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Identification
HMDB Protein ID HMDBP02568
Secondary Accession Numbers
  • 8067
Name Carbohydrate sulfotransferase 14
Synonyms
  1. D4ST-1
  2. Dermatan 4-sulfotransferase 1
  3. hD4ST1
Gene Name CHST14
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 dermatan sulfate. Plays a pivotal role in the formation of 4-0-sulfated IdoA blocks in dermatan sulfate. Transfers sulfate to the C-4 hydroxyl of beta1,4-linked GalNAc that is substituted with an alpha-linked iduronic acid (IdoUA) at the C-3 hydroxyl. Transfers sulfate more efficiently to GalNAc residues in -IdoUA-GalNAc-IdoUA- than in -GlcUA-GalNAc-GlcUA-sequences. Has preference for partially desulfated dermatan sulfate. Addition of sulfate to GalNAc may occur immediately after epimerization of GlcUA to IdoUA. GlcUA to IdoUA. Appears to have an important role in the formation of the cerbellar neural network during postnatal brain development.
Pathways
  • Glycosaminoglycan biosynthesis - chondroitin sulfate / dermatan sulfate
Reactions
Phosphoadenosine phosphosulfate + [dermatan]-N-acetyl-D-galactosamine → Adenosine 3',5'-diphosphate + [dermatan]- 4-O-sulfo-N-acetyl-D-galactosamine details
GO Classification
Biological Process
carbohydrate biosynthetic process
dermatan sulfate biosynthetic process
carbohydrate metabolic process
chondroitin sulfate 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
N-acetylgalactosamine 4-O-sulfotransferase activity
phosphate ion binding
Process
metabolic process
primary metabolic process
carbohydrate metabolic process
carbohydrate biosynthetic process
Cellular Location
  1. Golgi apparatus membrane
  2. Single-pass type II membrane protein
Gene Properties
Chromosome Location 15
Locus 15q15.1
SNPs CHST14
Gene Sequence
>1131 bp
ATGTTCCCCCGCCCGCTGACCCCGCTGGCGGCCCCAAATGGCGCCGAGCCCCTGGGCCGG
GCGCTGAGGCGGGCCCCTCTGGGCAGGGCCCGGGCGGGGCTGGGTGGGCCGCCCCTGCTG
CTGCCGTCCATGCTGATGTTTGCGGTGATCGTGGCCTCCAGCGGGCTGCTGCTCATGATC
GAGCGGGGCATCCTGGCCGAGATGAAGCCCCTGCCCCTGCACCCGCCCGGCCGCGAGGGC
ACAGCCTGGCGCGGGAAAGCCCCCAAGCCTGGGGGCCTGTCCCTCAGGGCTGGGGACGCG
GACTTGCAAGTGCGGCAGGACGTCCGGAACAGGACCCTGCGGGCGGTGTGCGGACAGCCA
GGCATGCCCCGGGACCCCTGGGACTTGCCGGTGGGGCAGCGGCGCACCCTGCTGCGCCAC
ATCCTCGTAAGTGACCGTTACCGCTTCCTCTACTGCTACGTCCCCAAGGTGGCCTGCTCT
AACTGGAAGCGGGTGATGAAGGTGCTGGCAGGCGTCCTGGACAGCGTGGACGTCCGCCTC
AAGATGGACCACCGCAGTGACCTGGTGTTCCTGGCCGACCTGCGGCCTGAGGAGATTCGC
TACCGCCTGCAGCACTACTTTAAGTTCCTGTTTGTGCGGGAGCCCTTGGAACGCCTCCTC
TCTGCCTACCGCAACAAGTTTGGCGAGATCCGAGAGTACCAGCAACGCTATGGGGCTGAG
ATAGTGAGGCGGTACAGGGCTGGAGCGGGGCCCAGCCCTGCAGGCGACGATGTCACATTC
CCCGAGTTCCTGAGATACCTGGTGGATGAGGACCCTGAGCGCATGAATGAGCATTGGATG
CCCGTGTACCACCTGTGCCAGCCTTGTGCCGTGCACTATGACTTTGTGGGCTCCTATGAG
AGGCTGGAGGCTGATGCAAATCAGGTGCTGGAGTGGGTACGGGCACCACCTCACGTCCGA
TTTCCAGCTCGCCAGGCCTGGTACCGGCCAGCCAGCCCCGAAAGCCTGCATTACCACTTG
TGCAGTGCCCCCCGGGCCCTGCTGCAGGATGTGCTGCCTAAGTATATCCTGGACTTCTCC
CTCTTTGCCTACCCACTGCCTAATGTCACCAAGGAGGCGTGTCAGCAGTGA
Protein Properties
Number of Residues 376
Molecular Weight 42996.535
Theoretical pI 9.486
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Carbohydrate sulfotransferase 14
MFPRPLTPLAAPNGAEPLGRALRRAPLGRARAGLGGPPLLLPSMLMFAVIVASSGLLLMI
ERGILAEMKPLPLHPPGREGTAWRGKAPKPGGLSLRAGDADLQVRQDVRNRTLRAVCGQP
GMPRDPWDLPVGQRRTLLRHILVSDRYRFLYCYVPKVACSNWKRVMKVLAGVLDSVDVRL
KMDHRSDLVFLADLRPEEIRYRLQHYFKFLFVREPLERLLSAYRNKFGEIREYQQRYGAE
IVRRYRAGAGPSPAGDDVTFPEFLRYLVDEDPERMNEHWMPVYHLCQPCAVHYDFVGSYE
RLEADANQVLEWVRAPPHVRFPARQAWYRPASPESLHYHLCSAPRALLQDVLPKYILDFS
LFAYPLPNVTKEACQQ
GenBank ID Protein 18369804
UniProtKB/Swiss-Prot ID Q8NCH0
UniProtKB/Swiss-Prot Entry Name CHSTE_HUMAN
PDB IDs Not Available
GenBank Gene ID AB066595
GeneCard ID CHST14
GenAtlas ID CHST14
HGNC ID HGNC:24464
References
General References
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  4. Mikami T, Mizumoto S, Kago N, Kitagawa H, Sugahara K: Specificities of three distinct human chondroitin/dermatan N-acetylgalactosamine 4-O-sulfotransferases demonstrated using partially desulfated dermatan sulfate as an acceptor: implication of differential roles in dermatan sulfate biosynthesis. J Biol Chem. 2003 Sep 19;278(38):36115-27. Epub 2003 Jul 7. [PubMed:12847091 ]
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