ID G3T1J1_LOXAF Unreviewed; 883 AA.
AC G3T1J1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
GN Name=NDST2 {ECO:0000313|Ensembl:ENSLAFP00000006956.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000006956.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000006956.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000006956.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000006956.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000006956.3};
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 -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000256|ARBA:ARBA00010420}.
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DR RefSeq; XP_003409114.1; XM_003409066.2.
DR RefSeq; XP_010587535.1; XM_010589233.1.
DR AlphaFoldDB; G3T1J1; -.
DR STRING; 9785.ENSLAFP00000006956; -.
DR Ensembl; ENSLAFT00000008299.3; ENSLAFP00000006956.3; ENSLAFG00000008298.3.
DR GeneID; 100653641; -.
DR KEGG; lav:100653641; -.
DR CTD; 8509; -.
DR eggNOG; KOG3703; Eukaryota.
DR GeneTree; ENSGT00940000156237; -.
DR HOGENOM; CLU_011357_2_0_1; -.
DR InParanoid; G3T1J1; -.
DR OMA; GRQYPTM; -.
DR OrthoDB; 2913264at2759; -.
DR TreeFam; TF313193; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
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:0102140; F:heparan sulfate N-deacetylase activity; IEA:Ensembl.
DR GO; GO:0050119; F:N-acetylglucosamine deacetylase activity; IEA:Ensembl.
DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IEA:Ensembl.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0002448; P:mast cell mediated immunity; IEA:Ensembl.
DR GO; GO:0002002; P:regulation of angiotensin levels in blood; IEA:Ensembl.
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:SF53; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 2; 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:UP000007646};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..514
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 604..853
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT REGION 49..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 613
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 711
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 816
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 832..836
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 817..827
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 883 AA; 100857 MW; 2F1B135E69A2FEEB CRC64;
MLQLWKVVRP ARQLELHRLI LLLIAFSLGS MGFLAYYVST SPKAKEPLPL PLGDCSSGGA
AGPGPARPPV PPRPPRPPET ARTEPVVLVF VESAYSQLGQ EIVAILESSR FRYSTELAPG
RGDMPTLTDH TRGRYVLVIY ENLLKYVNLD AWSRELLDRY CVEYGVGIIG FFRAHEHSLL
SAQLKGFPLF LHSNLGLRDY QVNPSAPLLH LTRPSRLEPG PLPGDDWTIF QSNHSTYEPV
LLASLQPAEL PVPGPVPRRT RLPTVVQDLG LHDGIQRVLF GHGLSFWLHK LVFVDAVGYL
TGKRLCLDLD RYILVDIDDI FVGKEGTRMK VADVEALLNT QNKLRTLVPN FTFNLGFSGK
FYHTGTEEED AGDAMLLKHR RDFWWFPHMW SHMQPHLFHN RSVLAGQMRL NRQFALEHGI
PTDLGYAVAP HHSGVYPIHT QLYEAWKSVW GIQVTSTEEY PHLRPARYRR GFIHNGIMVL
PRQTCGLFTH TIFYNEYPGG SRELDRSIRG GELFLTVLLN PISIFMTHLS NYGNDRLGLY
TFESLVRFLQ CWTRLRLQTL PPVPLARKYF ELFPQERSPL WQNPCDDKRH KDIWSKEKTC
DRLPKFLIVG PQKTGTTAIH FFLSLHPAVT SSFPSPSTFE EIQFFNSPNY HKGIDWYMDF
FPVPSNASTD FLFEKSATYF DSEVVPRRGA ALLPRAKIIT VLTNPADRAY SWYQHQRAHG
DPVALNYTFY QVISASSHAP LALRSLQSRC LIPGHYSTHL QRWLTYYPSG QLLIVDGQEL
RTNPAASMES IQKFLGITPF LNYTQTLRFD EDKGFWCQGL EGGKTRCLGK SKGRRYPDMD
SESRLFLTDF FRNHNLELSK LLSRLGQPVP LWLREELQRS SLS
//
