NDST1_HUMAN
ID NDST1_HUMAN Reviewed; 882 AA.
AC P52848; B7Z1Q0; E7EVJ3; Q96E57;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 {ECO:0000305|PubMed:9230113};
DE AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 1;
DE Short=NDST-1;
DE AltName: Full=N-heparan sulfate sulfotransferase 1;
DE Short=N-HSST 1;
DE AltName: Full=[Heparan sulfate]-glucosamine N-sulfotransferase 1;
DE Short=HSNST 1;
DE Includes:
DE RecName: Full=Heparan sulfate N-deacetylase 1;
DE EC=3.5.1.- {ECO:0000269|PubMed:35137078, ECO:0000305|PubMed:9230113};
DE Includes:
DE RecName: Full=Heparan sulfate N-sulfotransferase 1;
DE EC=2.8.2.8 {ECO:0000269|PubMed:35137078, ECO:0000269|PubMed:9230113, ECO:0000269|PubMed:9744796};
GN Name=NDST1 {ECO:0000312|HGNC:HGNC:7680}; Synonyms=HSST, HSST1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=7601448; DOI=10.1016/0888-7543(95)80206-2;
RA Dixon J., Loftus S.K., Gladwin A.J., Scambler P.J., Wasmuth J.J.,
RA Dixon M.J.;
RT "Cloning of the human heparan sulfate-N-deacetylase/N-sulfotransferase gene
RT from the Treacher Collins syndrome candidate region at 5q32-q33.1.";
RL Genomics 26:239-244(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORM 1), CATALYTIC
RP ACTIVITY (ISOFORM 1), PATHWAY (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM
RP 1), TISSUE SPECIFICITY, AND REGION.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=9230113; DOI=10.1042/bj3250351;
RA Humphries D.E., Sullivan B.M., Aleixo M.D., Stow J.L.;
RT "Localization of human heparan glucosaminyl N-deacetylase/N-
RT sulphotransferase to the trans-Golgi network.";
RL Biochem. J. 325:351-357(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fibroblast;
RA Labell T.L., Milewicz D.J., Bonadio J., Edelhoff S., Disteche C.M.,
RA Byers P.H.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=19880432; DOI=10.1093/dnares/dsp022;
RA Wakamatsu A., Kimura K., Yamamoto J., Nishikawa T., Nomura N., Sugano S.,
RA Isogai T.;
RT "Identification and functional analyses of 11,769 full-length human cDNAs
RT focused on alternative splicing.";
RL DNA Res. 16:371-383(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 3).
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION (ISOFORM 1), CATALYTIC ACTIVITY (ISOFORM 1), PATHWAY (ISOFORM 1),
RP ACTIVE SITE, AND MUTAGENESIS OF LYS-614.
RX PubMed=9744796; DOI=10.1016/s0014-5793(98)00913-2;
RA Sueyoshi T., Kakuta Y., Pedersen L.C., Wall F.E., Pedersen L.G.,
RA Negishi M.;
RT "A role of Lys614 in the sulfotransferase activity of human heparan sulfate
RT N-deacetylase/N-sulfotransferase.";
RL FEBS Lett. 433:211-214(1998).
RN [8]
RP FUNCTION (ISOFORM 1).
RX PubMed=22660413; DOI=10.1038/ncb2502;
RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A.,
RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P.,
RA David G.;
RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
RL Nat. Cell Biol. 14:677-685(2012).
RN [9]
RP FUNCTION (ISOFORMS 1 AND 3), CATALYTIC ACTIVITY (ISOFORM 1), SUBCELLULAR
RP LOCATION (ISOFORMS 1 AND 3), INTERACTION WITH EXT1 AND EXT2 (ISOFORMS 1 AND
RP 3), AND SUBUNIT (ISOFORMS 1 AND 3).
RX PubMed=35137078; DOI=10.1093/glycob/cwac004;
RA Missaghian P., Dierker T., Khosrowabadi E., Axling F., Eriksson I.,
RA Ghanem A., Kusche-Gullberg M., Kellokumpu S., Kjellen L.;
RT "A dominant negative splice variant of the heparan sulfate biosynthesis
RT enzyme NDST1 reduces heparan sulfate sulfation.";
RL Glycobiology 0:0-0(2022).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 579-882 IN COMPLEX WITH ADENOSINE
RP 3',5'-BISPHOSPHATE, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=10196134; DOI=10.1074/jbc.274.16.10673;
RA Kakuta Y., Sueyoshi T., Negishi M., Pedersen L.C.;
RT "Crystal structure of the sulfotransferase domain of human heparan sulfate
RT N-deacetylase/N-sulfotransferase 1.";
RL J. Biol. Chem. 274:10673-10676(1999).
RN [11]
RP INVOLVEMENT IN MRT46, AND VARIANTS MRT46 SER-611; LEU-640; ASP-642 AND
RP GLN-709.
RX PubMed=25125150; DOI=10.1002/ajmg.a.36723;
RA Reuter M.S., Musante L., Hu H., Diederich S., Sticht H., Ekici A.B.,
RA Uebe S., Wienker T.F., Bartsch O., Zechner U., Oppitz C., Keleman K.,
RA Jamra R.A., Najmabadi H., Schweiger S., Reis A., Kahrizi K.;
RT "NDST1 missense mutations in autosomal recessive intellectual disability.";
RL Am. J. Med. Genet. A 164A:2753-2763(2014).
CC -!- FUNCTION: [Isoform 1]: Essential bifunctional enzyme that catalyzes
CC both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of
CC the glycosaminoglycan in heparan sulfate (PubMed:9230113,
CC PubMed:9744796, PubMed:35137078). Modifies the GlcNAc-GlcA disaccharide
CC repeating sugar backbone to make N-sulfated heparosan, a prerequisite
CC substrate for later modifications in heparin biosynthesis
CC (PubMed:9230113). Plays a role in determining the extent and pattern of
CC sulfation of heparan sulfate. Participates in biosynthesis of heparan
CC sulfate that can ultimately serve as L-selectin ligands, thereby
CC playing a role in inflammatory response (By similarity). Required for
CC the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413).
CC {ECO:0000250|UniProtKB:Q3UHN9, ECO:0000269|PubMed:22660413,
CC ECO:0000269|PubMed:9230113}.
CC -!- FUNCTION: [Isoform 3]: Lacks both N-deacetylase and N-sulfotransferase
CC activities. Acts as a dominant negative on isoform 1, likely by
CC changing the composition of enzyme complexes responsible for elongation
CC and modification of heparan sulfates. {ECO:0000269|PubMed:35137078}.
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=H2O + N-acetyl-alpha-D-glucosaminyl-[heparan sulfate](n) =
CC acetate + alpha-D-glucosaminyl-[heparan sulfate](n);
CC Xref=Rhea:RHEA:70587, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:11585,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:58388,
CC ChEBI:CHEBI:70974; Evidence={ECO:0000269|PubMed:35137078};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70588;
CC Evidence={ECO:0000305|PubMed:35137078};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:35137078, ECO:0000269|PubMed:9230113,
CC ECO:0000269|PubMed:9744796};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21981;
CC Evidence={ECO:0000269|PubMed:9230113};
CC -!- PATHWAY: [Isoform 1]: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000305|PubMed:9230113, ECO:0000305|PubMed:9744796}.
CC -!- PATHWAY: [Isoform 1]: Glycan metabolism; heparin biosynthesis.
CC {ECO:0000305|PubMed:9230113, ECO:0000305|PubMed:9744796}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10196134}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with heparan sulfate co-polymerase
CC subunits EXT1 and EXT2. Interacts with NDST1 isoform 3.
CC {ECO:0000269|PubMed:35137078}.
CC -!- SUBUNIT: [Isoform 3]: Interacts with heparan sulfate co-polymerase
CC subunits EXT1 and EXT2. Interacts with NDST1 isoform 1.
CC {ECO:0000269|PubMed:35137078}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:9230113}; Single-pass type II membrane
CC protein {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:35137078}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Golgi apparatus, cis-Golgi network
CC membrane {ECO:0000269|PubMed:35137078}; Single-pass type II membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NDST1A {ECO:0000303|PubMed:35137078};
CC IsoId=P52848-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52848-2; Sequence=VSP_017397, VSP_017398;
CC Name=3; Synonyms=NDST1B {ECO:0000303|PubMed:35137078};
CC IsoId=P52848-3; Sequence=VSP_061518;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expression is most abundant in
CC heart, liver and pancreas. {ECO:0000269|PubMed:9230113}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 46
CC (MRT46) [MIM:616116]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRT46
CC manifestations include delayed psychomotor development apparent from
CC infancy or early childhood, delayed or absent expressive speech,
CC hypotonia, and therapy-responsive seizures in some patients. Behavioral
CC abnormalities are variable and include aggression, self-injurious
CC behavior, and sleep disturbances. {ECO:0000269|PubMed:25125150}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
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 -!- MISCELLANEOUS: [Isoform 3]: The increased expression in several types
CC of cancer is associated with shorter survival.
CC {ECO:0000305|PubMed:35137078}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000305}.
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DR EMBL; U18918; AAA75281.1; -; mRNA.
DR EMBL; U36600; AAC27354.1; -; mRNA.
DR EMBL; U17970; AAA67765.1; -; mRNA.
DR EMBL; AK293746; BAH11586.1; -; mRNA.
DR EMBL; AC008472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF510896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012888; AAH12888.1; -; mRNA.
DR CCDS; CCDS34277.1; -. [P52848-1]
DR PIR; A57169; A57169.
DR RefSeq; NP_001287992.1; NM_001301063.1.
DR RefSeq; NP_001534.1; NM_001543.4. [P52848-1]
DR RefSeq; XP_005268496.1; XM_005268439.1.
DR RefSeq; XP_006714846.1; XM_006714783.1.
DR RefSeq; XP_016864917.1; XM_017009428.1.
DR RefSeq; XP_016864918.1; XM_017009429.1.
DR RefSeq; XP_016864919.1; XM_017009430.1.
DR RefSeq; XP_016864920.1; XM_017009431.1.
DR PDB; 1NST; X-ray; 2.30 A; A=558-882.
DR PDBsum; 1NST; -.
DR AlphaFoldDB; P52848; -.
DR SMR; P52848; -.
DR BioGRID; 109572; 36.
DR IntAct; P52848; 6.
DR STRING; 9606.ENSP00000261797; -.
DR DrugBank; DB01812; Adenosine 3',5'-diphosphate.
DR GlyGen; P52848; 4 sites.
DR iPTMnet; P52848; -.
DR PhosphoSitePlus; P52848; -.
DR BioMuta; NDST1; -.
DR EPD; P52848; -.
DR jPOST; P52848; -.
DR MassIVE; P52848; -.
DR MaxQB; P52848; -.
DR PaxDb; P52848; -.
DR PeptideAtlas; P52848; -.
DR PRIDE; P52848; -.
DR ProteomicsDB; 18650; -.
DR ProteomicsDB; 56543; -. [P52848-1]
DR ProteomicsDB; 56544; -. [P52848-2]
DR Antibodypedia; 28038; 199 antibodies from 23 providers.
DR DNASU; 3340; -.
DR Ensembl; ENST00000261797.7; ENSP00000261797.6; ENSG00000070614.15. [P52848-1]
DR Ensembl; ENST00000523767.5; ENSP00000428604.1; ENSG00000070614.15. [P52848-3]
DR GeneID; 3340; -.
DR KEGG; hsa:3340; -.
DR MANE-Select; ENST00000261797.7; ENSP00000261797.6; NM_001543.5; NP_001534.1.
DR UCSC; uc003lsk.4; human. [P52848-1]
DR CTD; 3340; -.
DR DisGeNET; 3340; -.
DR GeneCards; NDST1; -.
DR HGNC; HGNC:7680; NDST1.
DR HPA; ENSG00000070614; Low tissue specificity.
DR MalaCards; NDST1; -.
DR MIM; 600853; gene.
DR MIM; 616116; phenotype.
DR neXtProt; NX_P52848; -.
DR OpenTargets; ENSG00000070614; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA31486; -.
DR VEuPathDB; HostDB:ENSG00000070614; -.
DR eggNOG; KOG3703; Eukaryota.
DR GeneTree; ENSGT00940000157857; -.
DR HOGENOM; CLU_011357_2_0_1; -.
DR InParanoid; P52848; -.
DR OMA; QMELRTH; -.
DR OrthoDB; 388292at2759; -.
DR PhylomeDB; P52848; -.
DR TreeFam; TF313193; -.
DR BioCyc; MetaCyc:HS01001-MON; -.
DR BRENDA; 2.8.2.8; 2681.
DR PathwayCommons; P52848; -.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR SABIO-RK; P52848; -.
DR SignaLink; P52848; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR BioGRID-ORCS; 3340; 30 hits in 1083 CRISPR screens.
DR ChiTaRS; NDST1; human.
DR EvolutionaryTrace; P52848; -.
DR GeneWiki; NDST1; -.
DR GenomeRNAi; 3340; -.
DR Pharos; P52848; Tbio.
DR PRO; PR:P52848; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P52848; protein.
DR Bgee; ENSG00000070614; Expressed in stromal cell of endometrium and 204 other tissues.
DR ExpressionAtlas; P52848; baseline and differential.
DR Genevisible; P52848; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0102140; F:heparan sulfate N-deacetylase activity; IDA:UniProtKB.
DR GO; GO:0050119; F:N-acetylglucosamine deacetylase activity; TAS:Reactome.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome.
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 GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0006477; P:protein sulfation; IEA:Ensembl.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disease variant; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Hydrolase; Inflammatory response;
KW Intellectual disability; Membrane; Multifunctional enzyme;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..882
FT /note="Bifunctional heparan sulfate N-deacetylase/N-
FT sulfotransferase 1"
FT /id="PRO_0000085210"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..882
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..169
FT /note="Sufficient for localization to Golgi membrane"
FT /evidence="ECO:0000269|PubMed:9230113"
FT REGION 40..598
FT /note="Heparan sulfate N-deacetylase 1"
FT REGION 599..882
FT /note="Heparan sulfate N-sulfotransferase 1"
FT ACT_SITE 614
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000305|PubMed:9744796"
FT BINDING 614..618
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /evidence="ECO:0000269|PubMed:10196134,
FT ECO:0007744|PDB:1NST"
FT BINDING 712
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /evidence="ECO:0000269|PubMed:10196134,
FT ECO:0007744|PDB:1NST"
FT BINDING 817
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /evidence="ECO:0000269|PubMed:10196134,
FT ECO:0007744|PDB:1NST"
FT BINDING 833..837
FT /ligand="adenosine 3',5'-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58343"
FT /evidence="ECO:0000269|PubMed:10196134,
FT ECO:0007744|PDB:1NST"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 DISULFID 818..828
FT /evidence="ECO:0000269|PubMed:10196134,
FT ECO:0007744|PDB:1NST"
FT VAR_SEQ 523..556
FT /note="ISIFMTHLSNYGNDRLGLYTFKHLVRFLHSWTNL -> VSAPQPMAAGEKGL
FT LHSLSAADTGFLEPGKGGEA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017397"
FT VAR_SEQ 557..882
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017398"
FT VAR_SEQ 716..772
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000269|PubMed:19880432"
FT /id="VSP_061518"
FT VARIANT 611
FT /note="G -> S (in MRT46; dbSNP:rs606231459)"
FT /evidence="ECO:0000269|PubMed:25125150"
FT /id="VAR_072646"
FT VARIANT 640
FT /note="F -> L (in MRT46; dbSNP:rs606231458)"
FT /evidence="ECO:0000269|PubMed:25125150"
FT /id="VAR_072647"
FT VARIANT 642
FT /note="E -> D (in MRT46; dbSNP:rs606231457)"
FT /evidence="ECO:0000269|PubMed:25125150"
FT /id="VAR_072648"
FT VARIANT 709
FT /note="R -> Q (in MRT46; dbSNP:rs606231456)"
FT /evidence="ECO:0000269|PubMed:25125150"
FT /id="VAR_072649"
FT MUTAGEN 614
FT /note="K->A: Loss of heparan sulfate-glucosamine N-
FT sulfotransferase activity."
FT /evidence="ECO:0000269|PubMed:9744796"
FT CONFLICT 24..28
FT /note="FIFCL -> QVVCQ (in Ref. 6; AAH12888)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="P -> A (in Ref. 3; AAA67765)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="L -> R (in Ref. 4; BAH11586)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="H -> Q (in Ref. 6; AAH12888)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="R -> G (in Ref. 3; AAA67765)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="K -> R (in Ref. 3; AAA67765)"
FT /evidence="ECO:0000305"
FT STRAND 604..609
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 617..625
FT /evidence="ECO:0007829|PDB:1NST"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:1NST"
FT TURN 637..639
FT /evidence="ECO:0007829|PDB:1NST"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 649..653
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 655..659
FT /evidence="ECO:0007829|PDB:1NST"
FT STRAND 672..676
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 679..682
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 686..693
FT /evidence="ECO:0007829|PDB:1NST"
FT STRAND 698..703
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 706..719
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 723..727
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 730..734
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 742..752
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 753..755
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 757..765
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 770..772
FT /evidence="ECO:0007829|PDB:1NST"
FT STRAND 773..777
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 778..783
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 785..796
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 805..807
FT /evidence="ECO:0007829|PDB:1NST"
FT STRAND 808..811
FT /evidence="ECO:0007829|PDB:1NST"
FT TURN 812..815
FT /evidence="ECO:0007829|PDB:1NST"
FT STRAND 816..820
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 842..866
FT /evidence="ECO:0007829|PDB:1NST"
FT HELIX 872..878
FT /evidence="ECO:0007829|PDB:1NST"
SQ SEQUENCE 882 AA; 100868 MW; D4B716B84A0BF4C4 CRC64;
MPALACLRRL CRHVSPQAVL FLLFIFCLFS VFISAYYLYG WKRGLEPSAD APEPDCGDPP
PVAPSRLLPL KPVQAATPSR TDPLVLVFVE SLYSQLGQEV VAILESSRFK YRTEIAPGKG
DMPTLTDKGR GRFALIIYEN ILKYVNLDAW NRELLDKYCV AYGVGIIGFF KANENSLLSA
QLKGFPLFLH SNLGLKDCSI NPKSPLLYVT RPSEVEKGVL PGEDWTVFQS NHSTYEPVLL
AKTRSSESIP HLGADAGLHA ALHATVVQDL GLHDGIQRVL FGNNLNFWLH KLVFVDAVAF
LTGKRLSLPL DRYILVDIDD IFVGKEGTRM KVEDVKALFD TQNELRAHIP NFTFNLGYSG
KFFHTGTNAE DAGDDLLLSY VKEFWWFPHM WSHMQPHLFH NQSVLAEQMA LNKKFAVEHG
IPTDMGYAVA PHHSGVYPVH VQLYEAWKQV WSIRVTSTEE YPHLKPARYR RGFIHNGIMV
LPRQTCGLFT HTIFYNEYPG GSSELDKIIN GGELFLTVLL NPISIFMTHL SNYGNDRLGL
YTFKHLVRFL HSWTNLRLQT LPPVQLAQKY FQIFSEEKDP LWQDPCEDKR HKDIWSKEKT
CDRFPKLLII GPQKTGTTAL YLFLGMHPDL SSNYPSSETF EEIQFFNGHN YHKGIDWYME
FFPIPSNTTS DFYFEKSANY FDSEVAPRRA AALLPKAKVL TILINPADRA YSWYQHQRAH
DDPVALKYTF HEVITAGSDA SSKLRALQNR CLVPGWYATH IERWLSAYHA NQILVLDGKL
LRTEPAKVMD MVQKFLGVTN TIDYHKTLAF DPKKGFWCQL LEGGKTKCLG KSKGRKYPEM
DLDSRAFLKD YYRDHNIELS KLLYKMGQTL PTWLREDLQN TR
