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Database: UniProt
Entry: NDST4_MOUSE
LinkDB: NDST4_MOUSE
Original site: NDST4_MOUSE 
ID   NDST4_MOUSE             Reviewed;         872 AA.
AC   Q9EQW8; D3Z1R7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   28-FEB-2018, entry version 108.
DE   RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4;
DE            EC=2.8.2.8;
DE   AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 4;
DE            Short=NDST-4;
DE   AltName: Full=N-heparan sulfate sulfotransferase 4;
DE            Short=N-HSST 4;
DE   Includes:
DE     RecName: Full=Heparan sulfate N-deacetylase 4;
DE              EC=3.-.-.-;
DE   Includes:
DE     RecName: Full=Heparan sulfate N-sulfotransferase 4;
DE              EC=2.8.2.-;
GN   Name=Ndst4; Synonyms=Hsst4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=11087757; DOI=10.1074/jbc.M009606200;
RA   Aikawa J., Grobe K., Tsujimoto M., Esko J.D.;
RT   "Multiple isozymes of heparan sulfate/heparin GlcNAc N-
RT   deacetylase/GlcN N-sulfotransferase. Structure and activity of the
RT   fourth member, NDST4.";
RL   J. Biol. Chem. 276:5876-5882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Essential bifunctional enzyme that catalyzes both the N-
CC       deacetylation and the N-sulfation of glucosamine (GlcNAc) of the
CC       glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA
CC       disaccharide repeating sugar backbone to make N-sulfated
CC       heparosan, a prerequisite substrate for later modifications in
CC       heparin biosynthesis. Has low deacetylase activity but high
CC       sulfotransferase activity. {ECO:0000269|PubMed:11087757}.
CC   -!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + [heparan
CC       sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan
CC       sulfate]-N-sulfoglucosamine.
CC   -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC   -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at low level in brain and throughout
CC       embryogenesis. Not expressed in other tissues.
CC       {ECO:0000269|PubMed:11087757}.
CC   -!- MISCELLANEOUS: The presence of 4 different heparan sulfate N-
CC       deacetylase/N-sulfotransferase enzymes in mammals, as well as
CC       differences in their enzyme activity suggest that some initiate
CC       heparan sulfate modification/sulfation reactions, whereas other
CC       later on fill in or extend already modified heparan sulfate
CC       sequences.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST
CC       subfamily. {ECO:0000305}.
DR   EMBL; AB036838; BAB18517.1; -; mRNA.
DR   EMBL; AC111141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC164153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS17820.1; -.
DR   RefSeq; NP_072087.2; NM_022565.2.
DR   RefSeq; XP_017175172.1; XM_017319683.1.
DR   UniGene; Mm.444289; -.
DR   UniGene; Mm.483253; -.
DR   ProteinModelPortal; Q9EQW8; -.
DR   SMR; Q9EQW8; -.
DR   BioGrid; 211087; 1.
DR   STRING; 10090.ENSMUSP00000133341; -.
DR   PhosphoSitePlus; Q9EQW8; -.
DR   MaxQB; Q9EQW8; -.
DR   PaxDb; Q9EQW8; -.
DR   PRIDE; Q9EQW8; -.
DR   Ensembl; ENSMUST00000173932; ENSMUSP00000133341; ENSMUSG00000027971.
DR   GeneID; 64580; -.
DR   KEGG; mmu:64580; -.
DR   UCSC; uc008rfv.2; mouse.
DR   CTD; 64579; -.
DR   MGI; MGI:1932545; Ndst4.
DR   eggNOG; KOG3703; Eukaryota.
DR   eggNOG; ENOG410XQN4; LUCA.
DR   GeneTree; ENSGT00760000119023; -.
DR   HOGENOM; HOG000008010; -.
DR   HOVERGEN; HBG082011; -.
DR   InParanoid; Q9EQW8; -.
DR   KO; K02579; -.
DR   OMA; VSMDSWN; -.
DR   OrthoDB; EOG091G02CP; -.
DR   PhylomeDB; Q9EQW8; -.
DR   TreeFam; TF313193; -.
DR   BRENDA; 2.8.2.8; 3474.
DR   Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   PRO; PR:Q9EQW8; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000027971; -.
DR   ExpressionAtlas; Q9EQW8; baseline and differential.
DR   Genevisible; Q9EQW8; MM.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of 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; IDA:MGI.
DR   GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
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   InterPro; IPR021930; Heparan_SO4_deacetylase.
DR   InterPro; IPR037359; NST/OST.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   PANTHER; PTHR10605; PTHR10605; 1.
DR   Pfam; PF12062; HSNSD; 1.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; Glycoprotein; Golgi apparatus;
KW   Hydrolase; Membrane; Multifunctional enzyme; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    872       Bifunctional heparan sulfate N-
FT                                deacetylase/N-sulfotransferase 4.
FT                                /FTId=PRO_0000225662.
FT   TOPO_DOM      1     13       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     14     34       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     35    872       Lumenal. {ECO:0000255}.
FT   NP_BIND     604    608       PAPS. {ECO:0000250}.
FT   NP_BIND     823    827       PAPS. {ECO:0000250}.
FT   REGION       36    588       Heparan sulfate N-deacetylase 4.
FT   REGION      589    872       Heparan sulfate N-sulfotransferase 4.
FT   ACT_SITE    604    604       For sulfotransferase activity.
FT                                {ECO:0000250}.
FT   BINDING     702    702       PAPS. {ECO:0000250}.
FT   CARBOHYD    226    226       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    341    341       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    391    391       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    657    657       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    793    793       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    808    818       {ECO:0000250}.
FT   CONFLICT    681    681       A -> T (in Ref. 1; BAB18517).
FT                                {ECO:0000305}.
SQ   SEQUENCE   872 AA;  100655 MW;  C56980F256C757E4 CRC64;
     MNLILKFRRS FRTLIVLLAT FCLVSILISA YFLYSGYKQE MTLIETTAEA ECADIKDLPY
     RSIELRTIKP IDTSKTDPTV LLFVESQYSQ LGQDIIAILE SSRFQYQMVI APGKGDIPPL
     TDSGKGKYTL IIYENILKYV SMDSWNRELL EKYCIEYSVS IIGFHKANEN SLPTTQLKGF
     PLNLFNNVAL KDCSVNPQSP LLHITKGPKV EKGPLPGEDW TIFQYNHSTY QPVLLTELQS
     EKSLSFLSSQ TLYATIIQDL GLHDGIQRVL FGNNLNFWLH KLIFIDAISF LSGKRLTLSL
     DRYILVDIDD IFVGKEGTRM NVKDVKALLE TQNLLRTQVA NFTFNLGFSG KFYHTGTEEE
     DEGDDLLLRS VDEFWWFPHM WSHMQPHLFH NESSLVEQMI LNKEFALEHG IPINLGYAVA
     PHHSGVYPVH IQLYAAWKKV WGIQVTSTEE YPHLKPARYR KGFIHNSIMV LPRQTCGLFT
     HTIFYKEYPG GPQELDKSIK GGELFLTILL NPISIFMTHL SNYGNDRLGL YTFVNLANFV
     HSWTNLKLQT LPPVQLAHKY FELFPEQKDP LWQNPCDDKR HKDIWSREKT CDHLPKFLVI
     GPQKTGTTAL YLFLLMHPSI ISNLPSPKTF EEVQFFNGNN YHKGIEWYMD FFPTPSNITS
     DFLFEKSANY FHSEEAPKRA ASLVPKAKII TILIDPSDRA YSWYQHQRSH EDPAALRFNF
     YEVITTGHWA PPDLKTLQRR CLVPGWYAVH IERWLAYFST SQLLIIDGQQ LRSDPATVMD
     EVQKFLGVTP HYNYSEALTF DPQKGFWCQL LEGGKTKCLG KSKGRKYPPM DSESRTFLSS
     YYRDHNVELS KLLHRLGQPL PSWLRQELQK VR
//
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