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Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase) (Sulfateless) [Includes: Heparan sulfate N-deacetylase (EC 3.-.-.-); Heparan sulfate N-sulfotransferase (EC 2.8.2.-)]

 NDST_DROME              Reviewed;        1048 AA.
Q9V3L1;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
20-DEC-2017, entry version 135.
RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase;
EC=2.8.2.8;
AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase;
AltName: Full=Sulfateless;
Includes:
RecName: Full=Heparan sulfate N-deacetylase;
EC=3.-.-.-;
Includes:
RecName: Full=Heparan sulfate N-sulfotransferase;
EC=2.8.2.-;
Name=sfl; ORFNames=CG8339;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION IN WG SIGNALING.
PubMed=10421372; DOI=10.1038/22343;
Lin X., Perrimon N.;
"Dally cooperates with Drosophila Frizzled 2 to transduce Wingless
signalling.";
Nature 400:281-284(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
FUNCTION IN FGF RECEPTOR SIGNALING.
PubMed=10433902;
Lin X., Buff E.M., Perrimon N., Michelson A.M.;
"Heparan sulfate proteoglycans are essential for FGF receptor
signaling during Drosophila embryonic development.";
Development 126:3715-3723(1999).
[5]
FUNCTION.
PubMed=10644674; DOI=10.1074/jbc.275.4.2269;
Toyoda H., Kinoshita-Toyoda A., Selleck S.B.;
"Structural analysis of glycosaminoglycans in Drosophila and
Caenorhabditis elegans and demonstration that tout-velu, a Drosophila
gene related to EXT tumor suppressors, affects heparan sulfate in
vivo.";
J. Biol. Chem. 275:2269-2275(2000).
[6]
FUNCTION.
PubMed=15531366; DOI=10.1016/j.ydbio.2004.08.023;
Baeg G.-H., Selva E.M., Goodman R.M., Dasgupta R., Perrimon N.;
"The Wingless morphogen gradient is established by the cooperative
action of Frizzled and Heparan Sulfate Proteoglycan receptors.";
Dev. Biol. 276:89-100(2004).
-!- 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 diffusion of morphogen
wingless (wg) via its role in heparan sulfate proteoglycans
(HSPGs) biosynthesis, HSPGs being required for movement of wg
morphogens. Required for wg signaling during both embryonic and
imaginal disk development. Also required for FGF receptor
signaling. {ECO:0000269|PubMed:10421372,
ECO:0000269|PubMed:10433902, ECO:0000269|PubMed:10644674,
ECO:0000269|PubMed:15531366}.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + [heparan
sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan
sulfate]-N-sulfoglucosamine.
-!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
-!- PATHWAY: Glycan metabolism; heparin biosynthesis.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST
subfamily. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-154 is the
initiator. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF175689; AAD51842.1; -; mRNA.
EMBL; AE014296; AAF50658.1; -; Genomic_DNA.
RefSeq; NP_001163354.1; NM_001169883.3.
RefSeq; NP_523946.1; NM_079222.5.
UniGene; Dm.4995; -.
ProteinModelPortal; Q9V3L1; -.
SMR; Q9V3L1; -.
BioGrid; 64188; 6.
IntAct; Q9V3L1; 6.
MINT; MINT-1615688; -.
STRING; 7227.FBpp0076677; -.
PaxDb; Q9V3L1; -.
PRIDE; Q9V3L1; -.
EnsemblMetazoa; FBtr0076968; FBpp0076677; FBgn0020251.
EnsemblMetazoa; FBtr0301562; FBpp0290777; FBgn0020251.
GeneID; 38736; -.
KEGG; dme:Dmel_CG8339; -.
UCSC; CG8339-RA; d. melanogaster.
CTD; 38736; -.
FlyBase; FBgn0020251; sfl.
eggNOG; KOG3703; Eukaryota.
eggNOG; ENOG410XQN4; LUCA.
GeneTree; ENSGT00760000119023; -.
InParanoid; Q9V3L1; -.
KO; K02577; -.
OMA; NYYRGLD; -.
OrthoDB; EOG091G02CP; -.
PhylomeDB; Q9V3L1; -.
Reactome; R-DME-2022928; HS-GAG biosynthesis.
SignaLink; Q9V3L1; -.
UniPathway; UPA00756; -.
UniPathway; UPA00862; -.
GenomeRNAi; 38736; -.
PRO; PR:Q9V3L1; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0020251; -.
ExpressionAtlas; Q9V3L1; differential.
Genevisible; Q9V3L1; DM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
GO; GO:0000137; C:Golgi cis cisterna; IDA:FlyBase.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045202; C:synapse; IEA:GOC.
GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; TAS:FlyBase.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0008146; F:sulfotransferase activity; IMP:UniProtKB.
GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IMP:UniProtKB.
GO; GO:0007507; P:heart development; NAS:FlyBase.
GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; TAS:FlyBase.
GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IMP:UniProtKB.
GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:FlyBase.
GO; GO:0007509; P:mesoderm migration involved in gastrulation; IMP:UniProtKB.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:FlyBase.
GO; GO:0090097; P:regulation of decapentaplegic signaling pathway; IMP:FlyBase.
GO; GO:0045570; P:regulation of imaginal disc growth; IMP:FlyBase.
GO; GO:0007367; P:segment polarity determination; IMP:FlyBase.
GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
GO; GO:0006790; P:sulfur compound metabolic process; IMP:UniProtKB.
GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:FlyBase.
GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
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; Disulfide bond; Glycoprotein; Golgi apparatus;
Hydrolase; Membrane; Multifunctional enzyme; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix;
Wnt signaling pathway.
CHAIN 1 1048 Bifunctional heparan sulfate N-
deacetylase/N-sulfotransferase.
/FTId=PRO_0000085226.
TOPO_DOM 1 172 Cytoplasmic. {ECO:0000255}.
TRANSMEM 173 192 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 193 1048 Lumenal. {ECO:0000255}.
NP_BIND 768 772 PAPS. {ECO:0000250}.
NP_BIND 998 1002 PAPS. {ECO:0000250}.
REGION 192 752 Heparan sulfate N-deacetylase.
REGION 753 1048 Heparan sulfate N-sulfotransferase.
ACT_SITE 768 768 For sulfotransferase activity.
{ECO:0000250}.
BINDING 877 877 PAPS. {ECO:0000250}.
CARBOHYD 388 388 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 555 555 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 823 823 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 892 892 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 983 993 {ECO:0000250}.
SEQUENCE 1048 AA; 118590 MW; A7E56155578D564E CRC64;
MTISGGNQHN NNANRKYEKL IKQPQMQFGS SVTGTQTDVD SCRDADADAN AVRQDFSNFN
KHFGNGHAIT DRTMLLRLED DVTTAAGIVT YKGKSNGNGN GNGNGSIGSI SLDFNGSPTS
STSIGIASGS SSNTHLASGG GVGGIGGSEP AGWMCHCCNL IARRCFGINV RRCVLALLAI
TMVSIFYYTH YVDTGVFNGL IQRDTHPAPI INCRMINSGG KHIRNASPAP DHRSEARLRI
DPKVLVFVET TYSGLGRDIA ELLVYNRIKY KIEVAGKSLP VLTNLDKGRY GVIVFENLDK
YLNMDKWNRE LLDKYCREYS VGIVGFVSPS EETLVGAQLR DFPLFVNTNL RLRDASLNPL
SSVLRLTRAG ETAWGALPGD DWAVFQHNHS TYEPVEWAQR NTQEYPADSV GQVQLPLTTV
LQDRGQLDGI QRVLFGSSLR FWLHRLVFLD ALSYLSHGQL SLNLERMILV DIDDIFVGEK
GTRLRPDDVR ALIATQKNIA AMVPGFRFNL GFSGKYYHHG TREENLGDDF LLQNVQEFNW
FSHMWKHQQP HLYDNLTLLM AEMHLNYAFA VDHNIPTDSG YSISPHHSGV YPAHELLYMA
WKKVWNVKVT STEEYPHLRP ARLRRGFIHR NIMVLPRQTC GLFTHTMYID RYPGGRDKLD
ESIQGGELFQ TIVYNPINIF MTHMSNYGSD RLALYTFQSV IKFLQCWTNL KLASAPPVQL
AEMYFRLHPE EVDPVWGNPC DDVRHKKIWS KTKNCDSLPK FLVIGPQKTG TTALYTFLSM
HGSIASNIAS PETFEEVQFF NGNNYYRGLD WYMDFFPSES LPNTSSPMPT QLGSPRFMFE
KSATYFDGEA VPKRSHALLP HAKIVTILIS PAKRAYSWYQ HQRSHGDVIA NNYSFYQVIT
ASDSAPRALK DLRNRCLNPG KYAQHLEHWL AYYPAQQLHI IDGEQLRLNP IDVMNELQRF
LKIQPLLDYS NHLRYDVKKG FYCQAVSEKR NKCLGKSKGR QYPAMDERSA KLLQRYYLNH
NTALVKLLKK LGSRPIPQWL KDDLSTGT


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