HS3SB_HUMAN
ID HS3SB_HUMAN Reviewed; 390 AA.
AC Q9Y662; B3KN58; D3DTS6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Heparan sulfate glucosamine 3-O-sulfotransferase 3B1;
DE EC=2.8.2.30 {ECO:0000269|PubMed:9988768};
DE AltName: Full=Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 3B1 {ECO:0000303|PubMed:9988768};
DE Short=3-OST-3B {ECO:0000303|PubMed:9988768};
DE Short=Heparan sulfate 3-O-sulfotransferase 3B1;
DE Short=h3-OST-3B;
GN Name=HS3ST3B1; Synonyms=3OST3B1, HS3ST3B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9988767; DOI=10.1074/jbc.274.8.5170;
RA Shworak N.W., Liu J., Petros L.M., Zhang L., Kobayashi M., Copeland N.G.,
RA Jenkins N.A., Rosenberg R.D.;
RT "Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase.
RT Isolation, characterization, and expression of human cDNAs and
RT identification of distinct genomic loci.";
RL J. Biol. Chem. 274:5170-5184(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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).
RN [5]
RP FUNCTION IN HSV-1 ENTRY.
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 [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9988768; DOI=10.1074/jbc.274.8.5185;
RA Liu J., Shworak N.W., Sinay P., Schwartz J.J., Zhang L., Fritze L.M.S.,
RA Rosenberg R.D.;
RT "Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms
RT reveals novel substrate specificities.";
RL J. Biol. Chem. 274:5185-5192(1999).
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 sulfate
CC (PubMed:10520990, PubMed:9988768). Catalyzes the O-sulfation of
CC glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2
CC (PubMed:10520990, PubMed:9988768). The substrate-specific O-sulfation
CC generates an enzyme-modified heparan sulfate which acts as a binding
CC receptor to Herpes simplex virus-1 (HSV-1) and permits its entry
CC (PubMed:10520990). Unlike HS3ST1/3-OST-1, does not convert non-
CC anticoagulant heparan sulfate to anticoagulant heparan sulfate
CC (PubMed:9988768). {ECO:0000269|PubMed:10520990,
CC ECO:0000269|PubMed:9988768}.
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:0000269|PubMed:9988768};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Most abundant in liver and placenta,
CC followed by heart and kidney. {ECO:0000269|PubMed:9988767}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; AF105377; AAD30209.1; -; mRNA.
DR EMBL; AK023723; BAG51220.1; -; mRNA.
DR EMBL; CH471108; EAW89953.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW89954.1; -; Genomic_DNA.
DR EMBL; BC063301; AAH63301.1; -; mRNA.
DR EMBL; BC069664; AAH69664.1; -; mRNA.
DR EMBL; BC069725; AAH69725.1; -; mRNA.
DR CCDS; CCDS11167.1; -.
DR RefSeq; NP_006032.1; NM_006041.2.
DR AlphaFoldDB; Q9Y662; -.
DR SMR; Q9Y662; -.
DR BioGRID; 115278; 16.
DR IntAct; Q9Y662; 1.
DR STRING; 9606.ENSP00000354213; -.
DR GlyGen; Q9Y662; 2 sites.
DR iPTMnet; Q9Y662; -.
DR PhosphoSitePlus; Q9Y662; -.
DR BioMuta; HS3ST3B1; -.
DR DMDM; 61214548; -.
DR MassIVE; Q9Y662; -.
DR PaxDb; Q9Y662; -.
DR PeptideAtlas; Q9Y662; -.
DR PRIDE; Q9Y662; -.
DR ProteomicsDB; 86605; -.
DR Antibodypedia; 25106; 39 antibodies from 17 providers.
DR DNASU; 9953; -.
DR Ensembl; ENST00000360954.3; ENSP00000354213.2; ENSG00000125430.9.
DR Ensembl; ENST00000466596.5; ENSP00000436078.1; ENSG00000125430.9.
DR GeneID; 9953; -.
DR KEGG; hsa:9953; -.
DR MANE-Select; ENST00000360954.3; ENSP00000354213.2; NM_006041.3; NP_006032.1.
DR UCSC; uc002goh.2; human.
DR CTD; 9953; -.
DR DisGeNET; 9953; -.
DR GeneCards; HS3ST3B1; -.
DR HGNC; HGNC:5198; HS3ST3B1.
DR HPA; ENSG00000125430; Tissue enhanced (liver, retina).
DR MIM; 604058; gene.
DR neXtProt; NX_Q9Y662; -.
DR OpenTargets; ENSG00000125430; -.
DR PharmGKB; PA29471; -.
DR VEuPathDB; HostDB:ENSG00000125430; -.
DR eggNOG; KOG3704; Eukaryota.
DR GeneTree; ENSGT00940000162568; -.
DR HOGENOM; CLU_017703_0_1_1; -.
DR InParanoid; Q9Y662; -.
DR OMA; HFFDHHY; -.
DR OrthoDB; 712400at2759; -.
DR PhylomeDB; Q9Y662; -.
DR TreeFam; TF350755; -.
DR BioCyc; MetaCyc:HS04884-MON; -.
DR BRENDA; 2.8.2.30; 2681.
DR PathwayCommons; Q9Y662; -.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR SignaLink; Q9Y662; -.
DR BioGRID-ORCS; 9953; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; HS3ST3B1; human.
DR GeneWiki; HS3ST3B1; -.
DR GenomeRNAi; 9953; -.
DR Pharos; Q9Y662; Tbio.
DR PRO; PR:Q9Y662; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y662; protein.
DR Bgee; ENSG00000125430; Expressed in tibia and 130 other tissues.
DR Genevisible; Q9Y662; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0008467; F:[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity; IDA:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; TAS:ProtInc.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; TAS:ProtInc.
DR GO; GO:0006477; P:protein sulfation; IEA:Ensembl.
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 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..390
FT /note="Heparan sulfate glucosamine 3-O-sulfotransferase
FT 3B1"
FT /id="PRO_0000085219"
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 74..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
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 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"
SQ SEQUENCE 390 AA; 43324 MW; 5C54C3E9836BC614 CRC64;
MGQRLSGGRS CLDVPGRLLP QPPPPPPPVR RKLALLFAML CVWLYMFLYS CAGSCAAAPG
LLLLGSGSRA AHDPPALATA PDGTPPRLPF RAPPATPLAS GKEMAEGAAS PEEQSPEVPD
SPSPISSFFS GSGSKQLPQA IIIGVKKGGT RALLEFLRVH PDVRAVGAEP HFFDRSYDKG
LAWYRDLMPR TLDGQITMEK TPSYFVTREA PARISAMSKD TKLIVVVRDP VTRAISDYTQ
TLSKRPDIPT FESLTFKNRT AGLIDTSWSA IQIGIYAKHL EHWLRHFPIR QMLFVSGERL
ISDPAGELGR VQDFLGLKRI ITDKHFYFNK TKGFPCLKKA EGSSRPHCLG KTKGRTHPEI
DREVVRRLRE FYRPFNLKFY QMTGHDFGWD
