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Protein

Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3

Gene

Ndst3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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. Has high deacetylase activity but low sulfotransferase activity.1 Publication

Catalytic activityi

3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine.

Pathwayi: heparan sulfate biosynthesis

This protein is involved in the pathway heparan sulfate biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway heparan sulfate biosynthesis and in Glycan metabolism.

Pathwayi: heparin biosynthesis

This protein is involved in the pathway heparin biosynthesis, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway heparin biosynthesis and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei605 – 6051For sulfotransferase activityBy similarity
Binding sitei703 – 7031PAPSBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi605 – 6095PAPSBy similarity
Nucleotide bindingi824 – 8285PAPSBy similarity

GO - Molecular functioni

  • [heparan sulfate]-glucosamine N-sulfotransferase activity Source: UniProtKB-EC
  • deacetylase activity Source: MGI
  • sulfotransferase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Enzyme and pathway databases

BRENDAi2.8.2.8. 3474.
UniPathwayiUPA00756.
UPA00862.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3 (EC:2.8.2.8)
Alternative name(s):
Glucosaminyl N-deacetylase/N-sulfotransferase 3
Short name:
NDST-3
N-heparan sulfate sulfotransferase 3
Short name:
N-HSST 3
Including the following 2 domains:
Heparan sulfate N-deacetylase 3 (EC:3.-.-.-)
Heparan sulfate N-sulfotransferase 3 (EC:2.8.2.-)
Gene namesi
Name:Ndst3
Synonyms:Hsst3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1932544. Ndst3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence analysisAdd
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini35 – 873839LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 873873Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3PRO_0000225660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence analysis
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence analysis
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence analysis
Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence analysis
Glycosylationi658 – 6581N-linked (GlcNAc...)Sequence analysis
Glycosylationi794 – 7941N-linked (GlcNAc...)Sequence analysis
Disulfide bondi809 ↔ 819By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9EQH7.
MaxQBiQ9EQH7.
PaxDbiQ9EQH7.
PRIDEiQ9EQH7.

PTM databases

iPTMnetiQ9EQH7.
PhosphoSiteiQ9EQH7.

Expressioni

Tissue specificityi

Strongly expressed strongly in brain. Expressed at high level at embryonic day 11 compared to other stages of development. Weakly expressed in adult heart, kidney, muscle, endothelial cells and testis but not in other tissues.2 Publications

Gene expression databases

BgeeiQ9EQH7.
ExpressionAtlasiQ9EQH7. baseline and differential.
GenevisibleiQ9EQH7. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029602.

Structurei

3D structure databases

ProteinModelPortaliQ9EQH7.
SMRiQ9EQH7. Positions 570-870.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 589554Heparan sulfate N-deacetylase 3Add
BLAST
Regioni590 – 873284Heparan sulfate N-sulfotransferase 3Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3703. Eukaryota.
ENOG410XQN4. LUCA.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000008010.
HOVERGENiHBG082011.
InParanoidiQ9EQH7.
KOiK02578.
OrthoDBiEOG7FXZXJ.
PhylomeDBiQ9EQH7.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR021930. Heparan_SO4_deacetylase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF12062. HSNSD. 1 hit.
PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9EQH7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSFIMKPHRH FQRTLILLAT FCMVSIIISA YYLYSGYKQE SEVSGRASEV
60 70 80 90 100
DCGDLQHIPS RLMEVRRTMI SDASRTDPTV LVFVESQYSS LGQDIIMMLE
110 120 130 140 150
SIRFHYHTEI APGKGDLPAL TDNVKGKYVL IIYENILKYI NMDSWNRSLL
160 170 180 190 200
DKYCIEYGVG IIGFHKTSEK NLQSFQFRGF PFSISGNLAV KDCCINPHSP
210 220 230 240 250
LLRVTKSSKL DRGSLPGTDW TVFQINHSTY QPVIFAKVKT PENLSPPISK
260 270 280 290 300
HAFYATIIHD LGLHDGIQRV LFGNNLNFWL HKLIFIDAIS FLSGKRLTLS
310 320 330 340 350
LDRYILVDID DIFVGKEGTR MNTNDVKALL DTQNLLRTQI TNFTFNLGFS
360 370 380 390 400
GKFYHTGTEE EDEGDDCLLG SVDEFWWFPH MWSHMQPHLF HNESSLIEQM
410 420 430 440 450
ILNKKFALEH GIPTDMGYAV SPHHSGVYPV HVQLYEAWKK VWNIKITSTE
460 470 480 490 500
EYPHLKPARY RRGFIHKNIM VLPRQTCGLF THTIFYKEYP GGPRELDKSI
510 520 530 540 550
HGGELFFTVV LNPISIFMTH LSNYGNDRLG LYTFVNLANF VQTWTNLRLQ
560 570 580 590 600
TLPPAQLAHK YFELFPDQKD PLWQNPCDDK RHRDIWSKEK TCDRLPKFLV
610 620 630 640 650
IGPQKTGTTA LCLFLIMHPS ILSNSPSPKS FEEVQFFNRN NYHRGIDWYM
660 670 680 690 700
DFFPVPSNVT TDFLFEKSAN YFHSEDAPKR AASLVPKAKI ITILIDPSDR
710 720 730 740 750
AYSWYQHQRS HEDPAALKFS FYEVISAGPN APWELRTLQK RCLVPGWYAN
760 770 780 790 800
HIERWLVYFP PFQLLIIDGQ HLRTTPATVM DEVQKFLGVS PHYNYSEALT
810 820 830 840 850
FDSHKGFWCQ LLEEGKTKCL GKSKGRKYPP MDSDSRAFLS SYYRDHNVEL
860 870
SKLLHRLGQP LPSWLRQELQ KVR
Length:873
Mass (Da):101,040
Last modified:March 7, 2006 - v2
Checksum:i3B54622D85F75EF9
GO
Isoform 2 (identifier: Q9EQH7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     635-642: QFFNRNNY → HGFLPSPI
     643-873: Missing.

Show »
Length:642
Mass (Da):73,829
Checksum:i4DC6FD1FE983CE3F
GO
Isoform 3 (identifier: Q9EQH7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-415: Missing.

Note: No experimental confirmation available.
Show »
Length:458
Mass (Da):53,504
Checksum:i5144A1E20F1F5BF0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971M → T in AAG34793 (PubMed:11087757).Curated
Sequence conflicti177 – 1771F → V in AAG34793 (PubMed:11087757).Curated
Sequence conflicti373 – 3731D → E in AAG34793 (PubMed:11087757).Curated
Sequence conflicti726 – 7261S → F in BAB29967 (PubMed:16141072).Curated
Sequence conflicti771 – 7711H → Q in BAB29967 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 415415Missing in isoform 3. 1 PublicationVSP_017407Add
BLAST
Alternative sequencei635 – 6428QFFNRNNY → HGFLPSPI in isoform 2. 2 PublicationsVSP_017408
Alternative sequencei643 – 873231Missing in isoform 2. 2 PublicationsVSP_017409Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF221095 mRNA. Translation: AAG34793.1.
AK015768 mRNA. Translation: BAB29967.1.
AK141945 mRNA. Translation: BAE24894.1.
BC079622 mRNA. Translation: AAH79622.1.
CCDSiCCDS17818.1. [Q9EQH7-1]
CCDS80013.1. [Q9EQH7-3]
RefSeqiNP_001280611.1. NM_001293682.1.
NP_112463.2. NM_031186.3.
UniGeneiMm.443908.
Mm.487979.

Genome annotation databases

EnsembliENSMUST00000137404; ENSMUSP00000118796; ENSMUSG00000027977. [Q9EQH7-2]
GeneIDi83398.
KEGGimmu:83398.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF221095 mRNA. Translation: AAG34793.1.
AK015768 mRNA. Translation: BAB29967.1.
AK141945 mRNA. Translation: BAE24894.1.
BC079622 mRNA. Translation: AAH79622.1.
CCDSiCCDS17818.1. [Q9EQH7-1]
CCDS80013.1. [Q9EQH7-3]
RefSeqiNP_001280611.1. NM_001293682.1.
NP_112463.2. NM_031186.3.
UniGeneiMm.443908.
Mm.487979.

3D structure databases

ProteinModelPortaliQ9EQH7.
SMRiQ9EQH7. Positions 570-870.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029602.

PTM databases

iPTMnetiQ9EQH7.
PhosphoSiteiQ9EQH7.

Proteomic databases

EPDiQ9EQH7.
MaxQBiQ9EQH7.
PaxDbiQ9EQH7.
PRIDEiQ9EQH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000137404; ENSMUSP00000118796; ENSMUSG00000027977. [Q9EQH7-2]
GeneIDi83398.
KEGGimmu:83398.

Organism-specific databases

CTDi9348.
MGIiMGI:1932544. Ndst3.

Phylogenomic databases

eggNOGiKOG3703. Eukaryota.
ENOG410XQN4. LUCA.
GeneTreeiENSGT00760000119023.
HOGENOMiHOG000008010.
HOVERGENiHBG082011.
InParanoidiQ9EQH7.
KOiK02578.
OrthoDBiEOG7FXZXJ.
PhylomeDBiQ9EQH7.

Enzyme and pathway databases

UniPathwayiUPA00756.
UPA00862.
BRENDAi2.8.2.8. 3474.

Miscellaneous databases

PROiQ9EQH7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQH7.
ExpressionAtlasiQ9EQH7. baseline and differential.
GenevisibleiQ9EQH7. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR021930. Heparan_SO4_deacetylase.
IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF12062. HSNSD. 1 hit.
PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Multiple isozymes of heparan sulfate/heparin GlcNAc N-deacetylase/GlcN N-sulfotransferase. Structure and activity of the fourth member, NDST4."
    Aikawa J., Grobe K., Tsujimoto M., Esko J.D.
    J. Biol. Chem. 276:5876-5882(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Spinal ganglion and Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "Endothelial heparan sulfate deficiency impairs L-selectin- and chemokine-mediated neutrophil trafficking during inflammatory responses."
    Wang L., Fuster M., Sriramarao P., Esko J.D.
    Nat. Immunol. 6:902-910(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiNDST3_MOUSE
AccessioniPrimary (citable) accession number: Q9EQH7
Secondary accession number(s): Q6AXE0, Q9D557
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 7, 2006
Last modified: June 8, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.