ID A0A091E0C2_FUKDA Unreviewed; 811 AA.
AC A0A091E0C2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
GN ORFNames=H920_01804 {ECO:0000313|EMBL:KFO36762.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO36762.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO36762.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO36762.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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 -!- 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 EMBL; KN121273; KFO36762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091E0C2; -.
DR STRING; 885580.ENSFDAP00000023239; -.
DR eggNOG; KOG3703; Eukaryota.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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:UP000028990};
KW Transferase {ECO:0000313|EMBL:KFO36762.1}.
FT DOMAIN 14..444
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 534..782
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 543
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 641
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 746
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 762..766
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 747..757
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 811 AA; 93803 MW; 2B5775508FB9FC07 CRC64;
MEVKTTKLFD ASRTDPIVLV FVESQYSALG QDIVMILESS RFQYHIEIAP GKGDLPALID
KTKGKYILII YENILKYINM DSWNRSLLDK YCVEYGVGVI GFHKTSEKSL QSFQLKGFPF
SIYGNLAVRD CCINSHSPLL RVTKSSKVEK GSLPGTDWTV FQINHSAYQP VIFAKVKTPE
NFSPPISKGA FYATIIHDLG LHDGIQRVLF GNNLNFWLHK LIFVDAISFL SRKRLTLSLD
RYILVDIDDI FVGKEGTRMN TNDVKALLDT QNLLRAQITN FTFNLGFSGK FYHTGTEEED
EGDDCLLGSV DEFWWFPHMW SHMQPHLFHN ESSLVEQMIL NKKFALEHGI PTDMGYAVAP
HHSGVYPVHV QLYEAWKKVW NIKITSTEEY PHLKPARYRR GFIHKNIMVL PRQTCGLFTH
TIFYKEYPGG PKELDKSIQG GELFFTVVLN PISIFMTHLS NYGNDRLGLY TFVNLANFVQ
TWTNLRLKTL PPVQLAQKYF ELFPDQKDPL WQNPCDDKRH RDIWSKEKTC DRLPKFLVIG
PQKTGTTALY LFLVMHPSIL SNSPSPKTFE EVQFFNRNNY HRGIDWYMDF FPVPSNVTTD
FLFEKSANYF HSEEAPKRAA SLVPKAKIIT ILIDPSDRAY SWYQHQRSHE DPAALKFSFY
EVISARPHAP SELRTLQKRC LVPGWYASHI ERWLVYFPPF QLLIIDGQQL RTDPATVMDE
VQKFLGVSPH YNYSEALTFD SHKGFWCQLL EEGKTKCLGK SKGRKYPPMD SDSRAFLSSY
YRDHNVELSK LLHKLGQPLP SWLRQELQKV R
//
