ID HS3S1_HUMAN Reviewed; 307 AA. AC O14792; B3KUA6; Q6PEY8; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 13-FEB-2019, entry version 146. DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 1; DE EC=2.8.2.23; DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 1; DE Short=3-OST-1; DE Short=Heparan sulfate 3-O-sulfotransferase 1; DE Short=h3-OST-1; DE Flags: Precursor; GN Name=HS3ST1; Synonyms=3OST, 3OST1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Brain; RX PubMed=9346953; DOI=10.1074/jbc.272.44.28008; RA Shworak N.W., Liu J., Fritze L.M.S., Schwartz J.J., Zhang L., RA Logeart D., Rosenberg R.D.; RT "Molecular cloning and expression of mouse and human cDNAs encoding RT heparan sulfate D-glucosaminyl 3-O-sulfotransferase."; RL J. Biol. Chem. 272:28008-28019(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-22. RC TISSUE=Brain; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP CHARACTERIZATION. RX PubMed=8900198; DOI=10.1074/jbc.271.43.27072; RA Liu J., Shworak N.W., Fritze L.M., Edelberg J.M., Rosenberg R.D.; RT "Purification of heparan sulfate D-glucosaminyl 3-O- RT sulfotransferase."; RL J. Biol. Chem. 271:27072-27082(1996). RN [6] RP CHARACTERIZATION. RX PubMed=9988768; DOI=10.1074/jbc.274.8.5185; RA Liu J., Shworak N.W., Sinay P., Schwartz J.J., Zhang L., RA Fritze L.M.S., Rosenberg R.D.; RT "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase RT isoforms reveals novel substrate specificities."; RL J. Biol. Chem. 274:5185-5192(1999). RN [7] RP TISSUE SPECIFICITY. RX PubMed=9988767; DOI=10.1074/jbc.274.8.5170; RA Shworak N.W., Liu J., Petros L.M., Zhang L., Kobayashi M., RA Copeland N.G., Jenkins N.A., Rosenberg R.D.; RT "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O- RT sulfotransferase. Isolation, characterization, and expression of human RT cDNAs and identification of distinct genomic loci."; RL J. Biol. Chem. 274:5170-5184(1999). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-307 IN COMPLEX WITH RP SUBSTRATE ANALOG, DISULFIDE BOND, AND BINDING SITES. RG Structural genomics consortium (SGC); RT "Crystal structure of human heparan sulfate glucosamine 3-o- RT sulfotransferase 1 in complex with PAP."; RL Submitted (JUN-2005) to the PDB data bank. CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl CC sulfate (PAPS) to catalyze the transfer of a sulfo group to CC position 3 of glucosamine residues in heparan. Catalyzes the rate CC limiting step in the biosynthesis of heparan sulfate (HSact). This CC modification is a crucial step in the biosynthesis of CC anticoagulant heparan sulfate as it completes the structure of the CC antithrombin pentasaccharide binding site. CC {ECO:0000269|PubMed:9346953}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl- CC [heparan sulfate](n) = 3-sulfo-alpha-D-glucosaminyl-[heparan CC sulfate](n) + adenosine 3',5'-bisphosphate + H(+); CC Xref=Rhea:RHEA:15461, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:9831, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, CC ChEBI:CHEBI:58388, ChEBI:CHEBI:70975; EC=2.8.2.23; CC -!- SUBCELLULAR LOCATION: Golgi apparatus lumen {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and kidney and CC weakly expressed in the heart, lung and placenta. CC {ECO:0000269|PubMed:9988767}. CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. 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; AF019386; AAB84388.1; -; mRNA. DR EMBL; AK096823; BAG53368.1; -; mRNA. DR EMBL; CH471069; EAW92699.1; -; Genomic_DNA. DR EMBL; BC057803; AAH57803.1; -; mRNA. DR CCDS; CCDS3408.1; -. DR RefSeq; NP_005105.1; NM_005114.2. DR RefSeq; XP_011512215.1; XM_011513913.2. DR UniGene; Hs.507348; -. DR UniGene; Hs.605349; -. DR PDB; 1ZRH; X-ray; 2.10 A; A=36-307. DR PDBsum; 1ZRH; -. DR ProteinModelPortal; O14792; -. DR SMR; O14792; -. DR BioGrid; 115282; 2. DR STRING; 9606.ENSP00000002596; -. DR DrugBank; DB01812; Adenosine-3'-5'-Diphosphate. DR iPTMnet; O14792; -. DR PhosphoSitePlus; O14792; -. DR BioMuta; HS3ST1; -. DR EPD; O14792; -. DR PaxDb; O14792; -. DR PeptideAtlas; O14792; -. DR PRIDE; O14792; -. DR ProteomicsDB; 48242; -. DR DNASU; 9957; -. DR Ensembl; ENST00000002596; ENSP00000002596; ENSG00000002587. DR GeneID; 9957; -. DR KEGG; hsa:9957; -. DR UCSC; uc003gmq.4; human. DR CTD; 9957; -. DR DisGeNET; 9957; -. DR EuPathDB; HostDB:ENSG00000002587.9; -. DR GeneCards; HS3ST1; -. DR H-InvDB; HIX0004096; -. DR HGNC; HGNC:5194; HS3ST1. DR HPA; HPA002237; -. DR MIM; 603244; gene. DR neXtProt; NX_O14792; -. DR OpenTargets; ENSG00000002587; -. DR PharmGKB; PA29467; -. DR eggNOG; KOG3704; Eukaryota. DR eggNOG; ENOG410XS59; LUCA. DR GeneTree; ENSGT00940000160449; -. DR HOGENOM; HOG000036663; -. DR HOVERGEN; HBG053377; -. DR InParanoid; O14792; -. DR KO; K01024; -. DR OMA; RVHSMNP; -. DR OrthoDB; 712400at2759; -. DR PhylomeDB; O14792; -. DR TreeFam; TF350755; -. DR BioCyc; MetaCyc:HS00082-MONOMER; -. DR Reactome; R-HSA-2022928; HS-GAG biosynthesis. DR ChiTaRS; HS3ST1; human. DR EvolutionaryTrace; O14792; -. DR GeneWiki; HS3ST1; -. DR GenomeRNAi; 9957; -. DR PRO; PR:O14792; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000002587; Expressed in 190 organ(s), highest expression level in female gonad. DR ExpressionAtlas; O14792; baseline and differential. DR Genevisible; O14792; HS. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; IBA:GO_Central. DR GO; GO:0034483; F:heparan sulfate sulfotransferase activity; IBA:GO_Central. DR GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc. DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome. DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IBA:GO_Central. DR InterPro; IPR037359; NST/OST. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000863; Sulfotransferase_dom. DR PANTHER; PTHR10605; PTHR10605; 1. DR Pfam; PF00685; Sulfotransfer_1; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Golgi apparatus; Polymorphism; Reference proteome; Signal; KW Transferase. FT SIGNAL 1 20 {ECO:0000250}. FT CHAIN 21 307 Heparan sulfate glucosamine 3-O- FT sulfotransferase 1. FT /FTId=PRO_0000033451. FT NP_BIND 64 68 PAPS. FT NP_BIND 270 274 PAPS. FT BINDING 147 147 PAPS. FT BINDING 155 155 PAPS. FT BINDING 255 255 PAPS. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 192 192 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 242 242 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 249 249 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 256 265 {ECO:0000269|Ref.8}. FT VARIANT 22 22 P -> T (in dbSNP:rs11559238). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_021515. FT VARIANT 295 295 K -> R (in dbSNP:rs34719057). FT /FTId=VAR_052529. FT STRAND 56 59 {ECO:0000244|PDB:1ZRH}. FT HELIX 67 74 {ECO:0000244|PDB:1ZRH}. FT STRAND 80 82 {ECO:0000244|PDB:1ZRH}. FT TURN 89 91 {ECO:0000244|PDB:1ZRH}. FT HELIX 93 96 {ECO:0000244|PDB:1ZRH}. FT HELIX 99 105 {ECO:0000244|PDB:1ZRH}. FT STRAND 114 119 {ECO:0000244|PDB:1ZRH}. FT HELIX 121 125 {ECO:0000244|PDB:1ZRH}. FT HELIX 129 136 {ECO:0000244|PDB:1ZRH}. FT STRAND 141 146 {ECO:0000244|PDB:1ZRH}. FT HELIX 149 166 {ECO:0000244|PDB:1ZRH}. FT HELIX 174 178 {ECO:0000244|PDB:1ZRH}. FT HELIX 189 194 {ECO:0000244|PDB:1ZRH}. FT HELIX 196 204 {ECO:0000244|PDB:1ZRH}. FT HELIX 209 211 {ECO:0000244|PDB:1ZRH}. FT STRAND 212 216 {ECO:0000244|PDB:1ZRH}. FT HELIX 217 222 {ECO:0000244|PDB:1ZRH}. FT HELIX 224 234 {ECO:0000244|PDB:1ZRH}. FT HELIX 243 245 {ECO:0000244|PDB:1ZRH}. FT STRAND 246 249 {ECO:0000244|PDB:1ZRH}. FT TURN 250 253 {ECO:0000244|PDB:1ZRH}. FT STRAND 254 259 {ECO:0000244|PDB:1ZRH}. FT STRAND 262 264 {ECO:0000244|PDB:1ZRH}. FT HELIX 279 288 {ECO:0000244|PDB:1ZRH}. FT HELIX 290 300 {ECO:0000244|PDB:1ZRH}. SQ SEQUENCE 307 AA; 35773 MW; AA1052260633EA1C CRC64; MAALLLGAVL LVAQPQLVPS RPAELGQQEL LRKAGTLQDD VRDGVAPNGS AQQLPQTIII GVRKGGTRAL LEMLSLHPDV AAAENEVHFF DWEEHYSHGL GWYLSQMPFS WPHQLTVEKT PAYFTSPKVP ERVYSMNPSI RLLLILRDPS ERVLSDYTQV FYNHMQKHKP YPSIEEFLVR DGRLNVDYKA LNRSLYHVHM QNWLRFFPLR HIHIVDGDRL IRDPFPEIQK VERFLKLSPQ INASNFYFNK TKGFYCLRDS GRDRCLHESK GRAHPQVDPK LLNKLHEYFH EPNKKFFELV GRTFDWH //