ID HS3S2_RAT Reviewed; 367 AA.
AC Q80W66; A1A5M1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 125.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 2;
DE EC=2.8.2.29 {ECO:0000250|UniProtKB:Q9Y278};
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 2;
DE Short=Heparan sulfate 3-O-sulfotransferase 2;
GN Name=Hs3st2; Synonyms=3ost2;
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], FUNCTION IN CIRCADIAN PHYSIOLOGY, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=12601002; DOI=10.1074/jbc.m300828200;
RA Borjigin J., Deng J., Sun X., De Jesus M., Liu T., Wang M.M.;
RT "Diurnal pineal 3-O-sulphotransferase 2 expression controlled by beta-
RT adrenergic repression.";
RL J. Biol. Chem. 278:16315-16319(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted
CC glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan
CC sulfate. Catalyzes the O-sulfation of glucosamine in GlcA2S-GlcNS.
CC Unlike HS3ST1/3-OST-1, does not convert non-anticoagulant heparan
CC sulfate to anticoagulant heparan sulfate (By similarity). May
CC contribute to the pineal circadian physiology (PubMed:12601002).
CC {ECO:0000250|UniProtKB:Q9Y278, ECO:0000269|PubMed:12601002}.
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=2.8.2.29;
CC Evidence={ECO:0000250|UniProtKB:Q9Y278};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain, in the pineal gland
CC specifically during the daylight hours, and weakly in the olfactory
CC bulb and pineal gland during the night. First detected between
CC postnatal days 5 and 10. {ECO:0000269|PubMed:12601002}.
CC -!- INDUCTION: Activated by light stimulation at night through the
CC suppression of beta-adrenergic signaling.
CC {ECO:0000269|PubMed:12601002}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AY240873; AAP30887.1; -; mRNA.
DR EMBL; BC128721; AAI28722.1; -; mRNA.
DR RefSeq; NP_852035.1; NM_181370.2.
DR AlphaFoldDB; Q80W66; -.
DR SMR; Q80W66; -.
DR STRING; 10116.ENSRNOP00000023773; -.
DR GlyCosmos; Q80W66; 4 sites, No reported glycans.
DR GlyGen; Q80W66; 4 sites.
DR iPTMnet; Q80W66; -.
DR PhosphoSitePlus; Q80W66; -.
DR PaxDb; 10116-ENSRNOP00000023773; -.
DR Ensembl; ENSRNOT00000023773.7; ENSRNOP00000023773.5; ENSRNOG00000017659.8.
DR Ensembl; ENSRNOT00055014352; ENSRNOP00055011512; ENSRNOG00055008490.
DR Ensembl; ENSRNOT00060031034; ENSRNOP00060025138; ENSRNOG00060018101.
DR Ensembl; ENSRNOT00065054097; ENSRNOP00065044524; ENSRNOG00065031374.
DR GeneID; 293451; -.
DR KEGG; rno:293451; -.
DR UCSC; RGD:727787; rat.
DR AGR; RGD:727787; -.
DR CTD; 9956; -.
DR RGD; 727787; Hs3st2.
DR eggNOG; KOG3704; Eukaryota.
DR GeneTree; ENSGT00940000160498; -.
DR HOGENOM; CLU_017703_0_1_1; -.
DR InParanoid; Q80W66; -.
DR OMA; NIIFYRG; -.
DR OrthoDB; 10019at2759; -.
DR PhylomeDB; Q80W66; -.
DR TreeFam; TF350755; -.
DR Reactome; R-RNO-2022928; HS-GAG biosynthesis.
DR PRO; PR:Q80W66; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017659; Expressed in frontal cortex and 4 other cell types or tissues.
DR Genevisible; Q80W66; RN.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; ISS:UniProtKB.
DR GO; GO:0033871; F:[heparan sulfate]-glucosamine 3-sulfotransferase 2 activity; IEA:UniProtKB-EC.
DR GO; GO:0007623; P:circadian rhythm; IDA:RGD.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISO:RGD.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10605:SF10; HEPARAN SULFATE GLUCOSAMINE 3-O-SULFOTRANSFERASE 2; 1.
DR PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..367
FT /note="Heparan sulfate glucosamine 3-O-sulfotransferase 2"
FT /id="PRO_0000085216"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..367
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 66..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..128
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 146..152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 177..180
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 205
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 213
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 245..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 330..334
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 313..325
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
SQ SEQUENCE 367 AA; 41378 MW; 774E8E32C1C4588D CRC64;
MAYRVLGRAG PPQPRRARRL LFAFTLSLSC TYLCYSFLCC CDGLGQSRLL GAPRCLRGPS
ASGQKLLAKS RPCDPPGPTP SEPSAPSAPA AAAPAPRLSG SNHSGSPKPG TKRLPQALIV
GVKKGGTRAV LEFIRVHPDV RALGTEPHFF DRNYGRGLDW YRSLMPRTLE TQITLEKTPS
YFVTQEAPRR IFNMSRDTKL IVVVRNPVTR AISDYTQTLS KKPDIPTFEG LSFRNRSLGL
VDVSWNAIRI GMYALHLESW LRYFPLAQIH FVSGERLITD PAGEMGRIQD FLGIKRFITD
KHFYFNKTKG FPCLKKPEST LLPRCLGKSK GRTHVQIDPE VIDQLREFYR PYNIKFYETV
GQDFRWE
//
