Miscellaneous databases

    ChiTaRSi CHST2. mouse.
    NextBioi 311174.
    PROi Q80WV3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q80WV3.
    Bgeei Q80WV3.
    CleanExi MM_CHST2.
    Genevestigatori Q80WV3.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR016469. Carbohydrate_sulfotransferase.
    IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view ]
    Pfami PF00685. Sulfotransfer_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
    SUPFAMi SSF52540. SSF52540. 3 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of an N-acetylglucosamine-6-O-sulfotransferase."
      Uchimura K., Muramatsu H., Kadomatsu K., Fan Q.-W., Kurosawa N., Mitsuoka C., Kannagi R., Habuchi O., Muramatsu T.
      J. Biol. Chem. 273:22577-22583(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Embryo.
    2. "N-acetylglucosamine 6-O-sulfotransferase-1 regulates expression of L-selectin ligands and lymphocyte homing."
      Uchimura K., Kadomatsu K., El-Fasakhany F.M., Singer M.S., Izawa M., Kannagi R., Takeda N., Rosen S.D., Muramatsu T.
      J. Biol. Chem. 279:35001-35008(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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/6.
      Tissue: Brain.
    5. "Human N-acetylglucosamine-6-O-sulfotransferase involved in the biosynthesis of 6-sulfo sialyl Lewis X: molecular cloning, chromosomal mapping, and expression in various organs and tumor cells."
      Uchimura K., Muramatsu H., Kaname T., Ogawa H., Yamakawa T., Fan Q.-W., Mitsuoka C., Kannagi R., Habuchi O., Yokoyama I., Yamamura K., Ozaki T., Nakagawara A., Kadomatsu K., Muramatsu T.
      J. Biochem. 124:670-678(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiCHST2_MOUSE
    AccessioniPrimary (citable) accession number: Q80WV3
    Secondary accession number(s): E9QNG2, O88276, Q794G9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 93 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    It is uncertain whether Met-1 or Met-48 is the initiator.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3