NDST1_XENTR
ID NDST1_XENTR Reviewed; 878 AA.
AC Q5U4X8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 {ECO:0000250|UniProtKB:Q3UHN9};
DE AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 1;
DE Short=NDST-1;
DE Includes:
DE RecName: Full=Heparan sulfate N-deacetylase 1 {ECO:0000250|UniProtKB:Q3UHN9};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:Q3UHN9};
DE Includes:
DE RecName: Full=Heparan sulfate N-sulfotransferase 1 {ECO:0000250|UniProtKB:Q3UHN9};
DE EC=2.8.2.8 {ECO:0000250|UniProtKB:Q3UHN9};
GN Name=ndst1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:Q3UHN9}.
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 Evidence={ECO:0000250|UniProtKB:Q3UHN9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21981;
CC Evidence={ECO:0000250|UniProtKB:Q3UHN9};
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000250|UniProtKB:Q3UHN9}.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC {ECO:0000250|UniProtKB:Q3UHN9}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P52848}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q02353}; Single-pass type II membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:P52848}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000305}.
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DR EMBL; BC084915; AAH84915.1; -; mRNA.
DR RefSeq; NP_001011159.1; NM_001011159.1.
DR AlphaFoldDB; Q5U4X8; -.
DR SMR; Q5U4X8; -.
DR STRING; 8364.ENSXETP00000060802; -.
DR PaxDb; Q5U4X8; -.
DR DNASU; 496577; -.
DR GeneID; 496577; -.
DR KEGG; xtr:496577; -.
DR CTD; 3340; -.
DR Xenbase; XB-GENE-955052; ndst1.
DR eggNOG; KOG3703; Eukaryota.
DR InParanoid; Q5U4X8; -.
DR OrthoDB; 388292at2759; -.
DR Reactome; R-XTR-2022928; HS-GAG biosynthesis.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; ISS:UniProtKB.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0102140; F:heparan sulfate N-deacetylase activity; ISS:UniProtKB.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.300; -; 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; PTHR10605; 1.
DR Pfam; PF12062; HSNSD; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 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..878
FT /note="Bifunctional heparan sulfate N-deacetylase/N-
FT sulfotransferase 1"
FT /id="PRO_0000225657"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..878
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..169
FT /note="Sufficient for localization to Golgi membrane"
FT /evidence="ECO:0000250|UniProtKB:P52848"
FT REGION 40..594
FT /note="Heparan sulfate N-deacetylase 1"
FT REGION 47..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..878
FT /note="Heparan sulfate N-sulfotransferase 1"
FT ACT_SITE 610
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000250|UniProtKB:P52848"
FT BINDING 610..614
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /evidence="ECO:0000250|UniProtKB:P52848"
FT BINDING 708
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /evidence="ECO:0000250|UniProtKB:P52848"
FT BINDING 813
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /evidence="ECO:0000250|UniProtKB:P52848"
FT BINDING 829..833
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /evidence="ECO:0000250|UniProtKB:P52848"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 814..824
FT /evidence="ECO:0000250|UniProtKB:P52848"
SQ SEQUENCE 878 AA; 101135 MW; 7185AAC0AFF274C1 CRC64;
MSLSLKTRRF GRPVRPQLVL LLLFALCLLS VFISAYYLYG WKRGLEPSGS EAQSPDCDEP
KISPSRLLPM KPLKPVDSSR TDPLVLVFVE SLYSQLGQEI VAILESSRFK YRTEIAPGKG
DMPTLTDKDR GRFALIVYEN ILKYVNLDAW NRELLDKYCV EYGVGIIGFF KANENSLLSA
QLKGFPLYLH SNLGLKDCSI NPKSPLLYIT RPNQVEKGDL PGEDWTVFQS NHSTYEPVLL
AKTKSAESIP HLSVDAALHT TVVQDLGLHD GIQRVLFGNN LNFWLHKLVF VDAVSFLTGK
RLSLPLNRYV LVDIDDIFVG KEGTRMKVED VKALYDTQME LRTHIPNFTF NLGFSGKFFH
TGTDAEDEGD DLLLSYVKQF WWFPHMWSHM QPHLFHNQSV LAEQMALNRK FAVEHGIPTD
MGYAVAPHHS GVYPVHVQLY EAWKQIWGIK VTSTEEYPHL KPARYRRGFV HNGIMVLPRQ
TCGLFTHTIF YNEYPGGPVE LDKIINGGEL FLTVLLNPIS IFMTHLSNYG NDRLGLYTFK
HLVQFLNTWT NLKLETLPPV QLAHKYFQIF PEEKDPLWQD PCEDKRHKDI WSKEKTCDRF
PKLLIIGPQK TGTTALYLFL GMHSDLSSNY PSSETFEEIQ FFNGQNYHKG IDWFMEFFPI
PSNTTSDFYF EKSANYFDSE LAPRRVAALL PKAKIITILI NPADRAYSWY QHQRAHDDPV
AMKYTFQEVI TAGPEAPQRL RALQNRCLVP GWYSTHIERW MNHFHANQIL VLDGKLLRTE
PANVMETVQK FLGVTNAMDY HKTLAFDPKK GFWCQLLDGG RTKCLGKSKG RKYPDMDSDS
RSFLMDYYRD HNIELSKLLY KMGQTLPTWL REELQSTR
