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Q966W3 (NDST_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 61. 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 1
EC=2.8.2.8
Alternative name(s):
Glucosaminyl N-deacetylase/N-sulfotransferase 1

Including the following 2 domains:

  1. Heparan sulfate N-deacetylase 1
    EC=3.-.-.-
  2. Heparan sulfate N-sulfotransferase 1
    EC=2.8.2.-
Gene names
Name:hst-1
ORF Names:F08B4.6
OrganismCaenorhabditis elegans
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length852 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 Probable. Ref.3

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

Present in some specific neurons in head and tail regions and muscles. Ref.3

Sequence similarities

Belongs to the sulfotransferase 1 family. NDST subfamily.

Sequence caution

The sequence CCD67652.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 852852Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
PRO_0000225664

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain35 – 852818Lumenal Potential
Nucleotide binding592 – 5965PAPS By similarity
Nucleotide binding803 – 8075PAPS By similarity
Region34 – 574541Heparan sulfate N-deacetylase 1
Region575 – 852278Heparan sulfate N-sulfotransferase 1

Sites

Active site5921For sulfotransferase activity By similarity
Binding site6861PAPS By similarity

Amino acid modifications

Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation2611N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation3771N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation5761N-linked (GlcNAc...) Potential
Glycosylation6071N-linked (GlcNAc...) Potential
Glycosylation7121N-linked (GlcNAc...) Potential
Disulfide bond789 ↔ 798 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q966W3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1DD390CCDA5EDE21

FASTA85299,061
        10         20         30         40         50         60 
MIITPYLNRK ITRPLKWILA LIFLYLIYIC LFSNNSKPPK PRKKPKLVEN YTCPFARTEG 

        70         80         90        100        110        120 
TASENLFFHT NNGTDARILV ILDSLFSRHG KTIIQILNSQ KLQFKAEAVS KNLPVLTTSR 

       130        140        150        160        170        180 
RGRYSLIIIE NYYKYLNMAQ WNRQLLDKYC KEYRVPMFSF MSSKPNDQLK RIKIKGSSLW 

       190        200        210        220        230        240 
MWQNQRIQRL AVTPSIIHRI SKIGNYRQFS SSDPADWILF ETSEKFESVL SGTVKSGYER 

       250        260        270        280        290        300 
AVVVRDKGLE DGVERIIFGR NLTDFQVKIT FLDALWWAMG NQKSFTLDRF VQVDIDDVFV 

       310        320        330        340        350        360 
GAQGTRIVEE DVRKLISTQK EFRNYVQNFT FMLGFSGSYF RNGDDLEDRG DEFLVENAEK 

       370        380        390        400        410        420 
FVWFPHMWRH NHAHEHNFTY LEAIMAQNKL FAQNMHLPVD YPYAIAPQHD GVFPVHEQLF 

       430        440        450        460        470        480 
RAWRKVWNVS VTATEEYPHF KPATARKGFI HAGIHVLPRQ TCGLYTHTQL FDEYPEGFDK 

       490        500        510        520        530        540 
VQKSIEGGDL FFTILLNPIS IFMTHQQNYA YDRLALYTFE NLFRFIKCWT NIKLKWQDPL 

       550        560        570        580        590        600 
TSSQLYFQKF PDERTPLWTN PCTDPRHHAI LPPSINCTKK SLPDLLIIGP QKTGSTALAS 

       610        620        630        640        650        660 
FLSLHPNTSQ NTPVPGSFEE VQFFGGQNYL KGVEWYMSNF PSSSTVTFEK SATYFDNPSA 

       670        680        690        700        710        720 
PKQAASLVPH AKIVIILQNP AQRAYSWFQH ILAHEDPVAI TAGSLEVILD SNSTSSKKVR 

       730        740        750        760        770        780 
QRCISGGRYV HHLTKWLEHF SLQQMIFVDS DELKMKPPTV LNSLSKWLDL PEFPFETYIR 

       790        800        810        820        830        840 
YSPSKGFHCR LLDGKTKCLG ESKGRKYPEM PENLRRKLDK IFSLDNSALY KFLRKNRLKI 

       850 
PTWLEESVRI RA

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of N-deacetylase/N-sulfotransferase in worm."
Aikawa J.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Structure and function of heparan sulfate/heparin N-deacetylase/ N-sulfotransferase in worm."
Aikawa J.
(In) Proceedings of the 14th international C. elegans meeting, pp.345-345, Los Angeles (2003)
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB037941 mRNA. Translation: BAB61756.1.
AB037942 mRNA. Translation: BAB61757.1.
AB037943 mRNA. Translation: BAB61758.1.
AB038044 mRNA. Translation: BAB62394.1.
FO080903 Genomic DNA. Translation: CCD67652.1. Different initiation.
PIRT29486.
RefSeqNP_501491.3. NM_069090.3.
UniGeneCel.18357.

3D structure databases

ProteinModelPortalQ966W3.
SMRQ966W3. Positions 555-849.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ966W3.

Proteomic databases

PRIDEQ966W3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID177675.
KEGGcel:F08B4.6.
NMPDRfig|6239.3.peg.14334.
UCSCF08B4.6. c. elegans.

Organism-specific databases

CTD177675.
WormBaseF08B4.6; CE33047; WBGene00002028; hst-1.

Phylogenomic databases

eggNOGmeNOG04445.
GeneTreeEMGT00050000001485.
HOGENOMHBG356867.
InParanoidQ966W3.

Gene expression databases

ArrayExpressQ966W3.

Family and domain databases

InterProIPR021930. Heparan_SO4_deacetylase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
KOK01025.
PfamPF12062. HSNSD. 1 hit.
PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNDST_CAEEL
AccessionPrimary (citable) accession number: Q966W3
Secondary accession number(s): Q19197 expand/collapse secondary AC list , Q966W4, Q966W5, Q966W6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: December 1, 2001
Last modified: December 14, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents