Reviewed, UniProtKB/Swiss-Prot Q9EQH7 (NDST3_MOUSE)

Names and origin

Protein names

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:
    1- Recommended name:
            Heparan sulfate N-deacetylase 3
              EC=3.-.-.-
    2- Recommended name:
            Heparan sulfate N-sulfotransferase 3
              EC=2.8.2.-

Gene names

Name:	Ndst3
Synonyms:	Hsst3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	873 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

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 dissacharide 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. Ref.1
Catalytic activity	3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-N-sulfoglucosamine.
Pathway	Glycan metabolism; heparan sulfate biosynthesis. Glycan metabolism; heparin biosynthesis.
Subunit structure	Monomer By similarity.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	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. Ref.1 Ref.4
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.
Sequence similarities	Belongs to the sulfotransferase 1 family. NDST subfamily.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane
Molecular function	Hydrolase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	[heparan sulfate]-glucosamine N-sulfotransferase activity Inferred from electronic annotation. Source: EC hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9EQH7-1)

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.

Isoform 2 (identifier: Q9EQH7-2)

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

Isoform 3 (identifier: Q9EQH7-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 873	873	Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3		PRO_0000225660
Regions
	Topological domain	1 – 13	13	Cytoplasmic Potential
	Transmembrane	14 – 34	21	Signal-anchor for type II membrane protein Potential
	Topological domain	35 – 873	839	Lumenal Potential
	Nucleotide binding	605 – 609	5	PAPS By similarity
	Nucleotide binding	824 – 828	5	PAPS By similarity
	Region	36 – 589	554	Heparan sulfate N-deacetylase 3
	Region	590 – 873	284	Heparan sulfate N-sulfotransferase 3
Sites
	Active site	605	1	For sulfotransferase activity By similarity
	Binding site	703	1	PAPS By similarity
Amino acid modifications
	Glycosylation	146	1	N-linked (GlcNAc...) Potential
	Glycosylation	226	1	N-linked (GlcNAc...) Potential
	Glycosylation	342	1	N-linked (GlcNAc...) Potential
	Glycosylation	392	1	N-linked (GlcNAc...) Potential
	Glycosylation	658	1	N-linked (GlcNAc...) Potential
	Glycosylation	794	1	N-linked (GlcNAc...) Potential
	Disulfide bond	809 ↔ 819		By similarity
Natural variations
	Alternative sequence	1 – 415	415	Missing in isoform 3.		VSP_017407
	Alternative sequence	635 – 642	8	QFFNRNNY → HGFLPSPI in isoform 2.		VSP_017408
	Alternative sequence	643 – 873	231	Missing in isoform 2.		VSP_017409
Experimental info
	Sequence conflict	97	1	M → T in AAG34793. Ref.1
	Sequence conflict	177	1	F → V in AAG34793. Ref.1
	Sequence conflict	373	1	D → E in AAG34793. Ref.1
	Sequence conflict	726	1	S → F in BAB29967. Ref.2
	Sequence conflict	771	1	H → Q in BAB29967. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 3B54622D85F75EF9	FASTA	873	101,040
	10 20 30 40 50 60 MSFIMKPHRH FQRTLILLAT FCMVSIIISA YYLYSGYKQE SEVSGRASEV DCGDLQHIPS 70 80 90 100 110 120 RLMEVRRTMI SDASRTDPTV LVFVESQYSS LGQDIIMMLE SIRFHYHTEI APGKGDLPAL 130 140 150 160 170 180 TDNVKGKYVL IIYENILKYI NMDSWNRSLL DKYCIEYGVG IIGFHKTSEK NLQSFQFRGF 190 200 210 220 230 240 PFSISGNLAV KDCCINPHSP LLRVTKSSKL DRGSLPGTDW TVFQINHSTY QPVIFAKVKT 250 260 270 280 290 300 PENLSPPISK HAFYATIIHD LGLHDGIQRV LFGNNLNFWL HKLIFIDAIS FLSGKRLTLS 310 320 330 340 350 360 LDRYILVDID DIFVGKEGTR MNTNDVKALL DTQNLLRTQI TNFTFNLGFS GKFYHTGTEE 370 380 390 400 410 420 EDEGDDCLLG SVDEFWWFPH MWSHMQPHLF HNESSLIEQM ILNKKFALEH GIPTDMGYAV 430 440 450 460 470 480 SPHHSGVYPV HVQLYEAWKK VWNIKITSTE EYPHLKPARY RRGFIHKNIM VLPRQTCGLF 490 500 510 520 530 540 THTIFYKEYP GGPRELDKSI HGGELFFTVV LNPISIFMTH LSNYGNDRLG LYTFVNLANF 550 560 570 580 590 600 VQTWTNLRLQ TLPPAQLAHK YFELFPDQKD PLWQNPCDDK RHRDIWSKEK TCDRLPKFLV 610 620 630 640 650 660 IGPQKTGTTA LCLFLIMHPS ILSNSPSPKS FEEVQFFNRN NYHRGIDWYM DFFPVPSNVT 670 680 690 700 710 720 TDFLFEKSAN YFHSEDAPKR AASLVPKAKI ITILIDPSDR AYSWYQHQRS HEDPAALKFS 730 740 750 760 770 780 FYEVISAGPN APWELRTLQK RCLVPGWYAN HIERWLVYFP PFQLLIIDGQ HLRTTPATVM 790 800 810 820 830 840 DEVQKFLGVS PHYNYSEALT FDSHKGFWCQ LLEEGKTKCL GKSKGRKYPP MDSDSRAFLS 850 860 870 SYYRDHNVEL SKLLHRLGQP LPSWLRQELQ KVR
	Isoform 2. Checksum: 4DC6FD1FE983CE3F	FASTA	642	73,829
	10 20 30 40 50 60 MSFIMKPHRH FQRTLILLAT FCMVSIIISA YYLYSGYKQE SEVSGRASEV DCGDLQHIPS 70 80 90 100 110 120 RLMEVRRTMI SDASRTDPTV LVFVESQYSS LGQDIIMMLE SIRFHYHTEI APGKGDLPAL 130 140 150 160 170 180 TDNVKGKYVL IIYENILKYI NMDSWNRSLL DKYCIEYGVG IIGFHKTSEK NLQSFQFRGF 190 200 210 220 230 240 PFSISGNLAV KDCCINPHSP LLRVTKSSKL DRGSLPGTDW TVFQINHSTY QPVIFAKVKT 250 260 270 280 290 300 PENLSPPISK HAFYATIIHD LGLHDGIQRV LFGNNLNFWL HKLIFIDAIS FLSGKRLTLS 310 320 330 340 350 360 LDRYILVDID DIFVGKEGTR MNTNDVKALL DTQNLLRTQI TNFTFNLGFS GKFYHTGTEE 370 380 390 400 410 420 EDEGDDCLLG SVDEFWWFPH MWSHMQPHLF HNESSLIEQM ILNKKFALEH GIPTDMGYAV 430 440 450 460 470 480 SPHHSGVYPV HVQLYEAWKK VWNIKITSTE EYPHLKPARY RRGFIHKNIM VLPRQTCGLF 490 500 510 520 530 540 THTIFYKEYP GGPRELDKSI HGGELFFTVV LNPISIFMTH LSNYGNDRLG LYTFVNLANF 550 560 570 580 590 600 VQTWTNLRLQ TLPPAQLAHK YFELFPDQKD PLWQNPCDDK RHRDIWSKEK TCDRLPKFLV 610 620 630 640 IGPQKTGTTA LCLFLIMHPS ILSNSPSPKS FEEVHGFLPS PI
	Isoform 3. Checksum: 5144A1E20F1F5BF0	FASTA	458	53,504
	10 20 30 40 50 60 MGYAVSPHHS GVYPVHVQLY EAWKKVWNIK ITSTEEYPHL KPARYRRGFI HKNIMVLPRQ 70 80 90 100 110 120 TCGLFTHTIF YKEYPGGPRE LDKSIHGGEL FFTVVLNPIS IFMTHLSNYG NDRLGLYTFV 130 140 150 160 170 180 NLANFVQTWT NLRLQTLPPA QLAHKYFELF PDQKDPLWQN PCDDKRHRDI WSKEKTCDRL 190 200 210 220 230 240 PKFLVIGPQK TGTTALCLFL IMHPSILSNS PSPKSFEEVQ FFNRNNYHRG IDWYMDFFPV 250 260 270 280 290 300 PSNVTTDFLF EKSANYFHSE DAPKRAASLV PKAKIITILI DPSDRAYSWY QHQRSHEDPA 310 320 330 340 350 360 ALKFSFYEVI SAGPNAPWEL RTLQKRCLVP GWYANHIERW LVYFPPFQLL IIDGQHLRTT 370 380 390 400 410 420 PATVMDEVQK FLGVSPHYNY SEALTFDSHK GFWCQLLEEG KTKCLGKSKG RKYPPMDSDS 430 440 450 RAFLSSYYRD HNVELSKLLH RLGQPLPSWL RQELQKVR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11087757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY. Strain: BALB/c. 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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6. 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: 16056228] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF221095 mRNA. Translation: AAG34793.1. AK015768 mRNA. Translation: BAB29967.1. AK141945 mRNA. Translation: BAE24894.1. BC079622 mRNA. Translation: AAH79622.1.
IPI	IPI00353519. IPI00742307. IPI00742340.
RefSeq	NP_112463.2.
UniGene	Mm.443908
3D structure databases
SMR	Q9EQH7. Positions 570-870.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9EQH7.
PTM databases
PhosphoSite	Q9EQH7.
Proteomic databases
PRIDE	Q9EQH7.
Genome annotation databases
Ensembl	ENSMUST00000029602; ENSMUSP00000029602; ENSMUSG00000027977; Mus musculus. [Genome view]
GeneID	83398.
KEGG	mmu:83398.
UCSC	uc008rfo.1. mouse. uc008rfp.1. mouse.
Organism-specific databases
CTD	83398.
MGI	MGI:1932544. Ndst3.
Phylogenomic databases
HOGENOM	HBG356867.
HOVERGEN	Q9EQH7.
InParanoid	Q9EQH7.
Enzyme and pathway databases
BRENDA	2.8.2.8. 244.
Gene expression databases
ArrayExpress	Q9EQH7.
Bgee	Q9EQH7.
Genevestigator	Q9EQH7.
GermOnline	ENSMUSG00000027977. Mus musculus.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	350527.
SOURCE	Search...

Entry information

Entry name

NDST3_MOUSE

Accession

Primary (citable) accession number: Q9EQH7
Secondary accession number(s): Q6AXE0, Q9D557

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	March 7, 2006
Last modified:	February 9, 2010
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)