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Database: UniProt
Entry: D3YXE5_MOUSE
LinkDB: D3YXE5_MOUSE
Original site: D3YXE5_MOUSE 
ID   D3YXE5_MOUSE            Unreviewed;       458 AA.
AC   D3YXE5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Sulfotransferase {ECO:0000256|RuleBase:RU361155};
DE            EC=2.8.2.- {ECO:0000256|RuleBase:RU361155};
GN   Name=Ndst3 {ECO:0000313|Ensembl:ENSMUSP00000120623.2,
GN   ECO:0000313|MGI:MGI:1932544};
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 {ECO:0000313|Ensembl:ENSMUSP00000120623.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000120623.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000120623.2,
RC   ECO:0000313|Proteomes:UP000000589};
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   [2] {ECO:0000313|Ensembl:ENSMUSP00000120623.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000120623.2};
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   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004323}.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC       {ECO:0000256|ARBA:ARBA00010420}.
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DR   RefSeq; NP_001280611.1; NM_001293682.1.
DR   RefSeq; XP_006502439.1; XM_006502376.3.
DR   ProteomicsDB; 332458; -.
DR   Antibodypedia; 26593; 146 antibodies from 18 providers.
DR   DNASU; 83398; -.
DR   Ensembl; ENSMUST00000124803.8; ENSMUSP00000122617.2; ENSMUSG00000027977.16.
DR   Ensembl; ENSMUST00000132112.8; ENSMUSP00000120623.2; ENSMUSG00000027977.16.
DR   GeneID; 83398; -.
DR   UCSC; uc008rfo.1; mouse.
DR   AGR; MGI:1932544; -.
DR   CTD; 9348; -.
DR   MGI; MGI:1932544; Ndst3.
DR   VEuPathDB; HostDB:ENSMUSG00000027977; -.
DR   GeneTree; ENSGT00940000160665; -.
DR   HOGENOM; CLU_011357_0_1_1; -.
DR   OrthoDB; 2913264at2759; -.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   BioGRID-ORCS; 83398; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Ndst3; mouse.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000027977; Expressed in cerebellar cortex and 61 other cell types or tissues.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:SF29; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 3; 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   Disulfide bond {ECO:0000256|PIRSR:PIRSR637359-3};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transferase {ECO:0000256|RuleBase:RU361155}.
FT   DOMAIN          1..91
FT                   /note="Heparan sulphate-N-deacetylase"
FT                   /evidence="ECO:0000259|Pfam:PF12062"
FT   DOMAIN          181..429
FT                   /note="Sulfotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00685"
FT   ACT_SITE        190
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT   BINDING         288
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         393
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   BINDING         409..413
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT   DISULFID        394..404
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ   SEQUENCE   458 AA;  53495 MW;  628B9D11DEF24DA4 CRC64;
     MGYAVSPHHS GVYPVHVQLY EAWKKVWNIK ITSTEEYPHL KPARYRRGFI HKNIMVLPRQ
     TCGLFTHTIF YKEYPGGPRE LDKSIHGGEL FFTVVLNPIS IFMTHLSNYG NDRLGLYTFV
     NLANFVQTWT NLRLQTLPPA QLAHKYFELF PDQKDPLWQN PCDDKRHRDI WSKEKTCDRL
     PKFLVIGPQK TGTTALCLFL IMHPSILSNS PSPKSFEEVQ FFNRNNYHRG IDWYMDFFPV
     PSNVTTDFLF EKSANYFHSE DAPKRAASLV PKAKIITILI DPSDRAYSWY QHQRSHEDPA
     ALKFSFYEVI SAGPNAPWEL RTLQKRCLVP GWYANHIERW LVYFPPFQLL IIDGQQLRTT
     PATVMDEVQK FLGVSPHYNY SEALTFDSHK GFWCQLLEEG KTKCLGKSKG RKYPPMDSDS
     RAFLSSYYRD HNVELSKLLH RLGQPLPSWL RQELQKVR
//
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