Identification |
HMDB Protein ID
| HMDBP00288 |
Secondary Accession Numbers
| |
Name
| Carbohydrate sulfotransferase 13 |
Synonyms
|
- C4ST-3
- C4ST3
- Chondroitin 4-O-sulfotransferase 3
- Chondroitin 4-sulfotransferase 3
|
Gene Name
| CHST13 |
Protein Type
| Enzyme |
Biological Properties |
General Function
| Involved in sulfotransferase activity |
Specific Function
| Catalyzes the transfer of sulfate to position 4 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. Transfers sulfate to the C4 hydroxyl of beta1,4-linked GalNAc that is substituted with a beta-linked glucuronic acid at the C-3 hydroxyl. No activity toward dermatan.
|
Pathways
|
- Glycosaminoglycan biosynthesis - chondroitin sulfate / dermatan sulfate
- Sulfur metabolism
|
Reactions
|
Phosphoadenosine phosphosulfate + Chondroitin → Adenosine 3',5'-diphosphate + chondroitin 4'-sulfate |
details
|
Phosphoadenosine phosphosulfate + Chondroitin → Adenosine 3',5'-diphosphate + Chondroitin 4-sulfate |
details
|
|
GO Classification
|
Biological Process |
chondroitin sulfate biosynthetic process |
carbohydrate biosynthetic process |
carbohydrate metabolic process |
Cellular Component |
integral to membrane |
Golgi membrane |
Component |
cell part |
membrane part |
intrinsic to membrane |
integral to membrane |
Function |
catalytic activity |
transferase activity |
transferase activity, transferring sulfur-containing groups |
sulfotransferase activity |
Molecular Function |
chondroitin 4-sulfotransferase activity |
N-acetylgalactosamine 4-O-sulfotransferase activity |
Process |
metabolic process |
primary metabolic process |
carbohydrate metabolic process |
carbohydrate biosynthetic process |
|
Cellular Location
|
- Golgi apparatus membrane
- Single-pass type II membrane protein
|
Gene Properties |
Chromosome Location
| 3 |
Locus
| 3q21.3 |
SNPs
| CHST13 |
Gene Sequence
|
>1026 bp
ATGGGGAGGCGCTGCTGCCGGCGGCGCGTGCTGGCGGCCGCCTGTCTGGGCGCCGCGCTC
CTGCTCCTATGCGCCGCGCCCCGCTCCCTGCGCCCGGCATTTGGAAACAGAGCCCTGGGC
TCCAGCTGGCTTGGTGGGGAGAAGAGAAGCCCCCTGCAGAAGCTCTATGACCTGGATCAG
GACCCGCGCTCGACCCTGGCGAAGGTGCACCGTCAGCGGCGCGACCTGCTGAACAGCGCC
TGTAGCCGCCACTCACGCCGGCAGCGCCTGCTACAGCCGGAGGACCTGCGGCACGTGCTG
GTGGACGACGCGCATGGCCTGCTCTACTGCTACGTGCCCAAGGTGGCCTGCACCAACTGG
AAGCGCGTGCTGCTGGCGCTGAGCGGCCAAGCCCGCGGCGACCCGCGCGCCATCTCCGCG
CAAGAGGCGCACGCGCCTGGCCGCCTGCCCTCACTGGCCGACTTCAGCCCCGCCGAGATC
AACCGGCGCCTGCGCGCCTACTTGGCCTTCCTGTTCGTGCGGGAGCCCTTCGAGCGCCTG
GCATCGGCTTACCGCAACAAGCTCGCGCGCCCCTACAGCGCCGCCTTCCAGAGGCGCTAC
GGTGCACGCATCGTTCAGCGCCTGCGGCCGCGCGCGCTCCCCGACGCCCGGGCCCGCGGC
CACGACGTGCGCTTCGCGGAGTTCCTGGCCTACCTGCTGGACCCGCGCACGCGGCGTGAG
GAGCCCTTCAACGAGCACTGGGAGCGCGCGCACGCGCTCTGCCACCCGTGTCGCCTCCGC
TACGACGTCGTGGGCAAGTTCGAGACGCTGGCGGAGGACGCGGCCTTCGTGCTGGGCCTG
GCGGGCGCATCCGACCTGAGCTTCCCTGGGCCGCCGCGGCCCCGGGGAGCCGCCGCCTCC
CGCGACCTGGCAGCGCGCCTCTTCCGGGACATCAGCCCCTTCTACCAGCGGCGCCTCTTC
GACCTCTACAAGATGGACTTCCTGCTTTTCAACTACTCCGCCCCCTCCTACCTGCGGCTG
CTCTAG
|
Protein Properties |
Number of Residues
| 341 |
Molecular Weight
| 38919.34 |
Theoretical pI
| 10.543 |
Pfam Domain Function
|
|
Signals
|
Not Available
|
Transmembrane Regions
|
Not Available
|
Protein Sequence
|
>Carbohydrate sulfotransferase 13
MGRRCCRRRVLAAACLGAALLLLCAAPRSLRPAFGNRALGSSWLGGEKRSPLQKLYDLDQ
DPRSTLAKVHRQRRDLLNSACSRHSRRQRLLQPEDLRHVLVDDAHGLLYCYVPKVACTNW
KRVLLALSGQARGDPRAISAQEAHAPGRLPSLADFSPAEINRRLRAYLAFLFVREPFERL
ASAYRNKLARPYSAAFQRRYGARIVQRLRPRALPDARARGHDVRFAEFLAYLLDPRTRRE
EPFNEHWERAHALCHPCRLRYDVVGKFETLAEDAAFVLGLAGASDLSFPGPPRPRGAAAS
RDLAARLFRDISPFYQRRLFDLYKMDFLLFNYSAPSYLRLL
|
External Links |
GenBank ID Protein
| 22651777 |
UniProtKB/Swiss-Prot ID
| Q8NET6 |
UniProtKB/Swiss-Prot Entry Name
| CHSTD_HUMAN |
PDB IDs
|
Not Available |
GenBank Gene ID
| AY120869 |
GeneCard ID
| CHST13 |
GenAtlas ID
| CHST13 |
HGNC ID
| HGNC:21755 |
References |
General References
| - Kang HG, Evers MR, Xia G, Baenziger JU, Schachner M: Molecular cloning and characterization of chondroitin-4-O-sulfotransferase-3. A novel member of the HNK-1 family of sulfotransferases. J Biol Chem. 2002 Sep 20;277(38):34766-72. Epub 2002 Jun 21. [PubMed:12080076 ]
|