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NDST3_MOUSE
ID   NDST3_MOUSE             Reviewed;         873 AA.
AC   Q9EQH7; Q6AXE0; Q9D557;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 3;
DE            EC=2.8.2.8;
DE   AltName: Full=Glucosaminyl N-deacetylase/N-sulfotransferase 3;
DE            Short=NDST-3;
DE   AltName: Full=N-heparan sulfate sulfotransferase 3;
DE            Short=N-HSST 3;
DE   Includes:
DE     RecName: Full=Heparan sulfate N-deacetylase 3;
DE              EC=3.-.-.-;
DE   Includes:
DE     RecName: Full=Heparan sulfate N-sulfotransferase 3;
DE              EC=2.8.2.-;
GN   Name=Ndst3; Synonyms=Hsst3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; 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-deacetylase/GlcN N-
RT   sulfotransferase. Structure and activity of the fourth member, NDST4.";
RL   J. Biol. Chem. 276:5876-5882(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=16056228; DOI=10.1038/ni1233;
RA   Wang L., Fuster M., Sriramarao P., Esko J.D.;
RT   "Endothelial heparan sulfate deficiency impairs L-selectin- and chemokine-
RT   mediated neutrophil trafficking during inflammatory responses.";
RL   Nat. Immunol. 6:902-910(2005).
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 heparosan, a
CC       prerequisite substrate for later modifications in heparin biosynthesis.
CC       Has high deacetylase activity but low sulfotransferase activity.
CC       {ECO:0000269|PubMed:11087757}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan
CC         sulfate](n) = adenosine 3',5'-bisphosphate + 2 H(+) + N-sulfo-alpha-
CC         D-glucosaminyl-[heparan sulfate](n); Xref=Rhea:RHEA:21980, Rhea:RHEA-
CC         COMP:9830, Rhea:RHEA-COMP:14602, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:58388,
CC         ChEBI:CHEBI:140572; EC=2.8.2.8;
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}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9EQH7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EQH7-2; Sequence=VSP_017408, VSP_017409;
CC       Name=3;
CC         IsoId=Q9EQH7-3; Sequence=VSP_017407;
CC   -!- TISSUE SPECIFICITY: Strongly expressed strongly in brain. Expressed at
CC       high level at embryonic day 11 compared to other stages of development.
CC       Weakly expressed in adult heart, kidney, muscle, endothelial cells and
CC       testis but not in other tissues. {ECO:0000269|PubMed:11087757,
CC       ECO:0000269|PubMed:16056228}.
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 heparan
CC       sulfate modification/sulfation reactions, whereas other later on fill
CC       in or extend already modified heparan sulfate sequences.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF221095; AAG34793.1; -; mRNA.
DR   EMBL; AK015768; BAB29967.1; -; mRNA.
DR   EMBL; AK141945; BAE24894.1; -; mRNA.
DR   EMBL; BC079622; AAH79622.1; -; mRNA.
DR   CCDS; CCDS17818.1; -. [Q9EQH7-1]
DR   CCDS; CCDS80013.1; -. [Q9EQH7-3]
DR   RefSeq; NP_001280611.1; NM_001293682.1.
DR   RefSeq; NP_112463.2; NM_031186.3.
DR   AlphaFoldDB; Q9EQH7; -.
DR   SMR; Q9EQH7; -.
DR   STRING; 10090.ENSMUSP00000118207; -.
DR   GlyGen; Q9EQH7; 6 sites.
DR   iPTMnet; Q9EQH7; -.
DR   PhosphoSitePlus; Q9EQH7; -.
DR   EPD; Q9EQH7; -.
DR   MaxQB; Q9EQH7; -.
DR   PaxDb; Q9EQH7; -.
DR   PRIDE; Q9EQH7; -.
DR   ProteomicsDB; 253042; -. [Q9EQH7-1]
DR   ProteomicsDB; 253043; -. [Q9EQH7-2]
DR   ProteomicsDB; 253044; -. [Q9EQH7-3]
DR   Antibodypedia; 26593; 128 antibodies from 18 providers.
DR   DNASU; 83398; -.
DR   Ensembl; ENSMUST00000137404; ENSMUSP00000118796; ENSMUSG00000027977. [Q9EQH7-2]
DR   GeneID; 83398; -.
DR   KEGG; mmu:83398; -.
DR   CTD; 9348; -.
DR   MGI; MGI:1932544; Ndst3.
DR   VEuPathDB; HostDB:ENSMUSG00000027977; -.
DR   eggNOG; KOG3703; Eukaryota.
DR   GeneTree; ENSGT00940000160665; -.
DR   HOGENOM; CLU_011357_1_0_1; -.
DR   InParanoid; Q9EQH7; -.
DR   PhylomeDB; Q9EQH7; -.
DR   BRENDA; 2.8.2.8; 3474.
DR   Reactome; R-MMU-2022928; HS-GAG biosynthesis.
DR   UniPathway; UPA00756; -.
DR   UniPathway; UPA00862; -.
DR   BioGRID-ORCS; 83398; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Ndst3; mouse.
DR   PRO; PR:Q9EQH7; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9EQH7; protein.
DR   Bgee; ENSMUSG00000027977; Expressed in cerebellar cortex and 60 other tissues.
DR   ExpressionAtlas; Q9EQH7; baseline and differential.
DR   Genevisible; Q9EQH7; MM.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; ISO:MGI.
DR   GO; GO:0019213; F:deacetylase activity; IDA:MGI.
DR   GO; GO:0102140; F:heparan sulfate N-deacetylase activity; ISO:MGI.
DR   GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
DR   GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; ISO:MGI.
DR   GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; ISO:MGI.
DR   GO; GO:0030210; P:heparin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.300; -; 1.
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   Alternative splicing; Disulfide bond; Glycoprotein; Golgi apparatus;
KW   Hydrolase; Membrane; Multifunctional enzyme; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..873
FT                   /note="Bifunctional heparan sulfate N-deacetylase/N-
FT                   sulfotransferase 3"
FT                   /id="PRO_0000225660"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..873
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          36..589
FT                   /note="Heparan sulfate N-deacetylase 3"
FT   REGION          590..873
FT                   /note="Heparan sulfate N-sulfotransferase 3"
FT   ACT_SITE        605
FT                   /note="For sulfotransferase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         605..609
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         703
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   BINDING         824..828
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        658
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        794
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        809..819
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..415
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_017407"
FT   VAR_SEQ         635..642
FT                   /note="QFFNRNNY -> HGFLPSPI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_017408"
FT   VAR_SEQ         643..873
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_017409"
FT   CONFLICT        97
FT                   /note="M -> T (in Ref. 1; AAG34793)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="F -> V (in Ref. 1; AAG34793)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        373
FT                   /note="D -> E (in Ref. 1; AAG34793)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        726
FT                   /note="S -> F (in Ref. 2; BAB29967)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        771
FT                   /note="H -> Q (in Ref. 2; BAB29967)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   873 AA;  101040 MW;  3B54622D85F75EF9 CRC64;
     MSFIMKPHRH FQRTLILLAT FCMVSIIISA YYLYSGYKQE SEVSGRASEV DCGDLQHIPS
     RLMEVRRTMI SDASRTDPTV LVFVESQYSS LGQDIIMMLE SIRFHYHTEI APGKGDLPAL
     TDNVKGKYVL IIYENILKYI NMDSWNRSLL DKYCIEYGVG IIGFHKTSEK NLQSFQFRGF
     PFSISGNLAV KDCCINPHSP LLRVTKSSKL DRGSLPGTDW TVFQINHSTY QPVIFAKVKT
     PENLSPPISK HAFYATIIHD LGLHDGIQRV LFGNNLNFWL HKLIFIDAIS FLSGKRLTLS
     LDRYILVDID DIFVGKEGTR MNTNDVKALL DTQNLLRTQI TNFTFNLGFS GKFYHTGTEE
     EDEGDDCLLG SVDEFWWFPH MWSHMQPHLF HNESSLIEQM ILNKKFALEH GIPTDMGYAV
     SPHHSGVYPV HVQLYEAWKK VWNIKITSTE EYPHLKPARY RRGFIHKNIM VLPRQTCGLF
     THTIFYKEYP GGPRELDKSI HGGELFFTVV LNPISIFMTH LSNYGNDRLG LYTFVNLANF
     VQTWTNLRLQ TLPPAQLAHK YFELFPDQKD PLWQNPCDDK RHRDIWSKEK TCDRLPKFLV
     IGPQKTGTTA LCLFLIMHPS ILSNSPSPKS FEEVQFFNRN NYHRGIDWYM DFFPVPSNVT
     TDFLFEKSAN YFHSEDAPKR AASLVPKAKI ITILIDPSDR AYSWYQHQRS HEDPAALKFS
     FYEVISAGPN APWELRTLQK RCLVPGWYAN HIERWLVYFP PFQLLIIDGQ HLRTTPATVM
     DEVQKFLGVS PHYNYSEALT FDSHKGFWCQ LLEEGKTKCL GKSKGRKYPP MDSDSRAFLS
     SYYRDHNVEL SKLLHRLGQP LPSWLRQELQ KVR
 
 
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