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O97583 (NDST2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 2
EC=2.8.2.8
Alternative name(s):
CCL44
Glucosaminyl N-deacetylase/N-sulfotransferase 2
Short name=NDST-2

Including the following 2 domains:

  1. Heparan sulfate N-deacetylase 2
    EC=3.-.-.-
  2. Heparan sulfate N-sulfotransferase 2
    EC=2.8.2.-
Gene names
Name:NDST2
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length884 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. Plays a role in determining the extent and pattern of sulfation of heparan sulfate By similarity. 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.

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 – 884884Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
PRO_0000225658

Regions

Topological domain1 – 1818Cytoplasmic Potential
Transmembrane19 – 3921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain40 – 884845Lumenal Potential
Nucleotide binding614 – 6185PAPS By similarity
Nucleotide binding833 – 8375PAPS By similarity
Region41 – 598558Heparan sulfate N-deacetylase 2
Region599 – 884286Heparan sulfate N-sulfotransferase 2

Sites

Active site6141For sulfotransferase activity By similarity
Binding site7121PAPS By similarity

Amino acid modifications

Glycosylation3511N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation6671N-linked (GlcNAc...) Potential
Glycosylation7271N-linked (GlcNAc...) Potential
Glycosylation8031N-linked (GlcNAc...) Potential
Disulfide bond818 ↔ 828 By similarity

Experimental info

Sequence conflict7351T → S in BAC56412. Ref.2
Sequence conflict737 – 7404SSQD → TSSS in BAC56285. Ref.2
Sequence conflict7401D → A in BAC56412. Ref.2
Sequence conflict7441L → F in BAC56285. Ref.2
Sequence conflict748 – 7525QNRCL → TKPLS in BAC56285. Ref.2
Sequence conflict7681Y → F in BAC56285. Ref.2
Sequence conflict7681Y → F in BAC56412. Ref.2
Sequence conflict7911I → S in BAC56285. Ref.2
Sequence conflict7911I → S in BAC56412. Ref.2
Sequence conflict8141K → R in BAC56412. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O97583 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 962E364E17C37FC2

FASTA884100,897
        10         20         30         40         50         60 
MLKLWKVVRP ARQLELHRLI LLLIAFSLGS MGFLAYYVST SPKAKEPLPL PLGDCSSSGA 

        70         80         90        100        110        120 
AGGPGPVRPP VPPRPPRPPE TARTEPVVLV FVESAYSQLG QEIVAILESS RFRYSTELAP 

       130        140        150        160        170        180 
GRGDMPTLTD HTRGRYVLVI YENLLKYVNL DAWSRELLDR YCVEYGVGII GFFRAHEHSL 

       190        200        210        220        230        240 
LSAQLKGFPL FLHSNLGLRD YQVNPTAPLL HLTRPSRLEP GPLPGDDWTI FQSNHRTYEP 

       250        260        270        280        290        300 
VLLGSLRPAE PPVPGPVARR ARLPTVVQDL GVHDGIQRVL FGHGLSFWLH KLVFRDAGGY 

       310        320        330        340        350        360 
LTGKGLLWDL DRYILVDIDD IFVGKEGTRM KVADVEALLT TQNKLRTLVP NFTFNLGFSG 

       370        380        390        400        410        420 
KFYHTGTEEE DAGDDMLLNH RREFWWFPHM WSHMQPHLFH NRSVLADQMR LNKQFALEHG 

       430        440        450        460        470        480 
IPTDLGYAVA PHHSGVYPIH TQLYEAWKSV WGIQVTSTEE YPHLRPARYR RGFIHNGIMV 

       490        500        510        520        530        540 
LPRQTCGLFT HTIFYNEYPG GSRELDRSIR GGELFLTVLL NPISIFMTHL SNYGNDRLGL 

       550        560        570        580        590        600 
YTFESLVRFL QCWTSLRLQT LPPVPLGRKY FDLFPQERSP LWQNPCDDKR HKDIWSKEKT 

       610        620        630        640        650        660 
CDRLPKFLIV GPQKTGTTAI HFFLSLHPAV TSSFPSPSTF EEIQFFNGPN YHKGIDWYMD 

       670        680        690        700        710        720 
FFPVPSNAST DFLFEKSATY FDSEVVPRRG AALLPRAKII TVLTNPADRA YSWYQHQRAH 

       730        740        750        760        770        780 
GDPVALNYTF YQVITASSQD PPALRSLQNR CLVPGYYSTH LQRWLTYYPS GQLLIVDGQE 

       790        800        810        820        830        840 
LRTNPAASME IIQKFLGITP FLNYTRTLRF DEDKGFWCQG LEGGKTRCLG KSKGRKYPDM 

       850        860        870        880 
DAESRLFLTD FFRNHNLELS KLLSRLGQPV PSWLREELQH SSSG

« Hide

References

[1]"The putative heparin-specific N-acetylglucosaminyl N-deacetylase/N-sulfotransferase also occurs in non-heparin-producing cells."
Toma L., Berninsone P., Hirschberg C.B.
J. Biol. Chem. 273:22458-22465(1998) [PubMed: 9712870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Trachea.
[2]"Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray."
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.
Mol. Reprod. Dev. 65:9-18(2003) [PubMed: 12658628] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 688-884.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF064825 mRNA. Translation: AAC77921.1.
AB098749 mRNA. Translation: BAC56285.1.
AB098922 mRNA. Translation: BAC56412.1.
IPIIPI00707827.
UniGeneBt.4950.

3D structure databases

ProteinModelPortalO97583.
SMRO97583. Positions 580-879.
ModBaseSearch...

Proteomic databases

PRIDEO97583.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGmaNOG11059.
GeneTreeENSGT00560000076777.
HOVERGENHBG082011.
InParanoidO97583.
OrthoDBEOG4NP72R.

Enzyme and pathway databases

BRENDA2.8.2.8. 908.

Family and domain databases

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

Entry information

Entry nameNDST2_BOVIN
AccessionPrimary (citable) accession number: O97583
Secondary accession number(s): Q862Q7, Q862Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 1999
Last modified: September 21, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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