ID A0A3Q1G905_9TELE Unreviewed; 866 AA.
AC A0A3Q1G905;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 {ECO:0000256|ARBA:ARBA00039538};
DE EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
DE AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 1 {ECO:0000256|ARBA:ARBA00042929};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000026493.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000026493.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-
CC D-glucosaminyl-[heparan sulfate](n); Xref=Rhea:RHEA:21980, Rhea:RHEA-
CC COMP:9830, Rhea:RHEA-COMP:14602, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC ChEBI:CHEBI:140572; EC=2.8.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00036125};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21981;
CC Evidence={ECO:0000256|ARBA:ARBA00036125};
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, trans-Golgi network membrane
CC {ECO:0000256|ARBA:ARBA00037848}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00037848}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000256|ARBA:ARBA00010420}.
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DR AlphaFoldDB; A0A3Q1G905; -.
DR Ensembl; ENSAPOT00000003569.1; ENSAPOP00000026493.1; ENSAPOG00000010420.1.
DR GeneTree; ENSGT00940000157857; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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:SF30; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 1; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..522
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 612..838
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT REGION 51..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 621
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 696
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 801
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 817..821
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 802..812
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 866 AA; 98670 MW; 182C065B5A73C7E3 CRC64;
MLGCVTRLRR LVRLLPLQTS LLLLFLFCTV SVFISAYFLY GVKRELEPSG GGVSGAEGAS
ADTDDPRVTP SRLLPLRSVS GGPGVDPGGA RTDPVVLVFV ESQYSQLGQE IVAILESGRF
RYRTEISPGK GDMPTLTDKE RGRFTLVIYE NILKYVNLDA WNRELLDKYC VEYGVGIIGF
FKANENSLLS AQLKGFPLFL HSNLGLKDCT VNPKSPLLFI TRSGQPLPGP LPGDDWTVFQ
SNHSTYEPVL LAKTQSAESV ASMGQNAALL PSVVQDLGLH DGIQRVLFGN NLVFWLHKLV
FVDAVAFLTG KRLSLSLERY ILVDIDDIFV GKEGTRMKVP DVKALLETQR ELRTHVPNFT
FNLGFSGKFF HAGSDEEDLG DDLLLSYVKD FWWFPHMWSH MQPHLFHNQS VLAEQMLLNK
KFAMEHGIPT NMGYAVAPHH SGVYPVHMQL YDAWKKVWGI KVTSTEEYPH LKPARFRRGF
IHSGISVLPR QTCGLFTHTI FYKDYPGSPN ELDKLINGGE LFLTVLLNPI SIFMTHLSNY
GNDRLGLYTF KSLVMFIQTW TNLKMQTLPP IQLAQKYFSL FPSERDPLWQ DPCEDKRHKD
IWSKEKTCDR FPKLLVIGPQ KTGTTALYLF LGMHPDLTSN YPNFHSHHVI FFFSYYYFEK
SANYFDSEVA AQRAAALLPK AKIVTILINP ADRAYSWYQH QRAHDDPVAL KYSFHDVITA
GHNAPVKLRV LQNRCLVPGW YAIHLERWLN FYHSSQLLVL DGQMLKTEPA SVMDKIQKFL
GLANIINYHK ILAFDPKKGF WCQLLEGGKT KCLGKSKGRR YPDMDPESQG FLREYYRDHN
IELSKLLYRM GQPLPSWLRE ELVHTR
//
