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Q9R1I1

- CHST4_MOUSE

UniProt

Q9R1I1 - CHST4_MOUSE

Protein

Carbohydrate sulfotransferase 4

Gene

Chst4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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 mucin-associated glycans that 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 SELL ligand sialyl 6-sulfo Lewis X on SELL counter-receptors SPN/CD43, GLYCAM1 and MADCAM1. Also involved in biosynthesis of SELL ligand recognized by MECA-79 antibody. Plays a central role in lymphocyte trafficking during chronic inflammation. Has a catalytic preference for core 2-branched mucin-type O-glycans. Can use GlcNAcbeta1-6[Galbeta1-3]GalNAc-pNP (core 2), GlcNAcbeta1-6ManOMe and GlcNAcbeta1-2Man oligosaccharide structures as acceptors. Has also activity toward core 3 of GlcNAcbeta1-3GalNAc-pNP. Its substrate specificity may be influenced by its subcellular location.5 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi50 – 567PAPSBy similarity
    Nucleotide bindingi204 – 2129PAPSBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW
    2. inflammatory response Source: UniProtKB-KW
    3. leukocyte tethering or rolling Source: MGI
    4. N-acetylglucosamine metabolic process Source: Ensembl
    5. protein sulfation Source: MGI

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Inflammatory response

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbohydrate sulfotransferase 4 (EC:2.8.2.-)
    Alternative name(s):
    Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3
    Short name:
    GST-3
    High endothelial cells N-acetylglucosamine 6-O-sulfotransferase
    Short name:
    HEC-GlcNAc6ST
    L-selectin ligand sulfotransferase
    Short name:
    LSST
    N-acetylglucosamine 6-O-sulfotransferase 2
    Short name:
    GlcNAc6ST-2
    Short name:
    Gn6st-2
    Gene namesi
    Name:Chst4
    Synonyms:Gst3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1349479. Chst4.

    Subcellular locationi

    Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    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 lymphocyte homing and exhibit faster lymphocyte rolling and reduced lymphocyte sticking in HEV. The epitope of SELL ligands recognized by the MECA-79 antibody is greatly reduced or abolished in the abluminal aspect of HEV.4 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 388388Carbohydrate sulfotransferase 4PRO_0000085194Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi369 – 3691N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ9R1I1.

    PTM databases

    PhosphoSiteiQ9R1I1.

    Expressioni

    Tissue specificityi

    Specifically expressed in HEV.1 Publication

    Gene expression databases

    BgeeiQ9R1I1.
    GenevestigatoriQ9R1I1.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000104845.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R1I1.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 77CytoplasmicSequence Analysis
    Topological domaini29 – 388360LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG80862.
    GeneTreeiENSGT00530000062902.
    HOGENOMiHOG000261614.
    HOVERGENiHBG050949.
    InParanoidiQ9R1I1.
    KOiK04746.
    OrthoDBiEOG7RZ5S0.
    PhylomeDBiQ9R1I1.
    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. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9R1I1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMLLKKGRLL MFLGSQVIVV ALFIHMSVHR HLSQREESRR PVHVLVLSSW    50
    RSGSSFVGQL FGQHPDVFYL MEPAWHVWMT FTSSTAWKLH MAVRDLLRSV 100
    FLCDMSVFDA YMNPGPRKQS SLFQWEQSRA LCSAPVCDFF PAHEISSPKH 150
    CKLLCGQQPF DMVEKACRSH GFVVLKEVRF LSLQALYPLL TDPSLNLHVV 200
    HLVRDPRAVF RSREHTTIEL VVDSHIVLGQ HLETIKEEDQ PYYAMKIICK 250
    SQVDIVKAIQ TLPEALQQRY LFLRYEDLVR APLAQTTRLY KFVGLDFLPH 300
    LQTWVHNVTR GKGMGQHAFH TNARNALNVS QAWRWSLPYE KVSQLQDACG 350
    EAMDLLGYLQ VRSQQEQGNL SLDLLSSSHI LGQVFREG 388
    Length:388
    Mass (Da):44,636
    Last modified:May 1, 2000 - v1
    Checksum:i6D5371AFB6884AEE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti221 – 2211V → M(PubMed:10330415)Curated
    Sequence conflicti221 – 2211V → M(PubMed:16141072)Curated
    Sequence conflicti306 – 3061H → Y(PubMed:10330415)Curated
    Sequence conflicti306 – 3061H → Y(PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF109155 mRNA. Translation: AAD45579.1.
    AF131236 Genomic DNA. Translation: AAD33016.1.
    AK009113 mRNA. Translation: BAB26078.1.
    BC057886 mRNA. Translation: AAH57886.1.
    CCDSiCCDS22659.1.
    RefSeqiNP_036128.3. NM_011998.4.
    XP_006531106.1. XM_006531043.1.
    XP_006531107.1. XM_006531044.1.
    XP_006531108.1. XM_006531045.1.
    UniGeneiMm.89207.

    Genome annotation databases

    EnsembliENSMUST00000109222; ENSMUSP00000104845; ENSMUSG00000035930.
    GeneIDi26887.
    KEGGimmu:26887.
    UCSCiuc009njt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF109155 mRNA. Translation: AAD45579.1 .
    AF131236 Genomic DNA. Translation: AAD33016.1 .
    AK009113 mRNA. Translation: BAB26078.1 .
    BC057886 mRNA. Translation: AAH57886.1 .
    CCDSi CCDS22659.1.
    RefSeqi NP_036128.3. NM_011998.4.
    XP_006531106.1. XM_006531043.1.
    XP_006531107.1. XM_006531044.1.
    XP_006531108.1. XM_006531045.1.
    UniGenei Mm.89207.

    3D structure databases

    ProteinModelPortali Q9R1I1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000104845.

    PTM databases

    PhosphoSitei Q9R1I1.

    Proteomic databases

    PRIDEi Q9R1I1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000109222 ; ENSMUSP00000104845 ; ENSMUSG00000035930 .
    GeneIDi 26887.
    KEGGi mmu:26887.
    UCSCi uc009njt.2. mouse.

    Organism-specific databases

    CTDi 10164.
    MGIi MGI:1349479. Chst4.

    Phylogenomic databases

    eggNOGi NOG80862.
    GeneTreei ENSGT00530000062902.
    HOGENOMi HOG000261614.
    HOVERGENi HBG050949.
    InParanoidi Q9R1I1.
    KOi K04746.
    OrthoDBi EOG7RZ5S0.
    PhylomeDBi Q9R1I1.
    TreeFami TF342871.

    Miscellaneous databases

    NextBioi 304707.
    PROi Q9R1I1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9R1I1.
    Genevestigatori Q9R1I1.

    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. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "A novel, high endothelial venule-specific sulfotransferase expresses 6-sulfo sialyl Lewis(x), an L-selectin ligand displayed by CD34."
      Hiraoka N., Petryniak B., Nakayama J., Tsuboi S., Suzuki M., Yeh J.-C., Izawa D., Tanaka T., Miyasaka M., Lowe J.B., Fukuda M.
      Immunity 11:79-89(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    2. "Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin."
      Bistrup A., Bhakta S., Lee J.K., Belov Y.Y., Gunn M.D., Zuo F.-R., Huang C.-C., Kannagi R., Rosen S.D., Hemmerich S.
      J. Cell Biol. 145:899-910(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C57BL/6.
      Tissue: Tonsil.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Tongue.
    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: FVB/N.
      Tissue: Colon.
    5. "Sulfation of L-selectin ligands by an HEV-restricted sulfotransferase regulates lymphocyte homing to lymph nodes."
      Hemmerich S., Bistrup A., Singer M.S., van Zante A., Lee J.K., Tsay D., Peters M., Carminati J.L., Brennan T.J., Carver-Moore K., Leviten M., Fuentes M.E., Ruddle N.H., Rosen S.D.
      Immunity 15:237-247(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    6. "Lymphocyte-HEV interactions in lymph nodes of a sulfotransferase-deficient mouse."
      van Zante A., Gauguet J.-M., Bistrup A., Tsay D., von Andrian U.H., Rosen S.D.
      J. Exp. Med. 198:1289-1300(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "Detection of a sulfotransferase (HEC-GlcNAc6ST) in high endothelial venules of lymph nodes and in high endothelial venule-like vessels within ectopic lymphoid aggregates: relationship to the MECA-79 epitope."
      Bistrup A., Tsay D., Shenoy P., Singer M.S., Bangia N., Luther S.A., Cyster J.G., Ruddle N.H., Rosen S.D.
      Am. J. Pathol. 164:1635-1644(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
    8. "Core 2 branching beta1,6-N-acetylglucosaminyltransferase and high endothelial venule-restricted sulfotransferase collaboratively control lymphocyte homing."
      Hiraoka N., Kawashima H., Petryniak B., Nakayama J., Mitoma J., Marth J.D., Lowe J.B., Fukuda M.
      J. Biol. Chem. 279:3058-3067(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiCHST4_MOUSE
    AccessioniPrimary (citable) accession number: Q9R1I1
    Secondary accession number(s): Q9WUE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 94 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3