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O95803 (NDST3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3

EC=2.8.2.8
Alternative name(s):
Glucosaminyl N-deacetylase/N-sulfotransferase 3
Short name=NDST-3
Short name=hNDST-3
N-heparan sulfate sulfotransferase 3
Short name=N-HSST 3

Including the following 2 domains:

  1. Heparan sulfate N-deacetylase 3
    EC=3.-.-.-
  2. Heparan sulfate N-sulfotransferase 3
    EC=2.8.2.-
Gene names
Name:NDST3
Synonyms:HSST3
ORF Names:UNQ2544/PRO4998
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length873 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 disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low 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 in brain, kidney, liver, fetal and adult lung, adult pancreas, placenta, fetal spleen and fetal thymus. Not detected in adult/ fetal heart and skeletal muscle. 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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95803-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O95803-2)

The sequence of this isoform differs from the canonical sequence as follows:
     328-385: ALLDTQNLLR...WWFPHMWSHM → VRLYFLKFQS...NQLRRLCISI
     386-873: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 873873Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3
PRO_0000225659

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Helical; Signal-anchor for type II membrane protein; Potential
Topological domain35 – 873839Lumenal Potential
Nucleotide binding605 – 6095PAPS By similarity
Nucleotide binding824 – 8285PAPS By similarity
Region36 – 589554Heparan sulfate N-deacetylase 3
Region590 – 873284Heparan sulfate N-sulfotransferase 3

Sites

Active site6051For sulfotransferase activity By similarity
Binding site7031PAPS By similarity

Amino acid modifications

Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation2261N-linked (GlcNAc...) Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation6581N-linked (GlcNAc...) Potential
Glycosylation7941N-linked (GlcNAc...) Potential
Disulfide bond809 ↔ 819 By similarity

Natural variations

Alternative sequence328 – 38558ALLDT…MWSHM → VRLYFLKFQSSVHLPAGIQL SQFVLQLGYPGHGIYWESLG NLGLSLTLNQLRRLCISI in isoform 2.
VSP_017405
Alternative sequence386 – 873488Missing in isoform 2.
VSP_017406
Natural variant2641H → Q in a colorectal cancer sample; somatic mutation. Ref.6
VAR_036131

Experimental info

Sequence conflict8 – 1710HRHFQRTVIL → STEQLSKEPVISW in AAD46061. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 4DDE39257CAC0D36

FASTA873100,902
        10         20         30         40         50         60 
MSFIMKLHRH FQRTVILLAT FCMVSIIISA YYLYSGYKQE NELSETASEV DCGDLQHLPY 

        70         80         90        100        110        120 
QLMEVKAMKL FDASRTDPTV LVFVESQYSS LGQDIIMILE SSRFQYHIEI APGKGDLPVL 

       130        140        150        160        170        180 
IDKMKGKYIL IIYENILKYI NMDSWNRSLL DKYCVEYGVG VIGFHKTSEK SVQSFQLKGF 

       190        200        210        220        230        240 
PFSIYGNLAV KDCCINPHSP LIRVTKSSKL EKGSLPGTDW TVFQINHSAY QPVIFAKVKT 

       250        260        270        280        290        300 
PENLSPSISK GAFYATIIHD LGLHDGIQRV LFGNNLNFWL HKLIFIDAIS FLSGKRLTLS 

       310        320        330        340        350        360 
LDRYILVDID DIFVGKEGTR MNTNDVKALL DTQNLLRAQI TNFTFNLGFS GKFYHTGTEE 

       370        380        390        400        410        420 
EDEGDDCLLG SVDEFWWFPH MWSHMQPHLF HNESSLVEQM ILNKKFALEH GIPTDMGYAV 

       430        440        450        460        470        480 
APHHSGVYPV HVQLYEAWKK VWNIKITSTE EYPHLKPARY RRGFIHKNIM VLPRQTCGLF 

       490        500        510        520        530        540 
THTIFYKEYP GGPKELDKSI QGGELFFTVV LNPISIFMTH LSNYGNDRLG LYTFVNLANF 

       550        560        570        580        590        600 
VKSWTNLRLQ TLPPVQLAHK YFELFPDQKD PLWQNPCDDK RHRDIWSKEK TCDRLPKFLV 

       610        620        630        640        650        660 
IGPQKTGTTA LYLFLVMHPS ILSNSPSPKT FEEVQFFNRN NYHRGIDWYM DFFPVPSNVT 

       670        680        690        700        710        720 
TDFLFEKSAN YFHSEEAPKR AASLVPKAKI ITILIDPSDR AYSWYQHQRS HEDPAALKFS 

       730        740        750        760        770        780 
FYEVISAGPR APSELRALQK RCLVPGWYAS HIERWLVYFP PFQLLIIDGQ QLRTDPATVM 

       790        800        810        820        830        840 
DEVQKFLGVL PHYNYSEALT FDSHKGFWCQ LLEEGKTKCL GKSKGRKYPP MDSDSRTFLS 

       850        860        870 
SYYRDHNVEL SKLLHKLGQP LPSWLRQELQ KVR 

« Hide

Isoform 2 [UniParc].

Checksum: 55EAC286AA742C09
Show »

FASTA38543,766

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a third member of the heparan sulfate/heparin GlcNAc N-deacetylase/ N-sulfotransferase family."
Aikawa J., Esko J.D.
J. Biol. Chem. 274:2690-2695(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Tissue: Brain.
[2]Sakakibara Y., Sanematsu F., Takami Y., Yanagisawa K., Nakayama T., Suiko M., Liu M.-C.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-264.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF074924 mRNA. Translation: AAD15978.1.
AF076605 mRNA. Translation: AAD46061.1.
AY358852 mRNA. Translation: AAQ89211.1.
AC096762 Genomic DNA. No translation available.
AC108201 Genomic DNA. Translation: AAY41001.1.
AC110999 Genomic DNA. Translation: AAY41056.1.
BC109309 mRNA. Translation: AAI09310.1.
BC109310 mRNA. Translation: AAI09311.1.
RefSeqNP_004775.1. NM_004784.2.
UniGeneHs.480596.

3D structure databases

ProteinModelPortalO95803.
SMRO95803. Positions 570-870.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000296499.

PTM databases

PhosphoSiteO95803.

Proteomic databases

PaxDbO95803.
PRIDEO95803.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296499; ENSP00000296499; ENSG00000164100. [O95803-1]
GeneID9348.
KEGGhsa:9348.
UCSCuc003ibw.3. human. [O95803-2]
uc003ibx.3. human. [O95803-1]

Organism-specific databases

CTD9348.
GeneCardsGC04P118954.
HGNCHGNC:7682. NDST3.
HPAHPA056189.
MIM603950. gene.
neXtProtNX_O95803.
PharmGKBPA31488.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267831.
HOGENOMHOG000008010.
HOVERGENHBG082011.
InParanoidO95803.
KOK02578.
OMATVIHDLG.
OrthoDBEOG7FXZXJ.
PhylomeDBO95803.
TreeFamTF313193.

Enzyme and pathway databases

BioCycMetaCyc:HS09011-MONOMER.
BRENDA2.8.2.8. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00756.
UPA00862.

Gene expression databases

ArrayExpressO95803.
BgeeO95803.
CleanExHS_NDST3.
GenevestigatorO95803.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR021930. Heparan_SO4_deacetylase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF12062. HSNSD. 1 hit.
PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

GeneWikiNDST3.
GenomeRNAi9348.
NextBio35005.
PROO95803.
SOURCESearch...

Entry information

Entry nameNDST3_HUMAN
AccessionPrimary (citable) accession number: O95803
Secondary accession number(s): Q4W5C1 expand/collapse secondary AC list , Q4W5D0, Q6UWC5, Q9UP21
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 106 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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

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