NDST1_XENLA
ID NDST1_XENLA Reviewed; 878 AA.
AC Q6GQK9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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; BC072733; AAH72733.1; -; mRNA.
DR RefSeq; NP_001085429.1; NM_001091960.1.
DR RefSeq; XP_018109729.1; XM_018254240.1.
DR AlphaFoldDB; Q6GQK9; -.
DR SMR; Q6GQK9; -.
DR GeneID; 443855; -.
DR KEGG; xla:443855; -.
DR CTD; 443855; -.
DR Xenbase; XB-GENE-955057; ndst1.S.
DR OMA; QMELRTH; -.
DR OrthoDB; 388292at2759; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 443855; Expressed in liver and 20 other tissues.
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: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_0000225656"
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 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; 101119 MW; 6FC6721BDAF3B17E CRC64;
MSLSLKTRRF GRPVRPQLVL LLLFALCLLS VFISAYYLYG WKRGLEPSGS EAQSPDCDEP
KISPSRLLPV 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 FAVDHGIPTD
MGYAVAPHHS GVYPVHVQLY EAWKQIWGIK VTSTEEYPHL KPARYRRGFV HNGIMILPRQ
TCGLFTHTIF YNEYPGGPVE LDKIINGGEL FLTVLLNPIS IFMTHLSNYG NDRLGLYTFK
LLVQFLNTWT NLKLETLPPV QLAHKYFQIF PEEKDPLWQD PCEDKRHKDI WSKEKTCDRF
PKLLIIGPQK TGTTALYLFL GMHSDLSSNY PSSETFEEIQ FYNGQNYHKG IDWYMEFFPI
PSNTTSDFYF EKSANYFDSE LAPRRVAALL PKAKIITILI NPADRAYSWY QHQRAHDDPV
AIKYTFQEVI KAGPEAPQRL RALQNRCLVP GWYSTHIERW MNHFHANQIL VLDGKLLRTE
PANVMETVQK FLGVTNAMDY HKTLAFDPKK GFWCQLLDGG KTKCLGKSKG RKYPDMDSDS
RSFLMDYYRD HNIELSKLLY KMGQTLPTWL REELQNTR
