ID NDST2_BOVIN Reviewed; 884 AA.
AC O97583; Q862Q7; Q862Y7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2;
DE EC=2.8.2.8;
DE AltName: Full=CCL44;
DE AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 2;
DE Short=NDST-2;
DE Includes:
DE RecName: Full=Heparan sulfate N-deacetylase 2;
DE EC=3.-.-.-;
DE Includes:
DE RecName: Full=Heparan sulfate N-sulfotransferase 2;
DE EC=2.8.2.-;
GN Name=NDST2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Trachea;
RX PubMed=9712870; DOI=10.1074/jbc.273.35.22458;
RA Toma L., Berninsone P., Hirschberg C.B.;
RT "The putative heparin-specific N-acetylglucosaminyl N-deacetylase/N-
RT sulfotransferase also occurs in non-heparin-producing cells.";
RL J. Biol. Chem. 273:22458-22465(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 688-884.
RX PubMed=12658628; DOI=10.1002/mrd.10292;
RA Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T.,
RA Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G.,
RA Izaike Y., Todoroki J., Hashizume K.;
RT "Characterization of gene expression profiles in early bovine pregnancy
RT using a custom cDNA microarray.";
RL Mol. Reprod. Dev. 65:9-18(2003).
CC -!- FUNCTION: Essential bifunctional enzyme that catalyzes both the N-
CC deacetylation and the N-sulfation of glucosamine (GlcNAc) of the
CC glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA
CC disaccharide repeating sugar backbone to make N-sulfated heparosan, a
CC prerequisite substrate for later modifications in heparin biosynthesis.
CC Plays a role in determining the extent and pattern of sulfation of
CC heparan sulfate. Required for the exosomal release of SDCBP, CD63 and
CC syndecan (By similarity). {ECO:0000250|UniProtKB:P52849,
CC ECO:0000269|PubMed:9712870}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-
CC D-glucosaminyl-[heparan sulfate](n); Xref=Rhea:RHEA:21980, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:14602, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC ChEBI:CHEBI:140572; EC=2.8.2.8;
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: The presence of 4 different heparan sulfate N-
CC deacetylase/N-sulfotransferase enzymes in mammals, as well as
CC differences in their enzyme activity suggest that some initiate heparan
CC sulfate modification/sulfation reactions, whereas other later on fill
CC in or extend already modified heparan sulfate sequences.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000305}.
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DR EMBL; AF064825; AAC77921.1; -; mRNA.
DR EMBL; AB098922; BAC56412.1; -; mRNA.
DR AlphaFoldDB; O97583; -.
DR SMR; O97583; -.
DR STRING; 9913.ENSBTAP00000016827; -.
DR GlyCosmos; O97583; 5 sites, No reported glycans.
DR PaxDb; 9913-ENSBTAP00000016827; -.
DR eggNOG; KOG3703; Eukaryota.
DR InParanoid; O97583; -.
DR BRENDA; 2.8.2.8; 908.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IBA:GO_Central.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR021930; Heparan_SO4_deacetylase.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10605:SF53; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 2; 1.
DR PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR Pfam; PF12062; HSNSD; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
KW Multifunctional enzyme; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..884
FT /note="Bifunctional heparan sulfate N-deacetylase/N-
FT sulfotransferase 2"
FT /id="PRO_0000225658"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..884
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 41..598
FT /note="Heparan sulfate N-deacetylase 2"
FT REGION 49..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..884
FT /note="Heparan sulfate N-sulfotransferase 2"
FT COMPBIAS 65..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 614
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000250"
FT BINDING 614..618
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 712
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 833..837
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 818..828
FT /evidence="ECO:0000250"
FT CONFLICT 735
FT /note="T -> S (in Ref. 2; BAC56412)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="D -> A (in Ref. 2; BAC56412)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="Y -> F (in Ref. 2; BAC56412)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="I -> S (in Ref. 2; BAC56412)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="K -> R (in Ref. 2; BAC56412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 884 AA; 100897 MW; 962E364E17C37FC2 CRC64;
MLKLWKVVRP ARQLELHRLI LLLIAFSLGS MGFLAYYVST SPKAKEPLPL PLGDCSSSGA
AGGPGPVRPP VPPRPPRPPE TARTEPVVLV FVESAYSQLG QEIVAILESS RFRYSTELAP
GRGDMPTLTD HTRGRYVLVI YENLLKYVNL DAWSRELLDR YCVEYGVGII GFFRAHEHSL
LSAQLKGFPL FLHSNLGLRD YQVNPTAPLL HLTRPSRLEP GPLPGDDWTI FQSNHRTYEP
VLLGSLRPAE PPVPGPVARR ARLPTVVQDL GVHDGIQRVL FGHGLSFWLH KLVFRDAGGY
LTGKGLLWDL DRYILVDIDD IFVGKEGTRM KVADVEALLT TQNKLRTLVP NFTFNLGFSG
KFYHTGTEEE DAGDDMLLNH RREFWWFPHM WSHMQPHLFH NRSVLADQMR LNKQFALEHG
IPTDLGYAVA PHHSGVYPIH TQLYEAWKSV WGIQVTSTEE YPHLRPARYR RGFIHNGIMV
LPRQTCGLFT HTIFYNEYPG GSRELDRSIR GGELFLTVLL NPISIFMTHL SNYGNDRLGL
YTFESLVRFL QCWTSLRLQT LPPVPLGRKY FDLFPQERSP LWQNPCDDKR HKDIWSKEKT
CDRLPKFLIV GPQKTGTTAI HFFLSLHPAV TSSFPSPSTF EEIQFFNGPN YHKGIDWYMD
FFPVPSNAST DFLFEKSATY FDSEVVPRRG AALLPRAKII TVLTNPADRA YSWYQHQRAH
GDPVALNYTF YQVITASSQD PPALRSLQNR CLVPGYYSTH LQRWLTYYPS GQLLIVDGQE
LRTNPAASME IIQKFLGITP FLNYTRTLRF DEDKGFWCQG LEGGKTRCLG KSKGRKYPDM
DAESRLFLTD FFRNHNLELS KLLSRLGQPV PSWLREELQH SSSG
//
