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Q80WV3 (CHST2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Chst2
Synonyms:Gst2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.1 Ref.2

Subunit structure

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

Subcellular location

Golgi apparatustrans-Golgi network membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

In brain, it is expressed in pyramidal cells in the CA3 subregion of the hippocampus, cerebellar nucleus and Purkinje cells. Ref.1 Ref.5

Disruption phenotype

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. Ref.2

Sequence similarities

Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc subfamily.

Caution

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

Sequence caution

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Carbohydrate sulfotransferase 2
PRO_0000085187

Regions

Topological domain1 – 5454Cytoplasmic Potential
Transmembrane55 – 7521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain76 – 530455Lumenal Potential
Nucleotide binding173 – 1797PAPS By similarity
Nucleotide binding332 – 3409PAPS By similarity

Amino acid modifications

Glycosylation2431N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation4751N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3011L → V in BAA32137. Ref.1
Sequence conflict3011L → V in BAA32139. Ref.1
Sequence conflict3011L → V in BAA32138. Ref.1
Sequence conflict3011L → V in BAD16775. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q80WV3 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 275363BF15440730

FASTA53057,828
        10         20         30         40         50         60 
MSRSSPRALP PGALPRPLPA APAAVQRALL PPWPRRAGRR WPASPLGMKV FRRKALVLCA 

        70         80         90        100        110        120 
GYALLLVLTM LNLLDYKWHK EPLQQCNPDG PLGAAVGAAG AGWGRPGSPP AAPPRAHSRM 

       130        140        150        160        170        180 
DPRTPYRPPA AGVGAVPAAA AGSAGAAASL GNATRGTRGG GDKRQLVYVF TTWRSGSSFF 

       190        200        210        220        230        240 
GELFNQNPEV FFLYEPVWHV WQKLYPGDAV SLQGAARDML SALYRCDLSV FQLYSPAGSG 

       250        260        270        280        290        300 
GRNLTTLGIF GAATNKVVCS SPLCPAYRKE VVGLVDDRVC KKCPPQRLAR FEEECRKYRT 

       310        320        330        340        350        360 
LVIKGVRVFD VAVLAPLLKD PALDLKVIHL VRDPRAVASS RIRSRHGLIR ESLQVVRSRD 

       370        380        390        400        410        420 
PRAHRMPFLE AAGHKLGAKK EGMGGPADYH ALGAMEVICN SMAKTLQTAL QPPDWLQGHY 

       430        440        450        460        470        480 
LVVRYEDLVG DPVKTLRRVY DFVGLLVSPE MEQFALNMTS GSGSSSKPFV VSARNATQAA 

       490        500        510        520        530 
NAWRTALTFQ QIKQVEEFCY QPMAVLGYER VNSPEEVKDL SKTLLRKPRL 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_061233.2. NM_018763.2.
UniGeneMm.212446.

3D structure databases

ProteinModelPortalQ80WV3.
SMRQ80WV3. Positions 417-501.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ80WV3.

Proteomic databases

PaxDbQ80WV3.
PRIDEQ80WV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000036267; ENSMUSP00000040775; ENSMUSG00000033350.
GeneID54371.
KEGGmmu:54371.
UCSCuc009raz.2. mouse.

Organism-specific databases

CTD9435.
MGIMGI:1891160. Chst2.

Phylogenomic databases

eggNOGNOG67451.
GeneTreeENSGT00530000062902.
HOGENOMHOG000261614.
HOVERGENHBG050949.
InParanoidQ80WV3.
KOK04745.
OMAMGGPADY.
OrthoDBEOG7RZ5S0.
TreeFamTF342871.

Gene expression databases

ArrayExpressQ80WV3.
BgeeQ80WV3.
CleanExMM_CHST2.
GenevestigatorQ80WV3.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR016469. Carbohydrate_sulfotransferase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
PIRSFPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
SUPFAMSSF52540. SSF52540. 3 hits.
ProtoNetSearch...

Other

ChiTaRSCHST2. mouse.
NextBio311174.
PROQ80WV3.
SOURCESearch...

Entry information

Entry nameCHST2_MOUSE
AccessionPrimary (citable) accession number: Q80WV3
Secondary accession number(s): E9QNG2, O88276, Q794G9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot