HS3S6_MOUSE
ID HS3S6_MOUSE Reviewed; 342 AA.
AC Q5GFD5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 6;
DE EC=2.8.2.23;
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 6;
DE Short=3-OST-6;
DE Short=Heparan sulfate 3-O-sulfotransferase 6;
GN Name=Hs3st6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15303968; DOI=10.1042/bj20040908;
RA Xu D., Tiwari V., Xia G., Clement C., Shukla D., Liu J.;
RT "Characterization of heparan sulphate 3-O-sulphotransferase isoform 6 and
RT its role in assisting the entry of herpes simplex virus type 1.";
RL Biochem. J. 385:451-459(2005).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) to catalyze the transfer of a sulfo group to heparan sulfate.
CC Unlike 3-OST-1, does not convert non-anticoagulant heparan sulfate to
CC anticoagulant heparan sulfate.
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 membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney, followed by heart,
CC brain, lung and testis. {ECO:0000269|PubMed:15303968}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AY574375; AAT84072.1; -; mRNA.
DR CCDS; CCDS28496.1; -.
DR RefSeq; NP_001012402.1; NM_001012402.1.
DR AlphaFoldDB; Q5GFD5; -.
DR SMR; Q5GFD5; -.
DR STRING; 10090.ENSMUSP00000040919; -.
DR GlyGen; Q5GFD5; 1 site.
DR iPTMnet; Q5GFD5; -.
DR PhosphoSitePlus; Q5GFD5; -.
DR MaxQB; Q5GFD5; -.
DR PaxDb; Q5GFD5; -.
DR PRIDE; Q5GFD5; -.
DR ProteomicsDB; 267164; -.
DR Antibodypedia; 23316; 27 antibodies from 14 providers.
DR DNASU; 328779; -.
DR Ensembl; ENSMUST00000044922; ENSMUSP00000040919; ENSMUSG00000039628.
DR GeneID; 328779; -.
DR KEGG; mmu:328779; -.
DR UCSC; uc008ayj.1; mouse.
DR CTD; 64711; -.
DR MGI; MGI:3580487; Hs3st6.
DR VEuPathDB; HostDB:ENSMUSG00000039628; -.
DR eggNOG; KOG3704; Eukaryota.
DR GeneTree; ENSGT00940000154768; -.
DR HOGENOM; CLU_017703_0_0_1; -.
DR InParanoid; Q5GFD5; -.
DR OMA; RVCTMNC; -.
DR OrthoDB; 712400at2759; -.
DR PhylomeDB; Q5GFD5; -.
DR TreeFam; TF350755; -.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR BioGRID-ORCS; 328779; 7 hits in 70 CRISPR screens.
DR PRO; PR:Q5GFD5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q5GFD5; protein.
DR Bgee; ENSMUSG00000039628; Expressed in renal corpuscle and 70 other tissues.
DR ExpressionAtlas; Q5GFD5; baseline and differential.
DR Genevisible; Q5GFD5; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; IDA:MGI.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
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; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..342
FT /note="Heparan sulfate glucosamine 3-O-sulfotransferase 6"
FT /id="PRO_0000085225"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..49
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..342
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 56..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100..104
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 122..128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 220..221
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 305..309
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 288..300
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 37415 MW; 9FA1585916862AB7 CRC64;
MAGSGGLGGG AGDLQGAGTG QGTALRALRA PLALVVLLLS AYCLFALPGR CPPAARAPAP
VPAPAEPPHT SLRLRAPGLP VASGPGRRRF PQALIVGVKK GGTRALLEFL RLHPDVRALG
SEPHFFDRCY DRGLAWYRGL MPRTLDGQIT MEKTPSYFVT QEAPRRIHGM SPDTKLIVVV
RNPVTRAISD YAQTLSKTPG LPSFRALAFR HGLGPVDTAW SAVRIGLYAQ HLDNWLRYFP
LSHFLFVSGE RLVSDPAGEV GRVQDFLGLK RVVTDKHFYF NATKGFPCLK KAQGSGRPRC
LGKSKGRPHP RVPEAVVQRL QAFYRPFNRK FYQMTGQDFG WD
