ID A0A452ESG6_CAPHI Unreviewed; 887 AA.
AC A0A452ESG6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
GN Name=NDST3 {ECO:0000313|Ensembl:ENSCHIP00000015142.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000015142.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000015142.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000015142.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 EMBL; LWLT01000006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005681335.2; XM_005681278.2.
DR RefSeq; XP_013819912.2; XM_013964458.2.
DR AlphaFoldDB; A0A452ESG6; -.
DR STRING; 9925.ENSCHIP00000015142; -.
DR Ensembl; ENSCHIT00000022944.1; ENSCHIP00000015142.1; ENSCHIG00000015901.1.
DR GeneID; 102171771; -.
DR KEGG; chx:102171771; -.
DR CTD; 9348; -.
DR GeneTree; ENSGT00940000160665; -.
DR OMA; PALIDKN; -.
DR OrthoDB; 2913264at2759; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000291000; Chromosome 6.
DR Bgee; ENSCHIG00000015901; Expressed in cerebellum and 12 other cell types or tissues.
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: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 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..520
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 610..859
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 619
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 717
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 822
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 838..842
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 823..833
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 887 AA; 102431 MW; 807A13934785BEE3 CRC64;
MVLLLEQSEE SICNMSFIMK LHRHFQRTVI LLATFCMVSI IISAYYLYSG YKQENELSEM
ALEVDCGDLQ HLPYRLMDVK PAKLSDASRT DTTVLVFVES QYSSLGQDII MILESSRFQY
HIEIAPGKGD LPALTEKSRG KYSLIIYENI LKYIHMDAWN RSLLDKYCVE YGVGVIGFHR
TSEKSPQSFQ LKGFPFSVYG SLAVKDCCIN PHSPLLHVTK SSKLEKGSLP GTDWTVFHIN
HSAYQPVIFA KVKTPENLSP PISKGAFYAT VIHDLGLHDG IQRVLFGNNL NFWLHKLIFI
DAVSFLSGKR LTLSLDRYIL VDIDDIFVGK EGTRMNTNDV KALLDTQNLL RAQITNFTFN
LGFSGKFYHT GTEEEDEGDD RLLGSVDEFW WFPHMWSHMQ PHLFHNESSL VEQMILNKKF
ALEHGIPTDM GYAVAPHHSG VYPVHVQLYE AWKKVWNIRI TSTEEYPHLK PARYRRGFIH
KNIMVLPRQT CGLFTHTIFY KEYPGGPKEL DKSIQGGELF FTVVLNPISI FMTHLSNYGN
DRLGLYTFVN LANFVQSWTN LRLQTLPPVQ LAHKYFELFP DQKDPLWQNP CDDKRHRDIW
SKEKTCDRLP KFLVIGPQKT GTTALYLFLV MHPSILSNSP SPKTFEEVQF FNRNNYHRGI
DWYMDFFPVP SNVTTDFLFE KSANYFHSEE APKRAASLVP KAKIITILID PSDRAYSWYQ
HQRSHEDPAA LKFSFYEVIS AGPRAPSELR ALQKRCLVPG WYASHIERWL VYFPPFQLLI
IDGQQLRTDP ATVMDEVQKF LGVSPHYNYS EALTFDSHKG FWCQLLEEGK TKCLGKSKGR
KYPPMDPDSR AFLSSYYRDH NVELSKLLHR LGQPLPSWLR QELQKVR
//
