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O88199

- CHST3_MOUSE

UniProt

O88199 - CHST3_MOUSE

Protein

Carbohydrate sulfotransferase 3

Gene

Chst3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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 the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues of keratan sulfate, another glycosaminoglycan, and the Gal residues in sialyl N-acetyllactosamine (sialyl LacNAc) oligosaccharides. May play a role in the maintenance of naive T-lymphocytes in the spleen.2 Publications

    Catalytic activityi

    3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi135 – 1417PAPSBy similarity
    Nucleotide bindingi295 – 3039PAPSBy similarity

    GO - Molecular functioni

    1. chondroitin 6-sulfotransferase activity Source: MGI
    2. proteoglycan sulfotransferase activity Source: MGI

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW
    2. chondroitin sulfate biosynthetic process Source: MGI
    3. T cell homeostasis Source: MGI

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BRENDAi2.8.2.17. 3474.
    ReactomeiREACT_196514. Chondroitin sulfate biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbohydrate sulfotransferase 3 (EC:2.8.2.17)
    Alternative name(s):
    Chondroitin 6-O-sulfotransferase 1
    Short name:
    C6ST-1
    Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0
    Short name:
    GST-0
    Gene namesi
    Name:Chst3
    Synonyms:C6st, Gst0
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1858224. Chst3.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice are viable through adulthood. In their spleen the level of chondroitin 6'-sulfate is almost undetectable. In the spleen of 5-6 week-old mice, the number of CD62L+CD44(low) T-lymphocytes corresponding to naive T-lymphocytes is significantly decreased, whereas those in other secondary lymphoid organs are unchanged.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 472472Carbohydrate sulfotransferase 3PRO_0000085189Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi74 – 741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiO88199.

    PTM databases

    PhosphoSiteiO88199.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in spleen, lung, eye and stomach. Constitutively expressed at low level during the mid- to late-gestation period. Expressed in the brain in a temporally controlled manner: peaks at 2 weeks after birth in the cerebellum, but at 3 weeks in the cerebrum. Localizes to stromal cells in the bone marrow, and stromal cells in the marginal zone and red pulp of the spleen, but the sense probe did not.1 Publication

    Gene expression databases

    ArrayExpressiO88199.
    BgeeiO88199.
    GenevestigatoriO88199.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000065010.

    Structurei

    3D structure databases

    ProteinModelPortaliO88199.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini39 – 472434LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei20 – 3819Helical; 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.
    HOVERGENiHBG106811.
    InParanoidiO88199.
    KOiK01020.
    OrthoDBiEOG7RZ5S0.
    PhylomeDBiO88199.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    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.

    O88199-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKGLALPQD FRDLVHSLKI RGRYVLFLAF VVIVFIFIEK ENKIISRVSD    50
    KLKQIPHFVA DANSTDPALL LSENASLLSL SELDSTFSHL RSRLHNLSLQ 100
    LGVEPAMESQ EAGAEKPSQQ AGAGTRRHVL LMATTRTGSS FVGEFFNQQG 150
    NIFYLFEPLW HIERTVFFQQ RGASAAGSAL VYRDVLKQLL LCDLYVLEPF 200
    ISPPPEDHLT QFLFRRGSSR SLCEDPVCTP FVKKVFEKYH CRNRRCGPLN 250
    VTLAGEACRR KDHVALKAVR IRQLEFLQPL VEDPRLDLRV IQLVRDPRAV 300
    LASRIVAFAG KYENWKKWLS EGQDQLSEDE VQRLRGNCES IRLSAELGLR 350
    QPAWLRGRYM LVRYEDVARR PLQKAREMYS FAGIPLTPQV EDWIQKNTQA 400
    TRDSSDVYST QKNSSEQFEK WRFSMPFKLA QVVQAACGPT MHLFGYKLAR 450
    DAASLTNRSI SLLEERGTFW VT 472
    Length:472
    Mass (Da):53,997
    Last modified:November 1, 1998 - v1
    Checksum:iF021147196D9D339
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008937 mRNA. Translation: BAA29054.1.
    AB008938 mRNA. Translation: BAA29055.1.
    AB062109 Genomic DNA. Translation: BAB72166.1.
    BC055055 mRNA. Translation: AAH55055.1.
    RefSeqiNP_058083.2. NM_016803.3.
    UniGeneiMm.12866.

    Genome annotation databases

    EnsembliENSMUST00000068690; ENSMUSP00000065010; ENSMUSG00000057337.
    ENSMUST00000167915; ENSMUSP00000131532; ENSMUSG00000057337.
    GeneIDi53374.
    KEGGimmu:53374.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB008937 mRNA. Translation: BAA29054.1 .
    AB008938 mRNA. Translation: BAA29055.1 .
    AB062109 Genomic DNA. Translation: BAB72166.1 .
    BC055055 mRNA. Translation: AAH55055.1 .
    RefSeqi NP_058083.2. NM_016803.3.
    UniGenei Mm.12866.

    3D structure databases

    ProteinModelPortali O88199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000065010.

    PTM databases

    PhosphoSitei O88199.

    Proteomic databases

    PRIDEi O88199.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000068690 ; ENSMUSP00000065010 ; ENSMUSG00000057337 .
    ENSMUST00000167915 ; ENSMUSP00000131532 ; ENSMUSG00000057337 .
    GeneIDi 53374.
    KEGGi mmu:53374.

    Organism-specific databases

    CTDi 9469.
    MGIi MGI:1858224. Chst3.

    Phylogenomic databases

    eggNOGi NOG80862.
    GeneTreei ENSGT00530000062902.
    HOGENOMi HOG000261614.
    HOVERGENi HBG106811.
    InParanoidi O88199.
    KOi K01020.
    OrthoDBi EOG7RZ5S0.
    PhylomeDBi O88199.

    Enzyme and pathway databases

    BRENDAi 2.8.2.17. 3474.
    Reactomei REACT_196514. Chondroitin sulfate biosynthesis.

    Miscellaneous databases

    NextBioi 310177.
    PROi O88199.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88199.
    Bgeei O88199.
    Genevestigatori O88199.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    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. "Mouse chondroitin 6-sulfotransferase: molecular cloning, characterization and chromosomal mapping."
      Uchimura K., Kadomatsu K., Fan Q.-W., Muramatsu H., Kurosawa N., Kaname T., Yamamura K., Fukuta M., Habuchi O., Muramatsu T.
      Glycobiology 8:489-496(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Strain: C57BL/6J.
      Tissue: Spleen.
    2. "Functional analysis of the chondroitin 6-sulfotransferase gene in relation to lymphocyte subpopulations, brain development, and oversulfated chondroitin sulfates."
      Uchimura K., Kadomatsu K., Nishimura H., Muramatsu H., Nakamura E., Kurosawa N., Habuchi O., El-Fasakhany F.M., Yoshikai Y., Muramatsu T.
      J. Biol. Chem. 277:1443-1450(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION.
    3. "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].
      Tissue: Eye.

    Entry informationi

    Entry nameiCHST3_MOUSE
    AccessioniPrimary (citable) accession number: O88199
    Secondary accession number(s): Q794I5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 96 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