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Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2 (EC 2.8.2.8) (CCL44) (Glucosaminyl N-deacetylase/N-sulfotransferase 2) (NDST-2) [Includes: Heparan sulfate N-deacetylase 2 (EC 3.-.-.-); Heparan sulfate N-sulfotransferase 2 (EC 2.8.2.-)]

 NDST2_BOVIN             Reviewed;         884 AA.
O97583; Q862Q7; Q862Y7;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
20-DEC-2017, entry version 93.
RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2;
EC=2.8.2.8;
AltName: Full=CCL44;
AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 2;
Short=NDST-2;
Includes:
RecName: Full=Heparan sulfate N-deacetylase 2;
EC=3.-.-.-;
Includes:
RecName: Full=Heparan sulfate N-sulfotransferase 2;
EC=2.8.2.-;
Name=NDST2;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Trachea;
PubMed=9712870; DOI=10.1074/jbc.273.35.22458;
Toma L., Berninsone P., Hirschberg C.B.;
"The putative heparin-specific N-acetylglucosaminyl N-deacetylase/N-
sulfotransferase also occurs in non-heparin-producing cells.";
J. Biol. Chem. 273:22458-22465(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 688-884.
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
-!- 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. Required for the exosomal
release of SDCBP, CD63 and syndecan (By similarity).
{ECO:0000250|UniProtKB:P52849, ECO:0000269|PubMed:9712870}.
-!- 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}.
-!- 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; AF064825; AAC77921.1; -; mRNA.
EMBL; AB098922; BAC56412.1; -; mRNA.
UniGene; Bt.4950; -.
ProteinModelPortal; O97583; -.
SMR; O97583; -.
STRING; 9913.ENSBTAP00000016827; -.
PaxDb; O97583; -.
PRIDE; O97583; -.
eggNOG; KOG3703; Eukaryota.
eggNOG; ENOG410XQN4; LUCA.
HOGENOM; HOG000008010; -.
HOVERGEN; HBG082011; -.
InParanoid; O97583; -.
BRENDA; 2.8.2.8; 908.
UniPathway; UPA00756; -.
UniPathway; UPA00862; -.
Proteomes; UP000009136; Unplaced.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
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.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Golgi apparatus;
Hydrolase; Membrane; Multifunctional enzyme; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 884 Bifunctional heparan sulfate N-
deacetylase/N-sulfotransferase 2.
/FTId=PRO_0000225658.
TOPO_DOM 1 18 Cytoplasmic. {ECO:0000255}.
TRANSMEM 19 39 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 40 884 Lumenal. {ECO:0000255}.
NP_BIND 614 618 PAPS. {ECO:0000250}.
NP_BIND 833 837 PAPS. {ECO:0000250}.
REGION 41 598 Heparan sulfate N-deacetylase 2.
REGION 599 884 Heparan sulfate N-sulfotransferase 2.
ACT_SITE 614 614 For sulfotransferase activity.
{ECO:0000250}.
BINDING 712 712 PAPS. {ECO:0000250}.
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}.
CARBOHYD 727 727 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 803 803 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 818 828 {ECO:0000250}.
CONFLICT 735 735 T -> S (in Ref. 2; BAC56412).
{ECO:0000305}.
CONFLICT 740 740 D -> A (in Ref. 2; BAC56412).
{ECO:0000305}.
CONFLICT 768 768 Y -> F (in Ref. 2; BAC56412).
{ECO:0000305}.
CONFLICT 791 791 I -> S (in Ref. 2; BAC56412).
{ECO:0000305}.
CONFLICT 814 814 K -> R (in Ref. 2; BAC56412).
{ECO:0000305}.
SEQUENCE 884 AA; 100897 MW; 962E364E17C37FC2 CRC64;
MLKLWKVVRP ARQLELHRLI LLLIAFSLGS MGFLAYYVST SPKAKEPLPL PLGDCSSSGA
AGGPGPVRPP VPPRPPRPPE TARTEPVVLV FVESAYSQLG QEIVAILESS RFRYSTELAP
GRGDMPTLTD HTRGRYVLVI YENLLKYVNL DAWSRELLDR YCVEYGVGII GFFRAHEHSL
LSAQLKGFPL FLHSNLGLRD YQVNPTAPLL HLTRPSRLEP GPLPGDDWTI FQSNHRTYEP
VLLGSLRPAE PPVPGPVARR ARLPTVVQDL GVHDGIQRVL FGHGLSFWLH KLVFRDAGGY
LTGKGLLWDL DRYILVDIDD IFVGKEGTRM KVADVEALLT TQNKLRTLVP NFTFNLGFSG
KFYHTGTEEE DAGDDMLLNH RREFWWFPHM WSHMQPHLFH NRSVLADQMR LNKQFALEHG
IPTDLGYAVA PHHSGVYPIH TQLYEAWKSV WGIQVTSTEE YPHLRPARYR RGFIHNGIMV
LPRQTCGLFT HTIFYNEYPG GSRELDRSIR GGELFLTVLL NPISIFMTHL SNYGNDRLGL
YTFESLVRFL QCWTSLRLQT LPPVPLGRKY FDLFPQERSP LWQNPCDDKR HKDIWSKEKT
CDRLPKFLIV GPQKTGTTAI HFFLSLHPAV TSSFPSPSTF EEIQFFNGPN YHKGIDWYMD
FFPVPSNAST DFLFEKSATY FDSEVVPRRG AALLPRAKII TVLTNPADRA YSWYQHQRAH
GDPVALNYTF YQVITASSQD PPALRSLQNR CLVPGYYSTH LQRWLTYYPS GQLLIVDGQE
LRTNPAASME IIQKFLGITP FLNYTRTLRF DEDKGFWCQG LEGGKTRCLG KSKGRKYPDM
DAESRLFLTD FFRNHNLELS KLLSRLGQPV PSWLREELQH SSSG


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