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 02-SEP-2026, entry version 206. 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:35137078, CC PubMed:9230113, PubMed:9744796). 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=N-acetyl-alpha-D-glucosaminyl-[heparan sulfate](n) + H2O = CC alpha-D-glucosaminyl-[heparan sulfate](n) + acetate; 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=alpha-D-glucosaminyl-[heparan sulfate](n) + 3'-phosphoadenylyl CC sulfate = N-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + CC adenosine 3',5'-bisphosphate + 2 H(+); Xref=Rhea:RHEA:21980, CC Rhea:RHEA-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS75358.1; -. [P52848-3] DR PIR; A57169; A57169. DR RefSeq; NP_001287992.1; NM_001301063.2. [P52848-3] DR RefSeq; NP_001534.1; NM_001543.5. [P52848-1] DR PDB; 1NST; X-ray; 2.30 A; A=558-882. DR PDB; 8CCY; EM; 2.70 A; A=79-882. DR PDB; 8CD0; EM; 2.42 A; A=1-882. DR PDB; 8CHS; EM; 3.15 A; A=79-882. DR PDB; 9F6Z; EM; 4.50 A; A/B=43-882. DR AlphaFoldDB; P52848; -. DR EMDB; EMD-16564; -. DR EMDB; EMD-16565; -. DR EMDB; EMD-16626; -. DR EMDB; EMD-16627; -. DR EMDB; EMD-16629; -. DR EMDB; EMD-16661; -. DR EMDB; EMD-16662; -. DR EMDB; EMD-16663; -. DR EMDB; EMD-16664; -. DR EMDB; EMD-17349; -. DR SMR; P52848; -. DR BioGRID; 109572; 60. DR FunCoup; P52848; 1422. DR IntAct; P52848; 37. DR NDEx; IQUERY-CP-NDST1; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000261797; -. DR DrugBank; DB01812; Adenosine 3',5'-diphosphate. DR GlyCosmos; P52848; 4 sites, No reported glycans. DR GlyGen; P52848; 5 sites, 1 N-linked glycan (1 site). DR iPTMnet; P52848; -. DR PhosphoSitePlus; P52848; -. DR SwissPalm; P52848; -. DR BioMuta; NDST1; -. DR jPOST; P52848; -. DR MassIVE; P52848; -. DR PaxDb; 9606-ENSP00000261797; -. DR PeptideAtlas; P52848; -. DR ProteomicsDB; 18650; -. DR ProteomicsDB; 56543; -. [P52848-1] DR ProteomicsDB; 56544; -. [P52848-2] DR Pumba; P52848; -. DR Antibodypedia; 28038; 197 antibodies from 24 providers. DR DNASU; 3340; -. DR Ensembl; ENST00000261797.7; ENSP00000261797.6; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000523767.5; ENSP00000428604.1; ENSG00000070614.16. [P52848-3] DR Ensembl; ENST00000891667.1; ENSP00000561726.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000891668.1; ENSP00000561727.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000891669.1; ENSP00000561728.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000891670.1; ENSP00000561729.1; ENSG00000070614.16. [P52848-3] DR Ensembl; ENST00000891674.1; ENSP00000561733.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000891675.1; ENSP00000561734.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000891676.1; ENSP00000561735.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000891677.1; ENSP00000561736.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000937575.1; ENSP00000607634.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000937577.1; ENSP00000607636.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000937578.1; ENSP00000607637.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000937579.1; ENSP00000607638.1; ENSG00000070614.16. [P52848-1] DR Ensembl; ENST00000965561.1; ENSP00000635620.1; ENSG00000070614.16. [P52848-1] 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 AGR; HGNC:7680; -. DR ClinPGx; PA31486; -. 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 OpenTargets; ENSG00000070614; -. DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability. DR VEuPathDB; HostDB:ENSG00000070614; -. DR eggNOG; KOG3703; Eukaryota. DR GeneTree; ENSGT00940000157857; -. DR HOGENOM; CLU_011357_2_0_1; -. DR InParanoid; P52848; -. DR OMA; VGPDCDE; -. DR OrthoDB; 8958249at2759; -. DR PAN-GO; P52848; 4 GO annotations based on evolutionary models. DR PhylomeDB; P52848; -. DR BioCyc; MetaCyc:HS01001-MONOMER; -. 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 Agora; ENSG00000070614; -. DR BioGRID-ORCS; 3340; 35 hits in 1166 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 206 other cell types or tissues. DR ExpressionAtlas; P52848; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; 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:0015016; F:heparan sulfate N-sulfotransferase activity; IDA:UniProtKB. DR GO; GO:0050119; F:N-acetylglucosamine deacetylase activity; TAS:Reactome. DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISS:UniProtKB. DR GO; GO:0030210; P:heparin proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway. DR DisProt; DP03254; -. DR FunFam; 3.40.50.300:FF:000176; bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR021930; Heparan_SO4_deacetylase_dom. DR InterPro; IPR056793; HSNSD_N. DR InterPro; IPR037359; NST/OST. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000863; Sulfotransferase_dom. DR PANTHER; PTHR10605:SF30; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 1; 1. DR PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1. DR Pfam; PF12062; HSNSD-CE; 1. DR Pfam; PF25119; HSNSD_N; 1. DR Pfam; PF00685; Sulfotransfer_1; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PDBsum; 1NST; -. DR PDBsum; 8CCY; -. DR PDBsum; 8CD0; -. DR PDBsum; 8CHS; -. DR PDBsum; 9F6Z; -. 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 Proteomics identification; Reference proteome; Signal-anchor; Transferase; KW Transmembrane; 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 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 615 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 616 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 617 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 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 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 834 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 835 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 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 FT N-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 85..88 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 95..106 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:8CCY" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:8CCY" FT STRAND 126..132 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 142..145 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 149..162 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:8CHS" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:8CD0" FT TURN 271..274 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 288..301 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 310..321 FT /evidence="ECO:0007829|PDB:8CD0" FT TURN 326..328 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 332..348 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 355..358 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 360..362 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 368..373 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 376..378 FT /evidence="ECO:0007829|PDB:8CD0" FT TURN 380..383 FT /evidence="ECO:0007829|PDB:8CCY" FT STRAND 385..388 FT /evidence="ECO:0007829|PDB:8CD0" FT TURN 396..399 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 402..419 FT /evidence="ECO:0007829|PDB:8CD0" FT TURN 434..439 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 441..450 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 455..459 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 464..466 FT /evidence="ECO:0007829|PDB:8CCY" FT HELIX 467..469 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 478..484 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 494..498 FT /evidence="ECO:0007829|PDB:8CHS" FT HELIX 502..509 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 513..520 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 522..528 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 530..532 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 534..536 FT /evidence="ECO:0007829|PDB:8CCY" FT HELIX 538..553 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 557..559 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 563..573 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 575..578 FT /evidence="ECO:0007829|PDB:8CD0" FT TURN 585..587 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 589..594 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 597..599 FT /evidence="ECO:0007829|PDB:8CHS" FT STRAND 604..609 FT /evidence="ECO:0007829|PDB:1NST" FT STRAND 613..616 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 617..625 FT /evidence="ECO:0007829|PDB:1NST" FT STRAND 630..632 FT /evidence="ECO:0007829|PDB:1NST" FT HELIX 633..635 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 667..669 FT /evidence="ECO:0007829|PDB:8CD0" FT STRAND 672..676 FT /evidence="ECO:0007829|PDB:1NST" FT TURN 678..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 STRAND 738..740 FT /evidence="ECO:0007829|PDB:8CCY" 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 TURN 830..833 FT /evidence="ECO:0007829|PDB:8CD0" FT HELIX 838..841 FT /evidence="ECO:0007829|PDB:1NST" FT HELIX 842..866 FT /evidence="ECO:0007829|PDB:1NST" FT HELIX 868..871 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 //