Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5RJQ0 (CHST1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
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 1
EC=2.8.2.21
Alternative name(s):
Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 1
Short name=GST-1
Keratan sulfate Gal-6 sulfotransferase
Short name=KS6ST
Short name=KSGal6ST
Short name=KSST
Gene names
Name:Chst1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length411 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 galactose (Gal) residues of keratan. Has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer. The sulfotransferase activity on sialyl LacNAc structures is much higher than the corresponding desialylated substrate, and only internal Gal residues are sulfated. May function in the sulfation of sialyl N-acetyllactosamine oligosaccharide chains attached to glycoproteins. Participates in biosynthesis of selectin ligands. Selectin ligands are present in high endothelial cells (HEVs) and play a central role in lymphocyte homing at sites of inflammation By similarity.

Catalytic activity

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

Subcellular location

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411Carbohydrate sulfotransferase 1
PRO_0000085184

Regions

Topological domain11Cytoplasmic Potential
Transmembrane2 – 2322Helical; Signal-anchor for type II membrane protein; Potential
Topological domain24 – 411388Lumenal Potential
Nucleotide binding69 – 757PAPS By similarity
Nucleotide binding234 – 2429PAPS By similarity
Motif337 – 3393Cell attachment site Potential

Amino acid modifications

Glycosylation561N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation1891N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q5RJQ0 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 715998736106E5CD

FASTA41146,885
        10         20         30         40         50         60 
MQCSWKAVLL LALASIAIQY TAIRTFTAKS FHTCPGLTET GLAERLCEEG PTFSYNLSRK 

        70         80         90        100        110        120 
THVLILATTR SGSSFVGQLF NQHMDVFYLF EPLYHVQNTL IPRFTQGKSP ADRRVMLGAS 

       130        140        150        160        170        180 
RDLLRSLYDC DLYFLENYIK PPPVNHTTDR VFRRGASRVL CSRPVCDPPG ASDLILEEGD 

       190        200        210        220        230        240 
CVRKCGLLNL TLAAEACRER SHVAIKTVRV PEVNDLRALV EDPRLNLKVI QLVRDPRGIL 

       250        260        270        280        290        300 
ASRSETFRDT YRLWRLWYGT GRKPYNLDVT QLTTVCEDFS SSVSTGLMRP SWLKGKYMLV 

       310        320        330        340        350        360 
RYEDLARNPM KKTEEIYEFL GIPLDSHVAR WIQNNTRGDP TLGKHKYGTV RNSAATAEKW 

       370        380        390        400        410 
RFRLSYDIVA FAQNACQHVL AQLGYKMATS EEELKNPAIS LVEERDFRPF L

« Hide

References

[1]"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: Ovary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC086551 mRNA. Translation: AAH86551.1.
IPIIPI00195966.
RefSeqNP_001011955.1. NM_001011955.1.
UniGeneRn.16695.

3D structure databases

ProteinModelPortalQ5RJQ0.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000010510.

Proteomic databases

PaxDbQ5RJQ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010510; ENSRNOP00000010510; ENSRNOG00000007989.
GeneID295934.
KEGGrno:295934.
UCSCRGD:1308142. rat.

Organism-specific databases

CTD8534.
RGD1308142. Chst1.

Phylogenomic databases

eggNOGNOG80862.
GeneTreeENSGT00530000062902.
HOGENOMHOG000261614.
HOVERGENHBG106811.
InParanoidQ5RJQ0.
KOK01022.
OMALWRIWDG.
OrthoDBEOG418BNF.

Gene expression databases

GenevestigatorQ5RJQ0.
GermOnlineENSRNOG00000007989. Rattus norvegicus.

Family and domain databases

InterProIPR016469. Carbohydrate_sulfotransferase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
PIRSFPIRSF005883. Carbohydrate_sulfotransferase. 1 hit.
ProtoNetSearch...

Other

NextBio640351.

Entry information

Entry nameCHST1_RAT
AccessionPrimary (citable) accession number: Q5RJQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: December 21, 2004
Last modified: April 3, 2013
This is version 65 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents