H6ST3_HUMAN
ID H6ST3_HUMAN Reviewed; 471 AA.
AC Q8IZP7; Q5W0L0; Q68CW6;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Heparan-sulfate 6-O-sulfotransferase 3;
DE Short=HS6ST-3;
DE EC=2.8.2.-;
GN Name=HS6ST3;
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].
RC TISSUE=Brain;
RA Bonner T.I., Ferraren D.O., Detera-Wadleigh S.;
RT "The coding sequence of HS6ST3 spans an intron of 741 kb.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-471.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 6 family. {ECO:0000305}.
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DR EMBL; AF539426; AAN33062.1; -; mRNA.
DR EMBL; AL138816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR749677; CAH18468.1; -; mRNA.
DR CCDS; CCDS9481.1; -.
DR RefSeq; NP_703157.2; NM_153456.3.
DR AlphaFoldDB; Q8IZP7; -.
DR SMR; Q8IZP7; -.
DR BioGRID; 129329; 26.
DR IntAct; Q8IZP7; 1.
DR STRING; 9606.ENSP00000365895; -.
DR GlyGen; Q8IZP7; 6 sites.
DR iPTMnet; Q8IZP7; -.
DR PhosphoSitePlus; Q8IZP7; -.
DR BioMuta; HS6ST3; -.
DR DMDM; 116242508; -.
DR MassIVE; Q8IZP7; -.
DR MaxQB; Q8IZP7; -.
DR PaxDb; Q8IZP7; -.
DR PeptideAtlas; Q8IZP7; -.
DR PRIDE; Q8IZP7; -.
DR ProteomicsDB; 71394; -.
DR Antibodypedia; 24893; 51 antibodies from 19 providers.
DR DNASU; 266722; -.
DR Ensembl; ENST00000376705.4; ENSP00000365895.2; ENSG00000185352.9.
DR GeneID; 266722; -.
DR KEGG; hsa:266722; -.
DR MANE-Select; ENST00000376705.4; ENSP00000365895.2; NM_153456.4; NP_703157.2.
DR UCSC; uc001vmw.4; human.
DR CTD; 266722; -.
DR DisGeNET; 266722; -.
DR GeneCards; HS6ST3; -.
DR HGNC; HGNC:19134; HS6ST3.
DR HPA; ENSG00000185352; Tissue enhanced (brain).
DR MIM; 609401; gene.
DR neXtProt; NX_Q8IZP7; -.
DR OpenTargets; ENSG00000185352; -.
DR PharmGKB; PA134879312; -.
DR VEuPathDB; HostDB:ENSG00000185352; -.
DR eggNOG; KOG3955; Eukaryota.
DR GeneTree; ENSGT00950000183071; -.
DR HOGENOM; CLU_027877_1_0_1; -.
DR InParanoid; Q8IZP7; -.
DR OMA; QRKTQYM; -.
DR OrthoDB; 1167623at2759; -.
DR PhylomeDB; Q8IZP7; -.
DR TreeFam; TF312835; -.
DR BioCyc; MetaCyc:MON-15787; -.
DR PathwayCommons; Q8IZP7; -.
DR Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR SignaLink; Q8IZP7; -.
DR BioGRID-ORCS; 266722; 16 hits in 1066 CRISPR screens.
DR ChiTaRS; HS6ST3; human.
DR GenomeRNAi; 266722; -.
DR Pharos; Q8IZP7; Tdark.
DR PRO; PR:Q8IZP7; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q8IZP7; protein.
DR Bgee; ENSG00000185352; Expressed in lateral nuclear group of thalamus and 144 other tissues.
DR ExpressionAtlas; Q8IZP7; baseline and differential.
DR Genevisible; Q8IZP7; HS.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017095; F:heparan sulfate 6-O-sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0015015; P:heparan sulfate proteoglycan biosynthetic process, enzymatic modification; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..471
FT /note="Heparan-sulfate 6-O-sulfotransferase 3"
FT /id="PRO_0000190809"
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..471
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 39..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..114
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 209
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 152..160
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 182..183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 245
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 253
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 377..379
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT BINDING 383..384
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250|UniProtKB:A0MGZ7"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 265
FT /note="K -> R (in dbSNP:rs9516771)"
FT /id="VAR_028159"
FT CONFLICT 37
FT /note="F -> L (in Ref. 1; AAN33062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 54844 MW; 4A5F4DEA26FC7302 CRC64;
MDERFNKWLL TPVLTLLFVV IMYQYVSPSC TSSCTNFGEQ PRAGEAGPPA VPGPARRAQA
PPEEWERRPQ LPPPPRGPPE GPRGAAAPEE EDEEPGDPRE GEEEEEEDEP DPEAPENGSL
PRFVPRFNFS LKDLTRFVDF NIKGRDVIVF LHIQKTGGTT FGRHLVKNIR LEQPCSCKAG
QKKCTCHRPG KKETWLFSRF STGWSCGLHA DWTELTNCVP AIMEKKDCPR NHSHTRNFYY
ITMLRDPVSR YLSEWKHVQR GATWKTSLHM CDGRSPTPDE LPTCYPGDDW SGVSLREFMD
CTYNLANNRQ VRMLADLSLV GCYNLTFMNE SERNTILLQS AKNNLKNMAF FGLTEFQRKT
QFLFERTFNL KFISPFTQFN ITRASNVEIN EGARQRIEDL NFLDMQLYEY AKDLFQQRYH
HTKQLEHQRD RQKRREERRL QREHRDHQWP KEDGAAEGTV TEDYNSQVVR W
