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Q7LGC8 (CHST3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·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
Chondroitin 6-sulfotransferase
Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 0
Short name=GST-0
Gene names
Name:CHST3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 in adult tissues. Expressed in heart, placenta, skeletal muscle and pancreas. Also expressed in various immune tissues such as spleen, lymph node, thymus and appendix. Ref.1

Involvement in disease

Spondyloepiphyseal dysplasia with congenital joint dislocations (SEDC-JD) [MIM:143095]: A bone dysplasia clinically characterized by dislocation of the knees and/or hips at birth, clubfoot, elbow joint dysplasia with subluxation and limited extension, short stature, and progressive kyphosis developing in late childhood. The disorder is usually evident at birth, with short stature and multiple joint dislocations or subluxations that dominate the neonatal clinical and radiographic picture. During childhood, the dislocations improve, both spontaneously and with surgical treatment, and features of spondyloepiphyseal dysplasia become apparent, leading to arthritis of the hips and spine with intervertebral disk degeneration, rigid kyphoscoliosis, and trunk shortening by late childhood.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.5

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Carbohydrate sulfotransferase 3
PRO_0000085188

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 3818Helical; Signal-anchor for type II membrane protein; Potential
Topological domain39 – 479441Lumenal Potential
Nucleotide binding141 – 1477PAPS By similarity
Nucleotide binding301 – 3099PAPS By similarity

Amino acid modifications

Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation4201N-linked (GlcNAc...) Potential
Glycosylation4641N-linked (GlcNAc...) Potential

Natural variations

Natural variant2221R → W in SEDC-JD; severely impairs or abolishes the enzyme function. Ref.5
VAR_047856
Natural variant2591L → P in SEDC-JD; severely impairs or abolishes the enzyme function. Ref.5
VAR_047857
Natural variant3041R → Q in SEDC-JD; reduced enzyme activity. Ref.4
Corresponds to variant rs28937593 [ dbSNP | Ensembl ].
VAR_021413
Natural variant3071L → P in SEDC-JD. Ref.5
VAR_047858
Natural variant3481I → M.
Corresponds to variant rs3740128 [ dbSNP | Ensembl ].
VAR_021414
Natural variant3571R → Q. Ref.3 Ref.5
Corresponds to variant rs3740129 [ dbSNP | Ensembl ].
VAR_021415
Natural variant3721E → K in SEDC-JD. Ref.5
VAR_047859

Experimental info

Sequence conflict3871R → P in BAA32576. Ref.1
Sequence conflict4431A → P in BAA32576. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7LGC8 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 7C290DC4970F66E0

FASTA47954,706
        10         20         30         40         50         60 
MEKGLTLPQD CRDFVHSLKM RSKYALFLVF VVIVFVFIEK ENKIISRVSD KLKQIPQALA 

        70         80         90        100        110        120 
DANSTDPALI LAENASLLSL SELDSAFSQL QSRLRNLSLQ LGVEPAMEAA GEEEEEQRKE 

       130        140        150        160        170        180 
EEPPRPAVAG PRRHVLLMAT TRTGSSFVGE FFNQQGNIFY LFEPLWHIER TVSFEPGGAN 

       190        200        210        220        230        240 
AAGSALVYRD VLKQLFLCDL YVLEHFITPL PEDHLTQFMF RRGSSRSLCE DPVCTPFVKK 

       250        260        270        280        290        300 
VFEKYHCKNR RCGPLNVTLA AEACRRKEHM ALKAVRIRQL EFLQPLAEDP RLDLRVIQLV 

       310        320        330        340        350        360 
RDPRAVLASR MVAFAGKYKT WKKWLDDEGQ DGLREEEVQR LRGNCESIRL SAELGLRQPA 

       370        380        390        400        410        420 
WLRGRYMLVR YEDVARGPLQ KAREMYRFAG IPLTPQVEDW IQKNTQAAHD GSGIYSTQKN 

       430        440        450        460        470 
SSEQFEKWRF SMPFKLAQVV QAACGPAMRL FGYKLARDAA ALTNRSVSLL EERGTFWVT 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of human chondroitin 6-sulfotransferase."
Fukuta M., Kobayashi Y., Uchimura K., Kimata K., Habuchi O.
Biochim. Biophys. Acta 1399:57-61(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"Functional expression and genomic structure of human chondroitin 6-sulfotransferase."
Tsutsumi K., Shimakawa H., Kitagawa H., Sugahara K.
FEBS Lett. 441:235-241(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Placenta.
[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], VARIANT GLN-357.
Tissue: Liver.
[4]"Loss of chondroitin 6-O-sulfotransferase-1 function results in severe human chondrodysplasia with progressive spinal involvement."
Thiele H., Sakano M., Kitagawa H., Sugahara K., Rajab A., Hoehne W., Ritter H., Leschik G., Nuernberg P., Mundlos S.
Proc. Natl. Acad. Sci. U.S.A. 101:10155-10160(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SEDC-JD GLN-304.
[5]"Congenital joint dislocations caused by carbohydrate sulfotransferase 3 deficiency in recessive Larsen syndrome and humero-spinal dysostosis."
Hermanns P., Unger S., Rossi A., Perez-Aytes A., Cortina H., Bonafe L., Boccone L., Setzu V., Dutoit M., Sangiorgi L., Pecora F., Reicherter K., Nishimura G., Spranger J., Zabel B., Superti-Furga A.
Am. J. Hum. Genet. 82:1368-1374(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SEDC-JD TRP-222; PRO-259; PRO-307 AND LYS-372, VARIANT GLN-357, CHARACTERIZATION OF VARIANTS SEDC-JD TRP-222 AND PRO-259.
[6]Erratum
Hermanns P., Unger S., Rossi A., Perez-Aytes A., Cortina H., Bonafe L., Boccone L., Setzu V., Dutoit M., Sangiorgi L., Pecora F., Reicherter K., Nishimura G., Spranger J., Zabel B., Superti-Furga A.
Am. J. Hum. Genet. 83:293-293(2008)
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012192 mRNA. Translation: BAA32576.1.
AB017915 mRNA. Translation: BAA36348.1.
BC093690 mRNA. Translation: AAH93690.1.
BC104856 mRNA. Translation: AAI04857.1.
RefSeqNP_004264.2. NM_004273.4.
UniGeneHs.158304.

3D structure databases

ProteinModelPortalQ7LGC8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114855. 2 interactions.
STRING9606.ENSP00000362207.

PTM databases

PhosphoSiteQ7LGC8.

Polymorphism databases

DMDM116241297.

Proteomic databases

PaxDbQ7LGC8.
PRIDEQ7LGC8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373115; ENSP00000362207; ENSG00000122863.
GeneID9469.
KEGGhsa:9469.
UCSCuc001jsn.3. human.

Organism-specific databases

CTD9469.
GeneCardsGC10P073724.
HGNCHGNC:1971. CHST3.
HPAHPA055704.
MIM143095. phenotype.
603799. gene.
neXtProtNX_Q7LGC8.
Orphanet263463. CHST3-related skeletal dysplasia.
PharmGKBPA26503.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80862.
HOGENOMHOG000261614.
HOVERGENHBG106811.
InParanoidQ7LGC8.
KOK01020.
OMAIPFKLAQ.
OrthoDBEOG7RZ5S0.
PhylomeDBQ7LGC8.
TreeFamTF342871.

Enzyme and pathway databases

BioCycMetaCyc:HS04610-MONOMER.
BRENDA2.8.2.17. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeQ7LGC8.
CleanExHS_CHST3.
GenevestigatorQ7LGC8.

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

GenomeRNAi9469.
NextBio35486.
PROQ7LGC8.
SOURCESearch...

Entry information

Entry nameCHST3_HUMAN
AccessionPrimary (citable) accession number: Q7LGC8
Secondary accession number(s): O75099, Q52M30
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM