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Protein

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4

Gene

Ndst4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 low deacetylase activity but high sulfotransferase activity.1 Publication

Catalytic activityi

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

Pathwayi: heparan sulfate biosynthesis

This protein is involved in the pathway heparan sulfate biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway heparan sulfate biosynthesis and in Glycan metabolism.

Pathwayi: heparin biosynthesis

This protein is involved in the pathway heparin biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway heparin biosynthesis and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei604 – 6041For sulfotransferase activityBy similarity
Binding sitei702 – 7021PAPSBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi604 – 6085PAPSBy similarity
Nucleotide bindingi823 – 8275PAPSBy similarity

GO - Molecular functioni

  • [heparan sulfate]-glucosamine N-sulfotransferase activity Source: UniProtKB-EC
  • deacetylase activity Source: MGI
  • sulfotransferase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Enzyme and pathway databases

BRENDAi2.8.2.8. 3474.
UniPathwayiUPA00756.
UPA00862.

Names & Taxonomyi

Protein namesi
Recommended 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:
Heparan sulfate N-deacetylase 4 (EC:3.-.-.-)
Heparan sulfate N-sulfotransferase 4 (EC:2.8.2.-)
Gene namesi
Name:Ndst4
Synonyms:Hsst4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1932545. Ndst4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence analysisAdd
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini35 – 872838LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 872872Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4PRO_0000225662Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence analysis
Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence analysis
Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence analysis
Glycosylationi657 – 6571N-linked (GlcNAc...)Sequence analysis
Glycosylationi793 – 7931N-linked (GlcNAc...)Sequence analysis
Disulfide bondi808 ↔ 818By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9EQW8.
PRIDEiQ9EQW8.

PTM databases

PhosphoSiteiQ9EQW8.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9EQW8.
ExpressionAtlasiQ9EQW8. baseline and differential.
GenevisibleiQ9EQW8. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi211087. 1 interaction.
STRINGi10090.ENSMUSP00000133341.

Structurei

3D structure databases

ProteinModelPortaliQ9EQW8.
SMRiQ9EQW8. Positions 569-869.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 588553Heparan sulfate N-deacetylase 4Add
BLAST
Regioni589 – 872284Heparan sulfate N-sulfotransferase 4Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3703. Eukaryota.
ENOG410XQN4. LUCA.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000008010.
HOVERGENiHBG082011.
InParanoidiQ9EQW8.
KOiK02579.
OMAiYPPMDQE.
OrthoDBiEOG7FXZXJ.
PhylomeDBiQ9EQW8.
TreeFamiTF313193.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR021930. Heparan_SO4_deacetylase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF12062. HSNSD. 1 hit.
PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9EQW8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLILKFRRS FRTLIVLLAT FCLVSILISA YFLYSGYKQE MTLIETTAEA
60 70 80 90 100
ECADIKDLPY RSIELRTIKP IDTSKTDPTV LLFVESQYSQ LGQDIIAILE
110 120 130 140 150
SSRFQYQMVI APGKGDIPPL TDSGKGKYTL IIYENILKYV SMDSWNRELL
160 170 180 190 200
EKYCIEYSVS IIGFHKANEN SLPTTQLKGF PLNLFNNVAL KDCSVNPQSP
210 220 230 240 250
LLHITKGPKV EKGPLPGEDW TIFQYNHSTY QPVLLTELQS EKSLSFLSSQ
260 270 280 290 300
TLYATIIQDL GLHDGIQRVL FGNNLNFWLH KLIFIDAISF LSGKRLTLSL
310 320 330 340 350
DRYILVDIDD IFVGKEGTRM NVKDVKALLE TQNLLRTQVA NFTFNLGFSG
360 370 380 390 400
KFYHTGTEEE DEGDDLLLRS VDEFWWFPHM WSHMQPHLFH NESSLVEQMI
410 420 430 440 450
LNKEFALEHG IPINLGYAVA PHHSGVYPVH IQLYAAWKKV WGIQVTSTEE
460 470 480 490 500
YPHLKPARYR KGFIHNSIMV LPRQTCGLFT HTIFYKEYPG GPQELDKSIK
510 520 530 540 550
GGELFLTILL NPISIFMTHL SNYGNDRLGL YTFVNLANFV HSWTNLKLQT
560 570 580 590 600
LPPVQLAHKY FELFPEQKDP LWQNPCDDKR HKDIWSREKT CDHLPKFLVI
610 620 630 640 650
GPQKTGTTAL YLFLLMHPSI ISNLPSPKTF EEVQFFNGNN YHKGIEWYMD
660 670 680 690 700
FFPTPSNITS DFLFEKSANY FHSEEAPKRA ASLVPKAKII TILIDPSDRA
710 720 730 740 750
YSWYQHQRSH EDPAALRFNF YEVITTGHWA PPDLKTLQRR CLVPGWYAVH
760 770 780 790 800
IERWLAYFST SQLLIIDGQQ LRSDPATVMD EVQKFLGVTP HYNYSEALTF
810 820 830 840 850
DPQKGFWCQL LEGGKTKCLG KSKGRKYPPM DSESRTFLSS YYRDHNVELS
860 870
KLLHRLGQPL PSWLRQELQK VR
Length:872
Mass (Da):100,655
Last modified:July 27, 2011 - v2
Checksum:iC56980F256C757E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti681 – 6811A → T in BAB18517 (PubMed:11087757).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB036838 mRNA. Translation: BAB18517.1.
AC111141 Genomic DNA. No translation available.
AC140797 Genomic DNA. No translation available.
AC164153 Genomic DNA. No translation available.
CCDSiCCDS17820.1.
RefSeqiNP_072087.2. NM_022565.2.
UniGeneiMm.444289.
Mm.483253.

Genome annotation databases

EnsembliENSMUST00000173932; ENSMUSP00000133341; ENSMUSG00000027971.
GeneIDi64580.
KEGGimmu:64580.
UCSCiuc008rfv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB036838 mRNA. Translation: BAB18517.1.
AC111141 Genomic DNA. No translation available.
AC140797 Genomic DNA. No translation available.
AC164153 Genomic DNA. No translation available.
CCDSiCCDS17820.1.
RefSeqiNP_072087.2. NM_022565.2.
UniGeneiMm.444289.
Mm.483253.

3D structure databases

ProteinModelPortaliQ9EQW8.
SMRiQ9EQW8. Positions 569-869.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211087. 1 interaction.
STRINGi10090.ENSMUSP00000133341.

PTM databases

PhosphoSiteiQ9EQW8.

Proteomic databases

PaxDbiQ9EQW8.
PRIDEiQ9EQW8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000173932; ENSMUSP00000133341; ENSMUSG00000027971.
GeneIDi64580.
KEGGimmu:64580.
UCSCiuc008rfv.2. mouse.

Organism-specific databases

CTDi64579.
MGIiMGI:1932545. Ndst4.

Phylogenomic databases

eggNOGiKOG3703. Eukaryota.
ENOG410XQN4. LUCA.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000008010.
HOVERGENiHBG082011.
InParanoidiQ9EQW8.
KOiK02579.
OMAiYPPMDQE.
OrthoDBiEOG7FXZXJ.
PhylomeDBiQ9EQW8.
TreeFamiTF313193.

Enzyme and pathway databases

UniPathwayiUPA00756.
UPA00862.
BRENDAi2.8.2.8. 3474.

Miscellaneous databases

NextBioi320119.
PROiQ9EQW8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQW8.
ExpressionAtlasiQ9EQW8. baseline and differential.
GenevisibleiQ9EQW8. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR021930. Heparan_SO4_deacetylase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF12062. HSNSD. 1 hit.
PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiNDST4_MOUSE
AccessioniPrimary (citable) accession number: Q9EQW8
Secondary accession number(s): D3Z1R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: July 27, 2011
Last modified: March 16, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.