H6ST3_MOUSE
ID H6ST3_MOUSE Reviewed; 470 AA.
AC Q9QYK4; Q148Q1;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase 3;
DE Short=HS6ST-3;
DE Short=mHS6ST-3;
DE EC=2.8.2.-;
GN Name=Hs6st3;
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], BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10644753; DOI=10.1074/jbc.275.4.2859;
RA Habuchi H., Tanaka M., Habuchi O., Yoshida K., Suzuki H., Ban K.,
RA Kimata K.;
RT "The occurrence of three isoforms of heparan sulfate 6-O-sulfotransferase
RT having different specificities for hexuronic acid adjacent to the targeted
RT N-sulfoglucosamine.";
RL J. Biol. Chem. 275:2859-2868(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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: 6-O-sulfation enzyme which catalyzes the transfer of sulfate
CC from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the
CC N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) +
CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:56604, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:14621, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC ChEBI:CHEBI:140604;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for CDSNS-heparin {ECO:0000269|PubMed:10644753};
CC KM=20 uM for NS-heparosan {ECO:0000269|PubMed:10644753};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10644753}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family. {ECO:0000305}.
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DR EMBL; AB024567; BAA89249.1; -; mRNA.
DR EMBL; BC118035; AAI18036.1; -; mRNA.
DR CCDS; CCDS27339.1; -.
DR RefSeq; NP_056635.2; NM_015820.3.
DR AlphaFoldDB; Q9QYK4; -.
DR SMR; Q9QYK4; -.
DR STRING; 10090.ENSMUSP00000070394; -.
DR GlyGen; Q9QYK4; 6 sites.
DR iPTMnet; Q9QYK4; -.
DR PhosphoSitePlus; Q9QYK4; -.
DR PaxDb; Q9QYK4; -.
DR PRIDE; Q9QYK4; -.
DR ProteomicsDB; 270919; -.
DR Antibodypedia; 24893; 51 antibodies from 19 providers.
DR DNASU; 50787; -.
DR Ensembl; ENSMUST00000065904; ENSMUSP00000070394; ENSMUSG00000053465.
DR GeneID; 50787; -.
DR KEGG; mmu:50787; -.
DR UCSC; uc007uzn.2; mouse.
DR CTD; 266722; -.
DR MGI; MGI:1354960; Hs6st3.
DR VEuPathDB; HostDB:ENSMUSG00000053465; -.
DR eggNOG; KOG3955; Eukaryota.
DR GeneTree; ENSGT00950000183071; -.
DR HOGENOM; CLU_027877_1_0_1; -.
DR InParanoid; Q9QYK4; -.
DR OMA; QRKTQYM; -.
DR OrthoDB; 1167623at2759; -.
DR PhylomeDB; Q9QYK4; -.
DR TreeFam; TF312835; -.
DR Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR SABIO-RK; Q9QYK4; -.
DR BioGRID-ORCS; 50787; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Hs6st3; mouse.
DR PRO; PR:Q9QYK4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9QYK4; protein.
DR Bgee; ENSMUSG00000053465; Expressed in cortical layer I and 46 other tissues.
DR Genevisible; Q9QYK4; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IDA:MGI.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IDA:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR010635; Heparan_SO4-6-sulfoTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR12812; PTHR12812; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="Heparan-sulfate 6-O-sulfotransferase 3"
FT /id="PRO_0000190810"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..470
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 36..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..113
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 151..159
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 181..182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 244
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 252
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 376..378
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 382..383
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 16
FT /note="L -> F (in Ref. 1; BAA89249)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 55037 MW; 195B376684A4328D CRC64;
MDERFNKWLL TPVLTLLFVV IMYQYVSPSC TSSCTNFGEQ LRSGEARPPA VPSPARRAQA
PLDEWERRPQ LPPPPRGPPE GSRGVAAPED EDEDPGDPEE EEEEEEEEPD PEAPENGSLP
RFVPRFNFTL KDLTRFVDFN IKGRDVIVFL HIQKTGGTTF GRHLVKNIRL EQPCSCKAGQ
KKCTCHRPGK KETWLFSRFS TGWSCGLHAD WTELTNCVPA IMEKKDCPRN HSHTRNFYYI
TMLRDPVSRY LSEWKHVQRG ATWKTSLHMC DGRSPTPDEL PTCYPGDDWS GVSLREFMDC
SYNLANNRQV RMLADLSLVG CYNLTFMNES ERNTILLQSA KNNLKNMAFF GLTEFQRKTQ
FLFERTFNLK FISPFTQFNI TRASNVDIND GARQHIEELN FLDMQLYEYA KDLFQQRYHH
TKQLEHQRDR QKRREERRLQ REHRAHRWPK EDRAMEGTVT EDYNSQVVRW
