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Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase 1) (NDST-1) (N-heparan sulfate sulfotransferase 1) (N-HSST 1) ([Heparan sulfate]-glucosamine N-sulfotransferase 1) (HSNST 1) [Includes: Heparan sulfate N-deacetylase 1 (EC 3.-.-.-); Heparan sulfate N-sulfotransferase 1 (EC 2.8.2.-)]

 NDST1_RAT               Reviewed;         882 AA.
Q02353;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
12-SEP-2018, entry version 135.
RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1;
EC=2.8.2.8;
AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 1;
Short=NDST-1;
AltName: Full=N-heparan sulfate sulfotransferase 1;
Short=N-HSST 1;
AltName: Full=[Heparan sulfate]-glucosamine N-sulfotransferase 1;
Short=HSNST 1;
Includes:
RecName: Full=Heparan sulfate N-deacetylase 1;
EC=3.-.-.-;
Includes:
RecName: Full=Heparan sulfate N-sulfotransferase 1;
EC=2.8.2.-;
Name=Ndst1; Synonyms=Hsst, Hsst1, Ndanst;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=1379236;
Hashimoto Y., Orellana A., Gil G., Hirschberg C.B.;
"Molecular cloning and expression of rat liver N-heparan sulfate
sulfotransferase.";
J. Biol. Chem. 267:15744-15750(1992).
[2]
CHARACTERIZATION.
PubMed=8483907; DOI=10.1073/pnas.90.9.3885;
Wei Z., Swiedler S.J., Ishihara M., Orellana A., Hirschberg C.B.;
"A single protein catalyzes both N-deacetylation and N-sulfation
during the biosynthesis of heparan sulfate.";
Proc. Natl. Acad. Sci. U.S.A. 90:3885-3889(1993).
[3]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-56; CYS-159;
CYS-486; CYS-586; CYS-601; CYS-751; CYS-818 AND CYS-828.
PubMed=9890952; DOI=10.1074/jbc.274.4.1966;
Wei Z., Swiedler S.J.;
"Functional analysis of conserved cysteines in heparan sulfate N-
deacetylase-N-sulfotransferases.";
J. Biol. Chem. 274:1966-1970(1999).
[4]
SUBCELLULAR LOCATION.
PubMed=11792394; DOI=10.1016/S0022-1759(01)00546-4;
Mura C.V., Becker M.I., Orellana A., Wolff D.;
"Immunopurification of Golgi vesicles by magnetic sorting.";
J. Immunol. Methods 260:263-271(2002).
-!- FUNCTION: Essential bifunctional enzyme that catalyzes both the N-
deacetylation and the N-sulfation of glucosamine (GlcNAc) of the
glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA
disaccharide repeating sugar backbone to make N-sulfated
heparosan, a prerequisite substrate for later modifications in
heparin biosynthesis. Plays a role in determining the extent and
pattern of sulfation of heparan sulfate. Compared to other NDST
enzymes, its presence is absolutely required. Participates in
biosynthesis of heparan sulfate that can ultimately serve as L-
selectin ligands, thereby playing a role in inflammatory response.
Required for the exosomal release of SDCBP, CD63 and syndecan.
{ECO:0000250|UniProtKB:P52848, ECO:0000250|UniProtKB:Q3UHN9}.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + [heparan
sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan
sulfate]-N-sulfoglucosamine.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=144 uM for K5 polysaccharide (for deacetylase activity)
{ECO:0000269|PubMed:9890952};
KM=160 uM for K5 polysaccharide (for sulfotransferase activity)
{ECO:0000269|PubMed:9890952};
Vmax=40 umol/min/mg enzyme with K5 polysaccharide as substrate
(for deacetylase activity) {ECO:0000269|PubMed:9890952};
Vmax=2104 umol/min/mg enzyme with K5 polysaccharide as substrate
(for sulfotransferase activity) {ECO:0000269|PubMed:9890952};
-!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
-!- PATHWAY: Glycan metabolism; heparin biosynthesis.
-!- SUBUNIT: Monomer. Interacts with EXT2.
{ECO:0000250|UniProtKB:P52848}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:11792394}; Single-pass type II membrane
protein {ECO:0000269|PubMed:11792394}.
-!- MISCELLANEOUS: The presence of 4 different heparan sulfate N-
deacetylase/N-sulfotransferase enzymes in mammals, as well as
differences in their enzyme activity suggest that some initiate
heparan sulfate modification/sulfation reactions, whereas other
later on fill in or extend already modified heparan sulfate
sequences.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M92042; AAA41701.1; -; mRNA.
PIR; A42855; A42855.
RefSeq; NP_077337.1; NM_024361.1.
RefSeq; XP_017456417.1; XM_017600928.1.
RefSeq; XP_017456418.1; XM_017600929.1.
RefSeq; XP_017456419.1; XM_017600930.1.
RefSeq; XP_017456420.1; XM_017600931.1.
RefSeq; XP_017456421.1; XM_017600932.1.
RefSeq; XP_017456422.1; XM_017600933.1.
UniGene; Rn.9705; -.
ProteinModelPortal; Q02353; -.
SMR; Q02353; -.
STRING; 10116.ENSRNOP00000025881; -.
PaxDb; Q02353; -.
PRIDE; Q02353; -.
Ensembl; ENSRNOT00000025881; ENSRNOP00000025881; ENSRNOG00000019014.
GeneID; 29633; -.
KEGG; rno:29633; -.
UCSC; RGD:69303; rat.
CTD; 3340; -.
RGD; 69303; Ndst1.
eggNOG; KOG3703; Eukaryota.
eggNOG; ENOG410XQN4; LUCA.
GeneTree; ENSGT00760000119023; -.
HOGENOM; HOG000008010; -.
HOVERGEN; HBG082011; -.
InParanoid; Q02353; -.
KO; K02576; -.
OMA; TNTIDYH; -.
OrthoDB; EOG091G02CP; -.
PhylomeDB; Q02353; -.
TreeFam; TF313193; -.
BRENDA; 2.8.2.8; 5301.
Reactome; R-RNO-2022928; HS-GAG biosynthesis.
SABIO-RK; Q02353; -.
UniPathway; UPA00756; -.
UniPathway; UPA00862; -.
PRO; PR:Q02353; -.
Proteomes; UP000002494; Chromosome 18.
Bgee; ENSRNOG00000019014; Expressed in 10 organ(s), highest expression level in lung.
Genevisible; Q02353; RN.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IEA:UniProtKB-EC.
GO; GO:0019213; F:deacetylase activity; IEA:Ensembl.
GO; GO:0042328; F:heparan sulfate N-acetylglucosaminyltransferase activity; IMP:UniProtKB.
GO; GO:0035904; P:aorta development; IEA:Ensembl.
GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
GO; GO:0048702; P:embryonic neurocranium morphogenesis; IEA:Ensembl.
GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IMP:UniProtKB.
GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IEA:Ensembl.
GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0030901; P:midbrain development; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
GO; GO:0006477; P:protein sulfation; IEA:Ensembl.
GO; GO:0007585; P:respiratory gaseous exchange; IEA:Ensembl.
InterPro; IPR021930; Heparan_SO4_deacetylase.
InterPro; IPR037359; NST/OST.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000863; Sulfotransferase_dom.
PANTHER; PTHR10605; PTHR10605; 1.
Pfam; PF12062; HSNSD; 1.
Pfam; PF00685; Sulfotransfer_1; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Golgi apparatus; Hydrolase; Inflammatory response;
Membrane; Multifunctional enzyme; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 882 Bifunctional heparan sulfate N-
deacetylase/N-sulfotransferase 1.
/FTId=PRO_0000085211.
TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.
TRANSMEM 18 39 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 40 882 Lumenal. {ECO:0000255}.
NP_BIND 614 618 PAPS. {ECO:0000250}.
NP_BIND 833 837 PAPS. {ECO:0000250}.
REGION 40 598 Heparan sulfate N-deacetylase 1.
REGION 599 882 Heparan sulfate N-sulfotransferase 1.
ACT_SITE 614 614 For sulfotransferase activity.
{ECO:0000250}.
BINDING 712 712 PAPS. {ECO:0000250}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 351 351 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 401 401 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 667 667 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 818 828 {ECO:0000250}.
MUTAGEN 56 56 C->A: Induces a reduction in
sulfotransferase activity but does not
affect deacetylase activity.
{ECO:0000269|PubMed:9890952}.
MUTAGEN 159 159 C->A: Induces a reduction in
sulfotransferase activity but increases
deacetylase activity.
{ECO:0000269|PubMed:9890952}.
MUTAGEN 486 486 C->A,V: Does not affect sulfotransferase
activity but increases deacetylase
activity. {ECO:0000269|PubMed:9890952}.
MUTAGEN 486 486 C->F: Does not affect sulfotransferase
activity but strongly decreases
deacetylase activity.
{ECO:0000269|PubMed:9890952}.
MUTAGEN 486 486 C->G: Does not affect sulfotransferase
activity but weakly affects deacetylase
activity. {ECO:0000269|PubMed:9890952}.
MUTAGEN 486 486 C->R,W: Does not affect sulfotransferase
activity but abolishes deacetylase
activity. {ECO:0000269|PubMed:9890952}.
MUTAGEN 586 586 C->A: Loss of deacetylase and
sulfotransferase activities.
{ECO:0000269|PubMed:9890952}.
MUTAGEN 601 601 C->A: Loss of sulfotransferase activity
but does not affect deacetylase activity.
{ECO:0000269|PubMed:9890952}.
MUTAGEN 751 751 C->A: Does not affect neither deacetylase
nor sulfotransferase activities.
{ECO:0000269|PubMed:9890952}.
MUTAGEN 818 818 C->A: Loss of sulfotransferase activity
but does not affect deacetylase activity.
{ECO:0000269|PubMed:9890952}.
MUTAGEN 828 828 C->A: Loss of sulfotransferase activity
but does not affect deacetylase activity.
{ECO:0000269|PubMed:9890952}.
SEQUENCE 882 AA; 100785 MW; F3AB9263EF6E4345 CRC64;
MPALACLRRL CRHLSPQAVL FLLFVFCLFS VFVSAYYLYG WNRGLEPSAD ASESDCGDPP
PVAPSRLLPI KPVQAVAPSR TDPLVLVFVE SLYSQLGQEV VAILESSRFK YRTEIAPGKG
DMPTLTDKGR GRFALIIYEN ILKYVNLDAW NRELLDKYCV AYGVGIIGFF KANENSLLSA
QLKGFPLFLH SNLGLKDCSI NPKSPLLYVT RPSEVEKGVL PGEDWTVFQS NHSTYEPVLL
AKTRSSESIP HLGADAGLHA ALHATVVQDL GLHDGIQRVL FGNNLNFWLH KLVFVDAVAF
LTGKRLSLPL DRYILVDIDD IFVGKEGTRM KVEDVKALFD TQNELRTHIP NFTFNLGYSG
KFFHTGTDAE DAGDDLLLSY VKEFWWFPHM WSHMQPHLFH NQSVLAEQMA LNKKFAVEHG
IPTDMGYAVA PHHSGVYPVH VQLYEAWKQV WNIRVTSTEE YPHLKPARYR RGFIHNGIMV
LPRQTCGLFT HTIFYNEYPG GSSELDKIIN GGELFLTVLL NPISVFMTHL SNYGNDRLGL
YTFKHLVRFL HSWTNLRLQT LPPVQLAQKY FQIFSEEKDP LWQDPCEDKR HKDIWSKEKT
CDRFPKLLII GPQKTGTTAL YLFLGMHPDL SSNYPSSETF EEIQFFNGHN YHKGIDWYME
FFPIPSNTTS DFYFEKSANY FDSEVAPRRA AALLPKAKVL TILINPADRA YSWYQHQRAH
DDPVALKYTF HEVITAGPDA SSKLRALQNR CLVPGWYATH IERWLSAFHA NQILVLDGKL
LRTEPAKVMD TVQKFLGVTS TVDYHKTLAF DPKKGFWCQL LEGGKTKCLG KSKGRKYPEM
DLDSRAFLKD YYRDHNIELS KLLYKMGQTL PTWLREDLQN TR


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