Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9EQW8 (NDST4_MOUSE)

Last modified October 13, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4
    EC=2.8.2.8
Alternative name(s):
    Glucosaminyl N-deacetylase/N-sulfotransferase 4
      Short name=NDST-4
    N-heparan sulfate sulfotransferase 4
      Short name=N-HSST 4
Including the following 2 domains:
    1- Recommended name:
            Heparan sulfate N-deacetylase 4
              EC=3.-.-.-
    2- Recommended name:
            Heparan sulfate N-sulfotransferase 4
              EC=2.8.2.-
Gene names
Name: Ndst4
Synonyms: Hsst4
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length872 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

Hide | Top

General annotation (Comments)

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 dissacharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has low deacetylase activity but high sulfotransferase activity. Ref.1

Catalytic activity

3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine.

Pathway

Glycan metabolism; heparan sulfate biosynthesis.

Glycan metabolism; heparin biosynthesis.

Subunit structure

Monomer By similarity.

Subcellular location

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

Tissue specificity

Expressed at low level in brain and throughout embryogenesis. Not expressed in other tissues. Ref.1

Miscellaneous

The presence of 4 different heparan sulfate N-deacetylase/N-sulfotransferase enzymes in mammals, as well as differences in their enzyme activity suggest that some initiate heparan sulfate modification/sulfation reactions, whereas other later on fill in or extend already modified heparan sulfate sequences.

Sequence similarities

Belongs to the sulfotransferase 1 family. NDST subfamily.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 872872Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4
PRO_0000225662

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Signal-anchor for type II membrane protein Potential
Topological domain35 – 872838Lumenal Potential
Nucleotide binding604 – 6085PAPS By similarity
Nucleotide binding823 – 8275PAPS By similarity
Region36 – 588553Heparan sulfate N-deacetylase 4
Region589 – 872284Heparan sulfate N-sulfotransferase 4

Sites

Active site6041For sulfotransferase activity By similarity
Binding site7021PAPS By similarity

Amino acid modifications

Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Potential
Glycosylation6571N-linked (GlcNAc...) Potential
Glycosylation7931N-linked (GlcNAc...) Potential
Disulfide bond808 ↔ 818 By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q9EQW8-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9815E1FF3BB74B9D

FASTA872100,685
        10         20         30         40         50         60 
MNLILKFRRS FRTLIVLLAT FCLVSILISA YFLYSGYKQE MTLIETTAEA ECADIKDLPY 

        70         80         90        100        110        120 
RSIELRTIKP IDTSKTDPTV LLFVESQYSQ LGQDIIAILE SSRFQYQMVI APGKGDIPPL 

       130        140        150        160        170        180 
TDSGKGKYTL IIYENILKYV SMDSWNRELL EKYCIEYSVS IIGFHKANEN SLPTTQLKGF 

       190        200        210        220        230        240 
PLNLFNNVAL KDCSVNPQSP LLHITKGPKV EKGPLPGEDW TIFQYNHSTY QPVLLTELQS 

       250        260        270        280        290        300 
EKSLSFLSSQ TLYATIIQDL GLHDGIQRVL FGNNLNFWLH KLIFIDAISF LSGKRLTLSL 

       310        320        330        340        350        360 
DRYILVDIDD IFVGKEGTRM NVKDVKALLE TQNLLRTQVA NFTFNLGFSG KFYHTGTEEE 

       370        380        390        400        410        420 
DEGDDLLLRS VDEFWWFPHM WSHMQPHLFH NESSLVEQMI LNKEFALEHG IPINLGYAVA 

       430        440        450        460        470        480 
PHHSGVYPVH IQLYAAWKKV WGIQVTSTEE YPHLKPARYR KGFIHNSIMV LPRQTCGLFT 

       490        500        510        520        530        540 
HTIFYKEYPG GPQELDKSIK GGELFLTILL NPISIFMTHL SNYGNDRLGL YTFVNLANFV 

       550        560        570        580        590        600 
HSWTNLKLQT LPPVQLAHKY FELFPEQKDP LWQNPCDDKR HKDIWSREKT CDHLPKFLVI 

       610        620        630        640        650        660 
GPQKTGTTAL YLFLLMHPSI ISNLPSPKTF EEVQFFNGNN YHKGIEWYMD FFPTPSNITS 

       670        680        690        700        710        720 
DFLFEKSANY FHSEEAPKRA TSLVPKAKII TILIDPSDRA YSWYQHQRSH EDPAALRFNF 

       730        740        750        760        770        780 
YEVITTGHWA PPDLKTLQRR CLVPGWYAVH IERWLAYFST SQLLIIDGQQ LRSDPATVMD 

       790        800        810        820        830        840 
EVQKFLGVTP HYNYSEALTF DPQKGFWCQL LEGGKTKCLG KSKGRKYPPM DSESRTFLSS 

       850        860        870 
YYRDHNVELS KLLHRLGQPL PSWLRQELQK VR

« Hide

Hide | Top

References

[1]"Multiple isozymes of heparan sulfate/heparin GlcNAc N-deacetylase/GlcN N-sulfotransferase. Structure and activity of the fourth member, NDST4."
Aikawa J., Grobe K., Tsujimoto M., Esko J.D.
J. Biol. Chem. 276:5876-5882(2001) [PubMed: 11087757] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Brain.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

AB036838 mRNA. Translation: BAB18517.1.
IPIIPI00111641.
UniGeneMm.444289

3D structure databases

HSSPHSSP built from PDB template 1NST based on UniProtKB P52848.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9EQW8.

Proteomic databases

PRIDEQ9EQW8.

Genome annotation databases

EnsemblENSMUST00000029596; ENSMUSP00000029596; ENSMUSG00000027971; Mus musculus. [Genome view]
UCSCuc008rfw.2. mouse.

Organism-specific databases

MGIMGI:1932545. Ndst4.

Phylogenomic databases

HOGENOMQ9EQW8.
HOVERGENQ9EQW8.

Enzyme and pathway databases

BRENDA2.8.2.8. 244.

Gene expression databases

ArrayExpressQ9EQW8.
BgeeQ9EQW8.
GenevestigatorQ9EQW8.
GermOnlineENSMUSG00000027971. Mus musculus.

Family and domain databases

InterProIPR000863. Sulfotransferase.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Hide | Top

Entry information

Entry nameNDST4_MOUSE
AccessionPrimary (citable) accession number: Q9EQW8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 1, 2001
Last modified: October 13, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents