ID   HS3S1_RAT               Reviewed;         311 AA.
AC   Q9ESG5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=Heparan sulfate 3-O-sulfotransferase 1;
DE   Flags: Precursor;
GN   Name=Hs3st1; Synonyms=3ost, 3ost1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RX   PubMed=10926552; DOI=10.1152/ajplung.2000.279.2.l292;
RA   Li Z.-Y., Hirayoshi K., Suzuki Y.;
RT   "Expression of N-deacetylase/sulfotransferase and 3-O-sulfotransferase in
RT   rat alveolar type II cells.";
RL   Am. J. Physiol. 279:L292-L301(2000).
CC   -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC       (PAPS) to catalyze the transfer of a sulfo group to position 3 of
CC       glucosamine residues in heparan. Catalyzes the rate limiting step in
CC       the biosynthesis of heparan sulfate (HSact). This modification is a
CC       crucial step in the biosynthesis of anticoagulant heparan sulfate as it
CC       completes the structure of the antithrombin pentasaccharide binding
CC       site (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC         sulfate](n) = 3-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC         adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:15461, Rhea:RHEA-
CC         COMP:9830, Rhea:RHEA-COMP:9831, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:58388, ChEBI:CHEBI:70975; EC=2.8.2.23;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus lumen {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {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; AF177430; AAG09283.1; -; mRNA.
DR   RefSeq; NP_445843.1; NM_053391.1.
DR   AlphaFoldDB; Q9ESG5; -.
DR   SMR; Q9ESG5; -.
DR   STRING; 10116.ENSRNOP00000068250; -.
DR   GlyGen; Q9ESG5; 4 sites.
DR   PaxDb; Q9ESG5; -.
DR   GeneID; 84406; -.
DR   KEGG; rno:84406; -.
DR   CTD; 9957; -.
DR   RGD; 71084; Hs3st1.
DR   eggNOG; KOG3704; Eukaryota.
DR   InParanoid; Q9ESG5; -.
DR   OrthoDB; 712400at2759; -.
DR   PhylomeDB; Q9ESG5; -.
DR   Reactome; R-RNO-2022928; HS-GAG biosynthesis.
DR   PRO; PR:Q9ESG5; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005796; C:Golgi lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; ISO:RGD.
DR   GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISO:RGD.
DR   Gene3D; 3.40.50.300; -; 1.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Golgi apparatus; Reference proteome; Signal;
KW   Transferase.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..311
FT                   /note="Heparan sulfate glucosamine 3-O-sulfotransferase 1"
FT                   /id="PRO_0000033453"
FT   BINDING         68..72
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..278
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        246
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        260..269
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   311 AA;  35810 MW;  ACEE78B365EBCB75 CRC64;
     MTLLLLGAVL LVAQPQLVPS HPAAPGPGLK QQGLLRKVII LPEDTGEGAA TNGSTQQLPQ
     TIIIGVRKGG TRALLEMLSL HPDVAAAENE VHFFDWEEHY SQGLGWYLTQ MPFSSPHQLT
     VEKTPAYFTS PKVPERIHSM NPTIRLLLIL RDPSERVLSD YTQVLYNHLQ KHKPYPPIED
     LLMRDGRLNV DYKALNRSLY HAHMLNWLRF FPLGHIHIVD GDRFIRDPFP EIQKVERFLK
     LSPQINASNF YFNKTKGFYC LRDSGKDRCL HESKGRAHPQ VDPKLLDKLH EYFREPNKKF
     FKLVGRTFDW H