GNS_HUMAN
ID GNS_HUMAN Reviewed; 552 AA.
AC P15586; B4DYH8; Q53F05;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=N-acetylglucosamine-6-sulfatase;
DE EC=3.1.6.14;
DE AltName: Full=Glucosamine-6-sulfatase;
DE Short=G6S;
DE Flags: Precursor;
GN Name=GNS;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP GLYCOSYLATION AT ASN-422.
RC TISSUE=Endothelial cell;
RX PubMed=1463457; DOI=10.1042/bj2880539;
RA Robertson D.A., Freeman C., Morris C.P., Hopwood J.J.;
RT "A cDNA clone for human glucosamine-6-sulphatase reveals differences
RT between arylsulphatases and non-arylsulphatases.";
RL Biochem. J. 288:539-544(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 178-552 (ISOFORM 1), AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=3196333; DOI=10.1016/s0006-291x(88)80035-4;
RA Robertson D.A., Freeman C., Nelson P.V., Morris C.P., Hopwood J.J.;
RT "Human glucosamine-6-sulfatase cDNA reveals homology with steroid
RT sulfatase.";
RL Biochem. Biophys. Res. Commun. 157:218-224(1988).
RN [7]
RP GLYCOSYLATION AT ASN-183 AND ASN-279.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-183; ASN-317; ASN-387 AND
RP ASN-422.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP INVOLVEMENT IN MPS3D.
RX PubMed=12573255; DOI=10.1016/s0888-7543(02)00014-9;
RA Mok A., Cao H., Hegele R.A.;
RT "Genomic basis of mucopolysaccharidosis type IIID (MIM 252940) revealed by
RT sequencing of GNS encoding N-acetylglucosamine-6-sulfatase.";
RL Genomics 81:1-5(2003).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP VARIANTS MPS3D ILE-94; 304-GLU--LEU-306 DEL; ARG-340 AND GLU-418.
RX PubMed=20232353; DOI=10.1002/humu.21234;
RA Valstar M.J., Bertoli-Avella A.M., Wessels M.W., Ruijter G.J.G.,
RA de Graaf B., Olmer R., Elfferich P., Neijs S., Kariminejad R.,
RA Suheyl Ezgue F., Tokatli A., Czartoryska B., Bosschaart A.N.,
RA van den Bos-Terpstra F., Puissant H., Buerger F., Omran H., Eckert D.,
RA Filocamo M., Simeonov E., Willems P.J., Wevers R.A., Niermeijer M.F.,
RA Halley D.J.J., Poorthuis B.J.H.M., van Diggelen O.P.;
RT "Mucopolysaccharidosis type IIID: 12 new patients and 15 novel mutations.";
RL Hum. Mutat. 31:E1348-E1360(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 6-sulfate groups of the N-acetyl-D-
CC glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.;
CC EC=3.1.6.14;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC P15586; P16333: NCK1; NbExp=2; IntAct=EBI-1752200, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P15586-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15586-2; Sequence=VSP_056486;
CC -!- PTM: The form A (78 kDa) is processed by internal peptidase cleavage to
CC a 32 kDa N-terminal species (form B) and a 48 kDa C-terminal species.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC residue in eukaryotes, is critical for catalytic activity.
CC {ECO:0000250}.
CC -!- DISEASE: Mucopolysaccharidosis 3D (MPS3D) [MIM:252940]: A form of
CC mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage
CC disease due to impaired degradation of heparan sulfate. MPS3 is
CC characterized by severe central nervous system degeneration, but only
CC mild somatic disease. Onset of clinical features usually occurs between
CC 2 and 6 years; severe neurologic degeneration occurs in most patients
CC between 6 and 10 years of age, and death occurs typically during the
CC second or third decade of life. {ECO:0000269|PubMed:12573255,
CC ECO:0000269|PubMed:20232353}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; Z12173; CAA78164.1; -; mRNA.
DR EMBL; AK302443; BAG63740.1; -; mRNA.
DR EMBL; AK223484; BAD97204.1; -; mRNA.
DR EMBL; AC025262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012482; AAH12482.1; -; mRNA.
DR CCDS; CCDS8970.1; -. [P15586-1]
DR PIR; S27164; KJHUGU.
DR RefSeq; NP_002067.1; NM_002076.3. [P15586-1]
DR AlphaFoldDB; P15586; -.
DR SMR; P15586; -.
DR BioGRID; 109061; 48.
DR IntAct; P15586; 23.
DR MINT; P15586; -.
DR STRING; 9606.ENSP00000258145; -.
DR GlyConnect; 796; 25 N-Linked glycans (8 sites).
DR GlyGen; P15586; 20 sites, 29 N-linked glycans (8 sites), 1 O-linked glycan (3 sites).
DR iPTMnet; P15586; -.
DR PhosphoSitePlus; P15586; -.
DR BioMuta; GNS; -.
DR DMDM; 232126; -.
DR EPD; P15586; -.
DR jPOST; P15586; -.
DR MassIVE; P15586; -.
DR MaxQB; P15586; -.
DR PaxDb; P15586; -.
DR PeptideAtlas; P15586; -.
DR PRIDE; P15586; -.
DR ProteomicsDB; 53189; -. [P15586-1]
DR ProteomicsDB; 5526; -.
DR Antibodypedia; 2462; 244 antibodies from 33 providers.
DR DNASU; 2799; -.
DR Ensembl; ENST00000258145.8; ENSP00000258145.3; ENSG00000135677.11. [P15586-1]
DR Ensembl; ENST00000542058.5; ENSP00000444819.1; ENSG00000135677.11. [P15586-2]
DR GeneID; 2799; -.
DR KEGG; hsa:2799; -.
DR MANE-Select; ENST00000258145.8; ENSP00000258145.3; NM_002076.4; NP_002067.1.
DR UCSC; uc001ssg.5; human. [P15586-1]
DR CTD; 2799; -.
DR DisGeNET; 2799; -.
DR GeneCards; GNS; -.
DR GeneReviews; GNS; -.
DR HGNC; HGNC:4422; GNS.
DR HPA; ENSG00000135677; Low tissue specificity.
DR MalaCards; GNS; -.
DR MIM; 252940; phenotype.
DR MIM; 607664; gene.
DR neXtProt; NX_P15586; -.
DR OpenTargets; ENSG00000135677; -.
DR Orphanet; 79272; Sanfilippo syndrome type D.
DR PharmGKB; PA28802; -.
DR VEuPathDB; HostDB:ENSG00000135677; -.
DR eggNOG; KOG3731; Eukaryota.
DR GeneTree; ENSGT00940000158420; -.
DR InParanoid; P15586; -.
DR OMA; LVEYWGE; -.
DR PhylomeDB; P15586; -.
DR TreeFam; TF313545; -.
DR BioCyc; MetaCyc:HS06046-MON; -.
DR BRENDA; 3.1.6.14; 2681.
DR PathwayCommons; P15586; -.
DR Reactome; R-HSA-2022857; Keratan sulfate degradation.
DR Reactome; R-HSA-2206305; MPS IIID - Sanfilippo syndrome D.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SABIO-RK; P15586; -.
DR SignaLink; P15586; -.
DR BioGRID-ORCS; 2799; 14 hits in 1071 CRISPR screens.
DR ChiTaRS; GNS; human.
DR GenomeRNAi; 2799; -.
DR Pharos; P15586; Tbio.
DR PRO; PR:P15586; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P15586; protein.
DR Bgee; ENSG00000135677; Expressed in adrenal tissue and 203 other tissues.
DR ExpressionAtlas; P15586; baseline and differential.
DR Genevisible; P15586; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005539; F:glycosaminoglycan binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008449; F:N-acetylglucosamine-6-sulfatase activity; IBA:GO_Central.
DR GO; GO:0043199; F:sulfate binding; IEA:Ensembl.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IDA:MGI.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; TAS:ProtInc.
DR GO; GO:0042340; P:keratan sulfate catabolic process; TAS:Reactome.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012251; GlcNAc_6-SO4ase.
DR InterPro; IPR015981; GlcNAc_6-SO4ase_met.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR43108:SF5; PTHR43108:SF5; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF036666; G6S; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Direct protein sequencing; Disease variant;
KW Glycoprotein; Hydrolase; Lysosome; Metal-binding; Mucopolysaccharidosis;
KW Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..36
FT CHAIN 37..552
FT /note="N-acetylglucosamine-6-sulfatase"
FT /id="PRO_0000033413"
FT ACT_SITE 91
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 91
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1463457,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 65..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056486"
FT VARIANT 94
FT /note="S -> I (in MPS3D)"
FT /evidence="ECO:0000269|PubMed:20232353"
FT /id="VAR_064070"
FT VARIANT 304..306
FT /note="Missing (in MPS3D)"
FT /evidence="ECO:0000269|PubMed:20232353"
FT /id="VAR_064071"
FT VARIANT 340
FT /note="K -> R (in MPS3D)"
FT /evidence="ECO:0000269|PubMed:20232353"
FT /id="VAR_064072"
FT VARIANT 418
FT /note="G -> E (in MPS3D)"
FT /evidence="ECO:0000269|PubMed:20232353"
FT /id="VAR_064073"
FT CONFLICT 252
FT /note="F -> C (in Ref. 3; BAD97204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 552 AA; 62082 MW; 85094043F6E64468 CRC64;
MRLLPLAPGR LRRGSPRHLP SCSPALLLLV LGGCLGVFGV AAGTRRPNVV LLLTDDQDEV
LGGMTPLKKT KALIGEMGMT FSSAYVPSAL CCPSRASILT GKYPHNHHVV NNTLEGNCSS
KSWQKIQEPN TFPAILRSMC GYQTFFAGKY LNEYGAPDAG GLEHVPLGWS YWYALEKNSK
YYNYTLSING KARKHGENYS VDYLTDVLAN VSLDFLDYKS NFEPFFMMIA TPAPHSPWTA
APQYQKAFQN VFAPRNKNFN IHGTNKHWLI RQAKTPMTNS SIQFLDNAFR KRWQTLLSVD
DLVEKLVKRL EFTGELNNTY IFYTSDNGYH TGQFSLPIDK RQLYEFDIKV PLLVRGPGIK
PNQTSKMLVA NIDLGPTILD IAGYDLNKTQ MDGMSLLPIL RGASNLTWRS DVLVEYQGEG
RNVTDPTCPS LSPGVSQCFP DCVCEDAYNN TYACVRTMSA LWNLQYCEFD DQEVFVEVYN
LTADPDQITN IAKTIDPELL GKMNYRLMML QSCSGPTCRT PGVFDPGYRF DPRLMFSNRG
SVRTRRFSKH LL
