Version 5.4
Mus musculus Protein: Ndst3
Summary
InnateDB Protein IDBP-536887.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ndst3
Protein Name N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 3
Synonyms 4921531K01Rik; 4930511P15Rik; N-HSST 3; NDST-3;
Species Mus musculus
Ensembl Protein ENSMUSP00000118796
InnateDB Gene IDBG-192318 (Ndst3)
Protein Structure
UniProt Annotation
Function Essential bifunctional enzyme that catalyzes both the N- deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low sulfotransferase activity. {ECO:0000269PubMed:11087757}.
Subcellular Localization Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Disease Associations
Tissue Specificity Strongly expressed strongly in brain. Expressed at high level at embryonic day 11 compared to other stages of development. Weakly expressed in adult heart, kidney, muscle, endothelial cells and testis but not in other tissues. {ECO:0000269PubMed:11087757, ECO:0000269PubMed:16056228}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0008146 sulfotransferase activity
GO:0015016 [heparan sulfate]-glucosamine N-sulfotransferase activity
GO:0016787 hydrolase activity
GO:0019213 deacetylase activity
Biological Process
GO:0015012 heparan sulfate proteoglycan biosynthetic process
GO:0030210 heparin biosynthetic process
Cellular Component
GO:0000139 Golgi membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1932544
InterPro IPR021930 Heparan sulphate-N-deacetylase
IPR027417 P-loop containing nucleoside triphosphate hydrolase
PFAM PF12062
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9EQH7
PhosphoSite PhosphoSite-Q9EQH7
TrEMBL
UniProt Splice Variant
Entrez Gene 83398
UniGene Mm.443908
RefSeq XP_006502435
MGI ID
MGI Symbol Ndst3
OMIM
CCDS
HPRD
IMGT
EMBL AF221095 AK015768 AK141945 BC079622
GenPept AAG34793 AAH79622 BAB29967 BAE24894

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca