ID A8K0V5_HUMAN Unreviewed; 872 AA.
AC A8K0V5;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
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|EMBL:BAF82359.1};
RN [1] {ECO:0000313|EMBL:BAF82359.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Amygdala {ECO:0000313|EMBL:BAF82359.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; AK289670; BAF82359.1; -; mRNA.
DR RefSeq; NP_072091.1; NM_022569.2.
DR AlphaFoldDB; A8K0V5; -.
DR PeptideAtlas; A8K0V5; -.
DR DNASU; 64579; -.
DR GeneID; 64579; -.
DR KEGG; hsa:64579; -.
DR CTD; 64579; -.
DR OrthoDB; 2913264at2759; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR BioGRID-ORCS; 64579; 7 hits in 1138 CRISPR screens.
DR GenomeRNAi; 64579; -.
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:SF45; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 4; 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 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR637359-3};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:BAF82359.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..505
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 595..844
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 604
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 702
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 807
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 823..827
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 808..818
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 872 AA; 100689 MW; 9C4E2DD45D963C74 CRC64;
MNLIVKLRRS FRTLIVLLAT FCLVSIVISA YFLYSGYKQE MTLIETTAEA ECTDIKILPY
RSMELKTVKP IDTSKTDPTV LLFVESQYSQ LGQDIIAILE SSRFQYHMVI APGKGDIPPL
TDNGKGKYTL VIYENILKYV SMDSWNRELL EKYCVEYSVS IIGFHKANEN SLPSTQLKGF
PLNLFNNLAL KDCFVNPQSP LLHITKAPKV EKGPLPGEDW TIFQYNHSTY QPVLLTELQT
EKSLSSLSSK TLFATVIQDL GLHDGIQRVL FGNNLNFWLH KLIFIDAISF LSGKRLTLSL
DRYILVDIDD IFVGKEGTRM NVKDVKALLE TQSLLRTQVA NFTFNLGFSG KFYHTGTEEE
DEGDDLLLRS VDEFWWFPHM WSHMQPHLFH NESSLVEQMI LNKEFALEHG IPINMGYAVA
PHHSGVYPVH IQLYAAWKKV WGIQVTSTEE YPHLKPARYR KGFIHNSIMV LPRQTCGLFT
HTIFYKEYPG GPQELDKSIR GGELFLTILL NPISIFMTHL SNYGNDRLGL YTFVNLVNFV
QSWTNLKLQT LPPVQLAHQY FELFPEQKDP LWQNPCDDKR HKDIWSREKT CDHLPKFLVI
GPQKTGTTAL YLFLLMHPSI ISNLPSPKTF EEVQFFNGNN YHKGIDWYMD FFPTPSNTTS
DFLFEKSANY FHSEEAPRRA ASLVPKAKII TILIDPSDRA YSWYQHQRSH EDPAALRFNF
YEVISTGHWA PSDLKTLQRR CLVPGWYAVH IERWLTYFAT SQLLIIDGQQ LRSDPATVMD
EVQKFLGVTP RYNYSEALTF DPQKGFWCQL LEGGKTKCLG KSKGRKYPPM DPESRTFLSN
YYRDHNVELS KLLHRLGQPL PSWLRQELQK VR
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