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Q9H3R1 (NDST4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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 By similarity.

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.

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_0000225661

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

Natural variations

Natural variant121R → Q.
Corresponds to variant rs35181627 [ dbSNP | Ensembl ].
VAR_061890

Sequences

Sequence LengthMass (Da)Tools
Q9H3R1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9C4E2DD1F98EA859

FASTA872100,716
        10         20         30         40         50         60 
MNLIVKLRRS FRTLIVLLAT FCLVSIVISA YFLYSGYKQE MTLIETTAEA ECTDIKILPY 

        70         80         90        100        110        120 
RSMELKTVKP IDTSKTDPTV LLFVESQYSQ LGQDIIAILE SSRFQYHMVI APGKGDIPPL 

       130        140        150        160        170        180 
TDNGKGKYTL VIYENILKYV SMDSWNRELL EKYCVEYSVS IIGFHKANEN SLPSTQLKGF 

       190        200        210        220        230        240 
PLNLFNNLAL KDCFVNPQSP LLHITKAPKV EKGPLPGEDW TIFQYNHSTY QPVLLTELQT 

       250        260        270        280        290        300 
EKSLSSLSSK TLFATVIQDL 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 IPINMGYAVA 

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

       490        500        510        520        530        540 
HTIFYKEYPG GPQELDKSIR GGELFLTILL NPISIFMTHL SNYGNDRLGL YTFVNLVNFV 

       550        560        570        580        590        600 
QSWTNLKLQT LPPVQLAHQY FELFPEQKDP LWQNPCDDKR HKDIWSREKT CDHLPKFLVI 

       610        620        630        640        650        660 
GPQKTGTTAL YLFLLMHPSI ISNLPSPKTF EEVQFFNGNN YHKGIDWYMD FFPTPSNTTS 

       670        680        690        700        710        720 
DFLFEKSANY FHSEEAPRRA ASLVPKAKII TILIDPSDRA YSWYQHQRSH EDPAALRFNF 

       730        740        750        760        770        780 
YEVISTGHWA PSDLKTLQRR CLVPGWYAVH IERWLTYFAT SQLLIIDGQQ LRSDPATVMD 

       790        800        810        820        830        840 
EVQKFLGVTP RYNYSEALTF DPQKGFWCQL LEGGKTKCLG KSKGRKYPPM DPESRTFLSN 

       850        860        870 
YYRDHNVELS KLLHRLGQPL PSWLRQELQK VR

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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].
Tissue: Fetal brain.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB036429 mRNA. Translation: BAB18535.1.
IPIIPI00021733.
RefSeqNP_072091.1. NM_022569.1.
UniGeneHs.591700.

3D structure databases

ProteinModelPortalQ9H3R1.
SMRQ9H3R1. Positions 569-869.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9H3R1.

Polymorphism databases

DMDM74718249.

Proteomic databases

PRIDEQ9H3R1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264363; ENSP00000264363; ENSG00000138653.
GeneID64579.
KEGGhsa:64579.
UCSCuc003ibu.1. human.

Organism-specific databases

CTD64579.
GeneCardsGC04M115748.
H-InvDBHIX0031346.
HGNCHGNC:20779. NDST4.
HPAHPA011129.
neXtProtNX_Q9H3R1.
PharmGKBPA134875549.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14211.
GeneTreeENSGT00560000076777.
HOGENOMHBG356867.
HOVERGENHBG082011.
InParanoidQ9H3R1.
OMAKGFPLNL.
OrthoDBEOG48KR9J.
PhylomeDBQ9H3R1.

Enzyme and pathway databases

BioCycMetaCyc:HS06527-MONOMER.
BRENDA2.8.2.8. 2681.

Gene expression databases

ArrayExpressQ9H3R1.
BgeeQ9H3R1.
CleanExHS_NDST4.
GenevestigatorQ9H3R1.
GermOnlineENSG00000138653. Homo sapiens.

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

NextBio66513.

Entry information

Entry nameNDST4_HUMAN
AccessionPrimary (citable) accession number: Q9H3R1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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