ID S4R438_HUMAN Unreviewed; 815 AA.
AC S4R438;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
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 {ECO:0000313|Ensembl:ENSP00000475031.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000475031.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [2] {ECO:0000313|Ensembl:ENSP00000475031.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005093}.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004841}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000256|ARBA:ARBA00010420}.
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DR EMBL; AC022400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001317036.1; NM_001330107.1.
DR AlphaFoldDB; S4R438; -.
DR SMR; S4R438; -.
DR MassIVE; S4R438; -.
DR MaxQB; S4R438; -.
DR PeptideAtlas; S4R438; -.
DR DNASU; 8509; -.
DR Ensembl; ENST00000603027.5; ENSP00000475031.1; ENSG00000272916.5.
DR GeneID; 8509; -.
DR UCSC; uc057udp.1; human.
DR CTD; 8509; -.
DR GeneCards; ENSG00000272916; -.
DR VEuPathDB; HostDB:ENSG00000272916; -.
DR HOGENOM; CLU_011357_2_0_1; -.
DR OMA; GRQYPTM; -.
DR OrthoDB; 2913264at2759; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR BioGRID-ORCS; 8509; 18 hits in 1150 CRISPR screens.
DR ChiTaRS; NDST2; human.
DR GenomeRNAi; 8509; -.
DR Proteomes; UP000005640; Chromosome 10.
DR Bgee; ENSG00000272916; Expressed in primordial germ cell in gonad and 96 other cell types or tissues.
DR ExpressionAtlas; S4R438; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019213; F:deacetylase activity; IEA:UniProt.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR021930; Heparan_SO4_deacetylase.
DR InterPro; IPR037359; NST/OST.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR PANTHER; PTHR10605:SF53; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 2; 1.
DR PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR Pfam; PF12062; HSNSD; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..514
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 604..798
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT REGION 49..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 613
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 711
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
SQ SEQUENCE 815 AA; 92872 MW; FDF2DBF21A8503F5 CRC64;
MLQLWKVVRP ARQLELHRLI LLLIAFSLGS MGFLAYYVST SPKAKEPLPL PLGDCSSGGA
AGPGPARPPV PPRPPRPPET ARTEPVVLVF VESAYSQLGQ EIVAILESSR FRYSTELAPG
RGDMPTLTDN THGRYVLVIY ENLLKYVNLD AWSRELLDRY CVEYGVGIIG FFRAHEHSLL
SAQLKGFPLF LHSNLGLRDY QVNPSAPLLH LTRPSRLEPG PLPGDDWTIF QSNHSTYEPV
LLASLRPAEP AVPGPVLRRA RLPTVVQDLG LHDGIQRVLF GHGLSFWLHK LIFVDAVAYL
TGKRLCLDLD RYILVDIDDI FVGKEGTRMK VADVEALLTT QNKLRTLVPN FTFNLGFSGK
FYHTGTEEED AGDDMLLKHR KEFWWFPHMW SHMQPHLFHN RSVLADQMRL NKQFALEHGI
PTDLGYAVAP HHSGVYPIHT QLYEAWKSVW GIQVTSTEEY PHLRPARYRR GFIHNGIMVL
PRQTCGLFTH TIFYNEYPGG SRELDRSIRG GELFLTVLLN PISIFMTHLS NYGNDRLGLY
TFESLVRFLQ CWTRLRLQTL PPVPLAQKYF ELFPQERSPL WQNPCDDKRH KDIWSKEKTC
DRLPKFLIVG PQKTGTTAIH FFLSLHPAVT SSFPSPSTFE EIQFFNSPNY HKGIDWYMDF
FPVPSNASTD FLFEKSATYF DSEVVPRRGA ALLPRAKIIT VLTNPADRAY SWYQHQRAHG
DPVALNYTFY QVISASSQTP LALRSLQNRC LVPGYYSTHL QRWLTYYPSG QLLIVDGQEL
RTNPAASMES IQKFLGLMMI RDFGARDLKV VRLAV
//