ID G1KPE7_ANOCA Unreviewed; 876 AA.
AC G1KPE7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 57.
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:ENSACAP00000013762.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000013762.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000013762.3, ECO:0000313|Proteomes:UP000001646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000013762.3,
RC ECO:0000313|Proteomes:UP000001646};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000013762.3}
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; G1KPE7; -.
DR STRING; 28377.ENSACAP00000013762; -.
DR Ensembl; ENSACAT00000014043.4; ENSACAP00000013762.3; ENSACAG00000013822.4.
DR eggNOG; KOG3703; Eukaryota.
DR GeneTree; ENSGT00940000160665; -.
DR HOGENOM; CLU_011357_1_0_1; -.
DR InParanoid; G1KPE7; -.
DR TreeFam; TF313193; -.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR Proteomes; UP000001646; Chromosome 5.
DR Bgee; ENSACAG00000013822; Expressed in testis and 3 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:Ensembl.
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:UP000001646};
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 TRANSMEM 603..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 81..511
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 614..847
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT BINDING 710
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 811
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 827..831
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 812..822
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 876 AA; 101126 MW; D1F59FD48B4E32E0 CRC64;
MTYNMTFVVK LHRHFQRTVI LLATFCMVSI VISAYYLYNG YKQENELSEI NSEVECGDLP
ILQPYKITPW KTVKPTNPLR TDPVVLVFVE SQYSALGQDI VMILESSRFQ YHIEIASGKG
DLPVLIDKNK GKYALIIYEN ISKYVNMDSW NQGLLHKYCG EYGVGMIGFH KSSDNTLQTF
RLKGFPFYVH SNVGIKDCCI NPHSSLLHIT KSSKFDKGSL PGNDWTVFHI NHSAYEPVIF
AKVKAPENLP PPLVKNALHA TIIHDLGLHD GIQRVLFGNN LNFWLHKLIF IDAVSFLTGK
RLVLPLDRYI LVDIDDIFVG KEGTRMKAND VQALLNTQNL LRAQISNFTF NLGFSGKFYH
TGTAEEDEGD DLLLGSVDEF WWFPHMWSHM QPHLFHNESS LVEQMILNKK FALEHGIPTD
MGYAVAPHHS GVYPVHVQLY DAWKKVWNIK ITSTEEYPHL KPARYRKGFI HKNIMVLPRQ
TCGLFTHTIF YKEYPGGPKE LNKSIQGGEL FFTVVLNPIS IFMTHLSNYG NDQLGLYTFV
NLANFVQSWT NLKLQTLPPI QLAHKYFELF PEQKDPLWQN PCDDKRHRDI WSKEKTCDRL
PKFLLFNFLI LFAGTTALYL FLIMHPSIIS NSPSPKTFEE VQFFNRNNYH RGIDWYMDFF
PTPSNVTTDF LFEKSANYFH SEEAPKRAAS LIPKAKIITI LIDPSDRAYS WYQHQRSHKD
PTALKFTFYQ VITAGHHSSP DLKALQKKCL VPGWYATPYR KMAHLLPSLP DGQQLRNDPA
IVMDEVQKFL GVTPHYNYSE ALTFDSHKGF WCQLLEEGKT KCLGKSKGRK YPPMDSECRV
FLSSYYRDHN VELSKLLHKL GQPLPSWLRQ ELQKVR
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