ID G3Q1R7_GASAC Unreviewed; 886 AA.
AC G3Q1R7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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 Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000023815.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000023815.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000023815.1}
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; G3Q1R7; -.
DR STRING; 69293.ENSGACP00000023815; -.
DR Ensembl; ENSGACT00000023862.1; ENSGACP00000023815.1; ENSGACG00000018023.1.
DR eggNOG; KOG3703; Eukaryota.
DR GeneTree; ENSGT00940000157857; -.
DR InParanoid; G3Q1R7; -.
DR OMA; PALIDKN; -.
DR TreeFam; TF313193; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000018023; Expressed in liver and 12 other cell types or tissues.
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:1904888; P:cranial skeletal system development; IEA:Ensembl.
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:UP000007635};
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 88..519
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 609..858
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 618
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 716
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 821
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 837..841
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 822..832
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 886 AA; 101038 MW; C989F71FEC5A65FD CRC64;
MLGCVTRLRR LVRLLPLQTS LLLLFLFCTV SVFISAYFLY GVKRELEPSG GGVSGAEGAS
ADSDDPRVTP SRLLPLRGVP GAPESPAEPV CLKIIYCIYK FFNTKMLTLV HHNSFTAYLR
SKFILGNGPC GPLNSNKKNT LKHCLISLEL VNTPHFFLEL LKTGCHICAK LSLLGFLLLA
NENSLLSAQL KGFPLFLHSN LGLKDCTVNP KSPLLFITRS GQPLPGPLPG DDWTVFQSNH
STYEPVLLAK TQSAESIASM GQNAALLPSV VQDLGLHDGI QRVLFGNNLV FWLHKLVFVD
AVAFLTGKRL SLSLERYVLV DVDDIFVGKE GTRMKVPDVK ALLETQRELR THVPNFTFNL
GFSGKFFHAG SDEEDLGDDL LLSFVKEFWW FPHMWSHMQP HLFHNQSVLA EQMLLNKKFA
IEHGIPTNMG YAVAPHHSGV YPVHIQLYDA WKKVWGIKVT STEEYPHLKP ARFRRGFIHS
GISVLPRQTC GLFTHTIFYK DYPGSPNELD KLINGGELFQ TVLLNPISIF MTHLSNYGND
RLGLYTFKSL VMFLQTWTNL KMQTLPPVQL AQKYFSLFPS ERDPLWQDPC EDKRHKDIWS
KEKTCDRFPK LLVIGPQKTG TTALYLFLGM HPDLTSNYPS KETFEEIQFF NGHNYHRGID
WYMEYFPLPS NTSSDYYFEK SANYFDSEVA AQRAAALLPK AKIITILINP ADRAYSWYQH
QRAHDDPVAL KYSFHDVITA GHNAPVRLRV LQNRCLVPGW YAIHLDRWLN FYHSSQLLVL
DGQMLKTEPA SIMDKIQKYL SLVNVINYHK ILAFDPKKGF WCQLLEGGKT KCLGKSKGRR
YPDMDPESQT FLREYYRDHN IELSKLLYKM GQPLPSWLRE ELVHTR
//
