ID NDST_CAEEL Reviewed; 852 AA.
AC Q966W3; Q19197; Q966W4; Q966W5; Q966W6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1;
DE EC=2.8.2.8;
DE AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 1;
DE Includes:
DE RecName: Full=Heparan sulfate N-deacetylase 1;
DE EC=3.-.-.-;
DE Includes:
DE RecName: Full=Heparan sulfate N-sulfotransferase 1;
DE EC=2.8.2.-;
GN Name=hst-1; ORFNames=F08B4.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Aikawa J.;
RT "Molecular characterization of N-deacetylase/N-sulfotransferase in worm.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RA Aikawa J.;
RT "Structure and function of heparan sulfate/heparin N-deacetylase/ N-
RT sulfotransferase in worm.";
RL (In) Proceedings of the 14th international C. elegans meeting, pp.345-345,
RL Los Angeles (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 (Probable). {ECO:0000305|Ref.3}.
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 -!- TISSUE SPECIFICITY: Present in some specific neurons in head and tail
CC regions and muscles. {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000305}.
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DR EMBL; AB037941; BAB61756.1; -; mRNA.
DR EMBL; AB037942; BAB61757.1; -; mRNA.
DR EMBL; AB037943; BAB61758.1; -; mRNA.
DR EMBL; AB038044; BAB62394.1; -; mRNA.
DR EMBL; FO080903; CCD67652.2; -; Genomic_DNA.
DR PIR; T29486; T29486.
DR RefSeq; NP_501491.4; NM_069090.4.
DR AlphaFoldDB; Q966W3; -.
DR SMR; Q966W3; -.
DR STRING; 6239.F08B4.6.1; -.
DR GlyCosmos; Q966W3; 9 sites, No reported glycans.
DR EPD; Q966W3; -.
DR PaxDb; 6239-F08B4-6; -.
DR EnsemblMetazoa; F08B4.6.1; F08B4.6.1; WBGene00002028.
DR GeneID; 177675; -.
DR KEGG; cel:CELE_F08B4.6; -.
DR UCSC; F08B4.6; c. elegans.
DR AGR; WB:WBGene00002028; -.
DR WormBase; F08B4.6; CE46914; WBGene00002028; hst-1.
DR eggNOG; KOG3703; Eukaryota.
DR GeneTree; ENSGT00940000168016; -.
DR HOGENOM; CLU_011357_2_0_1; -.
DR InParanoid; Q966W3; -.
DR OMA; GRQYPTM; -.
DR OrthoDB; 2913264at2759; -.
DR PhylomeDB; Q966W3; -.
DR Reactome; R-CEL-2022928; HS-GAG biosynthesis.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR PRO; PR:Q966W3; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002028; Expressed in germ line (C elegans) and 4 other cell types or tissues.
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:SF56; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE; 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..852
FT /note="Bifunctional heparan sulfate N-deacetylase/N-
FT sulfotransferase 1"
FT /id="PRO_0000225664"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..852
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 34..574
FT /note="Heparan sulfate N-deacetylase 1"
FT REGION 575..852
FT /note="Heparan sulfate N-sulfotransferase 1"
FT ACT_SITE 592
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000250"
FT BINDING 592..596
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 686
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 803..807
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 789..798
FT /evidence="ECO:0000250"
SQ SEQUENCE 852 AA; 99061 MW; 1DD390CCDA5EDE21 CRC64;
MIITPYLNRK ITRPLKWILA LIFLYLIYIC LFSNNSKPPK PRKKPKLVEN YTCPFARTEG
TASENLFFHT NNGTDARILV ILDSLFSRHG KTIIQILNSQ KLQFKAEAVS KNLPVLTTSR
RGRYSLIIIE NYYKYLNMAQ WNRQLLDKYC KEYRVPMFSF MSSKPNDQLK RIKIKGSSLW
MWQNQRIQRL AVTPSIIHRI SKIGNYRQFS SSDPADWILF ETSEKFESVL SGTVKSGYER
AVVVRDKGLE DGVERIIFGR NLTDFQVKIT FLDALWWAMG NQKSFTLDRF VQVDIDDVFV
GAQGTRIVEE DVRKLISTQK EFRNYVQNFT FMLGFSGSYF RNGDDLEDRG DEFLVENAEK
FVWFPHMWRH NHAHEHNFTY LEAIMAQNKL FAQNMHLPVD YPYAIAPQHD GVFPVHEQLF
RAWRKVWNVS VTATEEYPHF KPATARKGFI HAGIHVLPRQ TCGLYTHTQL FDEYPEGFDK
VQKSIEGGDL FFTILLNPIS IFMTHQQNYA YDRLALYTFE NLFRFIKCWT NIKLKWQDPL
TSSQLYFQKF PDERTPLWTN PCTDPRHHAI LPPSINCTKK SLPDLLIIGP QKTGSTALAS
FLSLHPNTSQ NTPVPGSFEE VQFFGGQNYL KGVEWYMSNF PSSSTVTFEK SATYFDNPSA
PKQAASLVPH AKIVIILQNP AQRAYSWFQH ILAHEDPVAI TAGSLEVILD SNSTSSKKVR
QRCISGGRYV HHLTKWLEHF SLQQMIFVDS DELKMKPPTV LNSLSKWLDL PEFPFETYIR
YSPSKGFHCR LLDGKTKCLG ESKGRKYPEM PENLRRKLDK IFSLDNSALY KFLRKNRLKI
PTWLEESVRI RA
//
