HS3SB_MOUSE
ID HS3SB_MOUSE Reviewed; 390 AA.
AC Q9QZS6; Q5NCR0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 3B1;
DE EC=2.8.2.30 {ECO:0000250|UniProtKB:Q9Y662};
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3B1;
DE Short=3-OST-3B;
DE Short=Heparan sulfate 3-O-sulfotransferase 3B1;
DE Short=m3-OST-3B;
GN Name=Hs3st3b1; Synonyms=3ost3b1, Hs3st3b;
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 SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=10520990; DOI=10.1016/s0092-8674(00)80058-6;
RA Shukla D., Liu J., Blaiklock P., Shworak N.W., Bai X., Esko J.D.,
RA Cohen G.H., Eisenberg R.J., Rosenberg R.D., Spear P.G.;
RT "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1
RT entry.";
RL Cell 99:13-22(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 IdoUA2S-GlcNS and
CC also in IdoUA2S-GlcNH2. Unlike HS3ST1/3-OST-1, does not convert non-
CC anticoagulant heparan sulfate to anticoagulant heparan sulfate (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y662}.
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=2.8.2.30;
CC Evidence={ECO:0000250|UniProtKB:Q9Y662};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:10520990}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:10520990}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AF168992; AAF04505.1; -; mRNA.
DR EMBL; AL603889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466601; EDL10388.1; -; Genomic_DNA.
DR CCDS; CCDS24838.1; -.
DR RefSeq; NP_061275.2; NM_018805.2.
DR AlphaFoldDB; Q9QZS6; -.
DR SMR; Q9QZS6; -.
DR STRING; 10090.ENSMUSP00000091647; -.
DR GlyGen; Q9QZS6; 3 sites.
DR iPTMnet; Q9QZS6; -.
DR PhosphoSitePlus; Q9QZS6; -.
DR PaxDb; Q9QZS6; -.
DR PRIDE; Q9QZS6; -.
DR ProteomicsDB; 267166; -.
DR Antibodypedia; 25106; 39 antibodies from 17 providers.
DR DNASU; 54710; -.
DR Ensembl; ENSMUST00000094103; ENSMUSP00000091647; ENSMUSG00000070407.
DR GeneID; 54710; -.
DR KEGG; mmu:54710; -.
DR UCSC; uc007jkn.1; mouse.
DR CTD; 9953; -.
DR MGI; MGI:1333853; Hs3st3b1.
DR VEuPathDB; HostDB:ENSMUSG00000070407; -.
DR eggNOG; KOG3704; Eukaryota.
DR GeneTree; ENSGT00940000162568; -.
DR HOGENOM; CLU_017703_0_1_1; -.
DR InParanoid; Q9QZS6; -.
DR OMA; TMPGLVM; -.
DR OrthoDB; 712400at2759; -.
DR PhylomeDB; Q9QZS6; -.
DR TreeFam; TF350755; -.
DR BRENDA; 2.8.2.30; 3474.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR BioGRID-ORCS; 54710; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Hs3st3b1; mouse.
DR PRO; PR:Q9QZS6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QZS6; protein.
DR Bgee; ENSMUSG00000070407; Expressed in epithelium of stomach and 162 other tissues.
DR Genevisible; Q9QZS6; MM.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; IDA:MGI.
DR GO; GO:0033872; F:[heparan sulfate]-glucosamine 3-sulfotransferase 3 activity; IEA:UniProtKB-EC.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006477; P:protein sulfation; IDA: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..390
FT /note="Heparan sulfate glucosamine 3-O-sulfotransferase
FT 3B1"
FT /id="PRO_0000085220"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..390
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147..151
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 169..175
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 200..203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 228
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 236
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 268..269
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT BINDING 353..357
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 336..348
FT /evidence="ECO:0000250|UniProtKB:Q9Y663"
FT CONFLICT 76
FT /note="A -> T (in Ref. 1; AAF04505)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43296 MW; EDDCAAF867B6D090 CRC64;
MGQRLSGGRS CLDVPGRFLP QPPPPPPPVR RKLALLFAML CIWLYMFLYS CAGSCTAAPG
LLLLGSGSRA THAQPALVTA PNETSPKMPF RAPPANSLAA GKDKTVGAGS QEEQSPEAPD
SPSPISSFFS GAGSKQLPQA IIIGVKKGGT RALLEFLRVH PDVRAVGAEP HFFDRSYHKG
LAWYRDLMPR TLKGQITMEK TPSYFVTREA PARISAMSKD TKLIVVVRDP VTRAISDYTQ
TLSKRPDIPS FESLTFRNRS AGLIDTSWSA IQIGLYAKHL EPWLRHFPLG QMLFVSGERL
VSDPAGELRR VQDFLGLKRI ITDKHFYFNQ TKGFPCLKKA EGSGKPHCLG KTKGRAHPTI
AREVLRQLRD FYRPFNRKFY QMTGRDFGWD
