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Q9EQW8 (NDST4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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. Heparan sulfate N-deacetylase 4
    EC=3.-.-.-
  2. 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 › Mus

Protein attributes

Sequence length872 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

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 – 3421Helical; Signal-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

Experimental info

Sequence conflict6811A → T in BAB18517. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9EQW8 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: C56980F256C757E4

FASTA872100,655
        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 ASLVPKAKII 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

References

« Hide 'large scale' 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.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB036838 mRNA. Translation: BAB18517.1.
AC111141 Genomic DNA. No translation available.
AC140797 Genomic DNA. No translation available.
AC164153 Genomic DNA. No translation available.
IPIIPI00111641.
RefSeqNP_072087.2. NM_022565.2.
UniGeneMm.444289.

3D structure databases

ProteinModelPortalQ9EQW8.
SMRQ9EQW8. Positions 569-869.
ModBaseSearch...

Proteomic databases

PRIDEQ9EQW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000143461; ENSMUSP00000121985; ENSMUSG00000027971.
GeneID64580.
KEGGmmu:64580.

Organism-specific databases

CTD64579.
MGIMGI:1932545. Ndst4.

Phylogenomic databases

eggNOGmaNOG08993.
GeneTreeENSGT00560000076777.
HOGENOMHBG356867.
HOVERGENHBG082011.
InParanoidQ9EQW8.
OrthoDBEOG48KR9J.

Enzyme and pathway databases

BRENDA2.8.2.8. 3474.

Gene expression databases

ArrayExpressQ9EQW8.
GenevestigatorQ9EQW8.
GermOnlineENSMUSG00000027971. Mus musculus.

Family and domain databases

InterProIPR021930. Heparan_SO4_deacetylase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
KOK02579.
PfamPF12062. HSNSD. 1 hit.
PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameNDST4_MOUSE
AccessionPrimary (citable) accession number: Q9EQW8
Secondary accession number(s): D3Z1R7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

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