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   27-MAR-2024, entry version 205.
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; 118.
DR   IntAct; P15586; 25.
DR   MINT; P15586; -.
DR   STRING; 9606.ENSP00000258145; -.
DR   GlyConnect; 796; 25 N-Linked glycans (8 sites).
DR   GlyCosmos; P15586; 16 sites, 28 glycans.
DR   GlyGen; P15586; 21 sites, 29 N-linked glycans (8 sites), 1 O-linked glycan (4 sites).
DR   iPTMnet; P15586; -.
DR   PhosphoSitePlus; P15586; -.
DR   SwissPalm; P15586; -.
DR   BioMuta; GNS; -.
DR   DMDM; 232126; -.
DR   EPD; P15586; -.
DR   jPOST; P15586; -.
DR   MassIVE; P15586; -.
DR   MaxQB; P15586; -.
DR   PaxDb; 9606-ENSP00000258145; -.
DR   PeptideAtlas; P15586; -.
DR   ProteomicsDB; 53189; -. [P15586-1]
DR   ProteomicsDB; 5526; -.
DR   Pumba; P15586; -.
DR   Antibodypedia; 2462; 268 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   AGR; HGNC:4422; -.
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; WCHGEHE; -.
DR   OrthoDB; 1365192at2759; -.
DR   PhylomeDB; P15586; -.
DR   TreeFam; TF313545; -.
DR   BioCyc; MetaCyc:HS06046-MONOMER; -.
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; 16 hits in 1157 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 205 other cell types or tissues.
DR   ExpressionAtlas; P15586; baseline and differential.
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   CDD; cd16147; G6S; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR012251; GlcNAc_6-SO4ase.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR43108:SF5; N-ACETYLGLUCOSAMINE-6-SULFATASE; 1.
DR   PANTHER; PTHR43108; N-ACETYLGLUCOSAMINE-6-SULFATASE FAMILY MEMBER; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   PIRSF; PIRSF036666; G6S; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
DR   PROSITE; PS00149; SULFATASE_2; 1.
DR   Genevisible; P15586; HS.
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
//