Carbohydrate sulfotransferase 2 - Mus musculus (Mouse)

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Q80WV3 (CHST2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Chst2
Synonyms:	Gst2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Protein existence	Evidence 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 apparatus › trans-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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Inflammatory response
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	N-acetylglucosamine metabolic process Traceable author statement Ref.1. Source: MGI carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW sulfur compound metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW trans-Golgi network Inferred from electronic annotation. Source: Compara
Molecular_function	N-acetylglucosamine 6-O-sulfotransferase activity Inferred from electronic annotation. Source: Compara sulfotransferase activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 530

530

Carbohydrate sulfotransferase 2

PRO_0000085187

Regions

Topological domain

1 – 54

Cytoplasmic Potential

Transmembrane

55 – 75

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

76 – 530

455

Lumenal Potential

Nucleotide binding

173 – 179

PAPS By similarity

Nucleotide binding

332 – 340

PAPS By similarity

Amino acid modifications

Glycosylation

152

N-linked (GlcNAc...) Potential

Glycosylation

243

N-linked (GlcNAc...) Potential

Glycosylation

457

N-linked (GlcNAc...) Potential

Glycosylation

475

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

301

L → V in BAA32137. Ref.1

Sequence conflict

301

L → V in BAA32139. Ref.1

Sequence conflict

301

L → V in BAA32138. Ref.1

Sequence conflict

301

L → V in BAD16775. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q80WV3 [UniParc].

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

FASTA

530

57,828

        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' referencesShow '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. 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.
IPI	IPI00330667.
RefSeq	NP_061233.2. NM_018763.2.
UniGene	Mm.212446.
3D structure databases
ProteinModelPortal	Q80WV3.
ModBase	Search...
PTM databases
PhosphoSite	Q80WV3.
Proteomic databases
PaxDb	Q80WV3.
PRIDE	Q80WV3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000036267; ENSMUSP00000040775; ENSMUSG00000033350.
GeneID	54371.
KEGG	mmu:54371.
UCSC	uc009raz.2. mouse.
Organism-specific databases
CTD	9435.
MGI	MGI:1891160. Chst2.
Phylogenomic databases
eggNOG	NOG67451.
GeneTree	ENSGT00530000062902.
HOGENOM	HOG000261614.
HOVERGEN	HBG050949.
InParanoid	Q80WV3.
KO	K04745.
OMA	RAHTRLD.
OrthoDB	EOG4GF3FW.
Gene expression databases
ArrayExpress	Q80WV3.
Bgee	Q80WV3.
CleanEx	MM_CHST2.
Genevestigator	Q80WV3.
GermOnline	ENSMUSG00000033350. Mus musculus.
Family and domain databases
InterPro	IPR016469. Carbohydrate_sulfotransferase. IPR000863. Sulfotransferase_dom. [Graphical view]
Pfam	PF00685. Sulfotransfer_1. 1 hit. [Graphical view]
PIRSF	PIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	CHST2. mouse.
NextBio	311174.
SOURCE	Search...

Entry information

Entry name

CHST2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents