ID Q14DQ0_MOUSE Unreviewed; 873 AA.
AC Q14DQ0;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=[heparan sulfate]-glucosamine N-sulfotransferase {ECO:0000256|ARBA:ARBA00012979};
DE EC=2.8.2.8 {ECO:0000256|ARBA:ARBA00012979};
GN Name=Ndst3 {ECO:0000313|EMBL:AAI12405.1, ECO:0000313|MGI:MGI:1932544};
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 {ECO:0000313|EMBL:AAI12405.1};
RN [1] {ECO:0000313|EMBL:AAI12405.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PCR rescued clones {ECO:0000313|EMBL:AAI12405.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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).
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005093}.
CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004841}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. NDST subfamily.
CC {ECO:0000256|ARBA:ARBA00010420}.
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DR EMBL; BC112404; AAI12405.1; -; mRNA.
DR AlphaFoldDB; Q14DQ0; -.
DR AGR; MGI:1932544; -.
DR MGI; MGI:1932544; Ndst3.
DR UniPathway; UPA00756; -.
DR UniPathway; UPA00862; -.
DR ChiTaRS; Ndst3; mouse.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015016; F:[heparan sulfate]-glucosamine N-sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019213; F:deacetylase activity; IEA:UniProt.
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 Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF29; BIFUNCTIONAL HEPARAN SULFATE N-DEACETYLASE_N-SULFOTRANSFERASE 3; 1.
DR PANTHER; PTHR10605; HEPARAN SULFATE SULFOTRANSFERASE; 1.
DR Pfam; PF12062; HSNSD; 1.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR637359-3};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:AAI12405.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..506
FT /note="Heparan sulphate-N-deacetylase"
FT /evidence="ECO:0000259|Pfam:PF12062"
FT DOMAIN 596..844
FT /note="Sulfotransferase"
FT /evidence="ECO:0000259|Pfam:PF00685"
FT ACT_SITE 605
FT /note="For sulfotransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-1"
FT BINDING 703
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 808
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT BINDING 824..828
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-2"
FT DISULFID 809..819
FT /evidence="ECO:0000256|PIRSR:PIRSR637359-3"
SQ SEQUENCE 873 AA; 100976 MW; E0EE8F5326377467 CRC64;
MSFIMKPHRH FQRTLILLAT FCMVSIIISA YYLYSGYKQE SEVSGRASEV DCGDLQHIPS
RLMEVRRTMI SDASRTDPTV LVFVESQYSS LGQDIITMLE SIRFHYHTEI APGKGDLPAL
TDNVKGKYVL IIYENILKYI NMDSWNRSLL DKYCIEYGVG IIGFHKTSEK NLQSFQVRGF
PFSISGNLAV KDCCINPHSP LLRVTKSSKL DRGSLPGTDW TVFQINHSTY QPVIFAKVKT
PENLSPPISK HAFYATIIHD LGLHDGIQRV LFGNNLNFWL HKLIFIDAIS FLSGKRLTLS
LDRYILVDID DIFVGKEGTR MNTNDVKALL DTQNLLRTQI TNFTFNLGFS GKFYHTGTEE
EDEGDDCLLG SVEEFWWFPH 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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