Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O88199 (CHST3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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 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 names
Name:Chst3
Synonyms:C6st, Gst0
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length472 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 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. Ref.1 Ref.2

Catalytic activity

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

Subcellular location

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

Tissue specificity

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. Ref.1

Disruption phenotype

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. Ref.2

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Carbohydrate sulfotransferase 3
PRO_0000085189

Regions

Topological domain1 – 1919Cytoplasmic Potential
Transmembrane20 – 3819Helical; Signal-anchor for type II membrane protein; Potential
Topological domain39 – 472434Lumenal Potential
Nucleotide binding135 – 1417PAPS By similarity
Nucleotide binding295 – 3039PAPS By similarity

Amino acid modifications

Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation4131N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O88199 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: F021147196D9D339

FASTA47253,997
        10         20         30         40         50         60 
MEKGLALPQD FRDLVHSLKI RGRYVLFLAF VVIVFIFIEK ENKIISRVSD KLKQIPHFVA 

        70         80         90        100        110        120 
DANSTDPALL LSENASLLSL SELDSTFSHL RSRLHNLSLQ LGVEPAMESQ EAGAEKPSQQ 

       130        140        150        160        170        180 
AGAGTRRHVL LMATTRTGSS FVGEFFNQQG NIFYLFEPLW HIERTVFFQQ RGASAAGSAL 

       190        200        210        220        230        240 
VYRDVLKQLL LCDLYVLEPF ISPPPEDHLT QFLFRRGSSR SLCEDPVCTP FVKKVFEKYH 

       250        260        270        280        290        300 
CRNRRCGPLN VTLAGEACRR KDHVALKAVR IRQLEFLQPL VEDPRLDLRV IQLVRDPRAV 

       310        320        330        340        350        360 
LASRIVAFAG KYENWKKWLS EGQDQLSEDE VQRLRGNCES IRLSAELGLR QPAWLRGRYM 

       370        380        390        400        410        420 
LVRYEDVARR PLQKAREMYS FAGIPLTPQV EDWIQKNTQA TRDSSDVYST QKNSSEQFEK 

       430        440        450        460        470 
WRFSMPFKLA QVVQAACGPT MHLFGYKLAR DAASLTNRSI SLLEERGTFW VT 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008937 mRNA. Translation: BAA29054.1.
AB008938 mRNA. Translation: BAA29055.1.
AB062109 Genomic DNA. Translation: BAB72166.1.
BC055055 mRNA. Translation: AAH55055.1.
RefSeqNP_058083.2. NM_016803.3.
UniGeneMm.12866.

3D structure databases

ProteinModelPortalO88199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000065010.

PTM databases

PhosphoSiteO88199.

Proteomic databases

PRIDEO88199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000068690; ENSMUSP00000065010; ENSMUSG00000057337.
ENSMUST00000167915; ENSMUSP00000131532; ENSMUSG00000057337.
GeneID53374.
KEGGmmu:53374.

Organism-specific databases

CTD9469.
MGIMGI:1858224. Chst3.

Phylogenomic databases

eggNOGNOG80862.
GeneTreeENSGT00530000062902.
HOGENOMHOG000261614.
HOVERGENHBG106811.
InParanoidO88199.
KOK01020.
OrthoDBEOG7RZ5S0.
PhylomeDBO88199.

Enzyme and pathway databases

BRENDA2.8.2.17. 3474.

Gene expression databases

ArrayExpressO88199.
BgeeO88199.
GenevestigatorO88199.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
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. 2 hits.
ProtoNetSearch...

Other

NextBio310177.
PROO88199.
SOURCESearch...

Entry information

Entry nameCHST3_MOUSE
AccessionPrimary (citable) accession number: O88199
Secondary accession number(s): Q794I5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 94 of the entry and version 1 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