ID H0Z942_TAEGU Unreviewed; 877 AA.
AC H0Z942;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 72.
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:ENSTGUP00000007095.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000007095.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000007095.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000007095.2}
RP IDENTIFICATION.
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 AlphaFoldDB; H0Z942; -.
DR STRING; 59729.ENSTGUP00000020256; -.
DR Ensembl; ENSTGUT00000007164.2; ENSTGUP00000007095.2; ENSTGUG00000006860.2.
DR GeneTree; ENSGT00940000156237; -.
DR HOGENOM; CLU_011357_2_0_1; -.
DR TreeFam; TF313193; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000007754; Chromosome 6.
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: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:UP000007754};
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 80..508
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 598..848
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 607
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 705
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 810
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 826..830
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 811..821
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 877 AA; 101322 MW; 5C1F163628392055 CRC64;
MIQLWKVVRH VRQLELHRLI LLLIAFSLIS MCILAYYVTN SPKIKEPPPL PFSDCSNQHR
ILIPPQASWR LTKSVDTSRT DPVVLVFVES IYSQLGQEIV AILESSRFKY RTEIAPGKGD
MPTLTDKDRG RYALIIYENI LKYVNLDAWN RELLDKYCVE YGVGIIGFFK ANENSLLSAQ
LKGFPLFLHS NLGLRDYHIN PSAPLLYVTR ANEVEQGPLP GDDWTVFQSN HSTYEPVLLA
STKSSESIPH LATHKALHAT VMQDLGLHDG IQRVLFGNNL NFWLHKLIFV DAIAYLTGKR
LCLTLDRYIL VDIDDIFVGK EGTRMKVSDA LLSTQNKLRT LVPNFTFNLG FSGKFYHTGT
DEEDEGDDML LKHRKEFWWF PHMWSHMQPH LFHNVTVLAE QMKLNKQFAV EHGIPTDLGY
AVAPHHSGVY PVHTQLYEAW KSVWSIQVTS TEEYPHLRPA RYRRGFIHNG IMVLPRQTCG
LFTHTIFYNE YPGGSKELDK SIRGGELFLT VLLNPISIFM THLSNYGNDR LGLYTFESLV
KFVQCWTNLR LQTLPPVQLA KKYFEIFPQE KNPLWQNPCD DKRHKDIWSK EKTCDRLPKF
LIVGPQKTGT TAVHFFLTMH PAVTSNFPSP STFEEIQFFN GPNYHKGIDW YMDFFPIPSN
ASTDFMFEKS ANYFDTEVVP KRGAALLPRA KIITVLINPA DRAYSWYQHQ RAHNDPVALN
YTFYQVISAK SQAPQELRNL QSRCLFPGWY STHLERWLTY YPSGQLLIVD GQELRHNPAS
VMDNIQKFLG VTPLFNYTQA LRFDEAKGFW CQLLDGGKTK CLGKSKGRKY PDMDSLSRLF
LRDFYREHNI ELSKLMNRLG QPLPTWLREE LQNSSWS
//
