IDS_HUMAN
ID IDS_HUMAN Reviewed; 550 AA.
AC P22304; D3DWT4; Q14604; Q9BRM3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Iduronate 2-sulfatase;
DE EC=3.1.6.13 {ECO:0000269|PubMed:10838181, ECO:0000269|PubMed:11731225, ECO:0000269|PubMed:28593992};
DE AltName: Full=Alpha-L-iduronate sulfate sulfatase;
DE Short=Idursulfase;
DE Contains:
DE RecName: Full=Iduronate 2-sulfatase 42 kDa chain;
DE Contains:
DE RecName: Full=Iduronate 2-sulfatase 14 kDa chain;
DE Flags: Precursor;
GN Name=IDS; Synonyms=SIDS;
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), AND PROTEIN SEQUENCE OF 34-58 AND
RP 456-473.
RC TISSUE=Endothelial cell;
RX PubMed=2122463; DOI=10.1073/pnas.87.21.8531;
RA Wilson P.J., Morris C.P., Anson D.S., Occhiodoro T., Bielicki J.,
RA Clements P.R., Hopwood J.J.;
RT "Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and
RT analysis of patient DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8531-8535(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8244397; DOI=10.1006/geno.1993.1406;
RA Wilson P.J., Meaney C.A., Hopwood J.J., Morris C.P.;
RT "Sequence of the human iduronate 2-sulfatase (IDS) gene.";
RL Genomics 17:773-775(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8717057; DOI=10.1101/gr.5.1.71;
RA Timms K.M., Lu F., Shen Y., Pierson C.A., Muzny D.M., Gu Y., Nelson D.L.,
RA Gibbs R.A.;
RT "130 kb of DNA sequence reveals two new genes and a regional duplication
RT distal to the human iduronate-2-sulfate sulfatase locus.";
RL Genome Res. 5:71-78(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Lymphocyte;
RX PubMed=8530090; DOI=10.1006/geno.1995.1249;
RA Malmgren H., Carlberg B.M., Pettersson U., Bondeson M.L.;
RT "Identification of an alternative transcript from the human iduronate-2-
RT sulfatase (IDS) gene.";
RL Genomics 29:291-293(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-398.
RX PubMed=8490623; DOI=10.1093/hmg/2.1.5;
RA Flomen R.H., Green E.P., Green P.M., Bentley D.R., Giannelli F.;
RT "Determination of the organisation of coding sequences within the iduronate
RT sulphate sulphatase (IDS) gene.";
RL Hum. Mol. Genet. 2:5-10(1993).
RN [9]
RP REVIEW ON MPS2 VARIANTS.
RX PubMed=8111411; DOI=10.1002/humu.1380020603;
RA Hopwood J.J., Bunge S., Morris C.P., Wilson P.J., Steglich C., Beck M.,
RA Schwinger E., Gal A.;
RT "Molecular basis of mucopolysaccharidosis type II: mutations in the
RT iduronate-2-sulphatase gene.";
RL Hum. Mutat. 2:435-442(1993).
RN [10]
RP PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION.
RX PubMed=7626005; DOI=10.1042/bj3090425;
RA Froissart R., Millat G., Mathieu M., Bozon D., Maire I.;
RT "Processing of iduronate 2-sulphatase in human fibroblasts.";
RL Biochem. J. 309:425-430(1995).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-115.
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 [12] {ECO:0007744|PDB:5FQL}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-550 IN COMPLEX WITH CALCIUM,
RP GLYCOSYLATION AT ASN-115; ASN-144; ASN-246; ASN-280; ASN-325; ASN-513 AND
RP ASN-537, DISULFIDE BOND, ACTIVE SITE, SUBUNIT, COFACTOR, OXOALANINE AT
RP CYS-84, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=28593992; DOI=10.1038/ncomms15786;
RA Demydchuk M., Hill C.H., Zhou A., Bunkoczi G., Stein P.E., Marchesan D.,
RA Deane J.E., Read R.J.;
RT "Insights into Hunter syndrome from the structure of iduronate-2-
RT sulfatase.";
RL Nat. Commun. 8:15786-15786(2017).
RN [13] {ECO:0007744|PDB:6IOZ}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 34-550.
RA Kim H., Kim D., Hong J., Lee K., Seo J., Oh B.H.;
RT "Structural insights of idursulfase beta.";
RL Submitted (NOV-2018) to the PDB data bank.
RN [14]
RP VARIANTS MPS2 ARG-135 AND GLY-422.
RX PubMed=1303211; DOI=10.1093/hmg/1.5.335;
RA Bunge S., Steglich C., Beck M., Rosenkranz W., Schwinger E., Hopwood J.J.,
RA Gal A.;
RT "Mutation analysis of the iduronate-2-sulfatase gene in patients with
RT mucopolysaccharidosis type II (Hunter syndrome).";
RL Hum. Mol. Genet. 1:335-339(1992).
RN [15]
RP VARIANT MPS2 TRP-468.
RX PubMed=1284597; DOI=10.1093/hmg/1.9.755;
RA Crotti P.L., Bunge S., Anderson R.A., Whitley C.B.;
RT "Mutation R468W of the iduronate-2-sulfatase gene in mild Hunter syndrome
RT (mucopolysaccharidosis type II) confirmed by in vitro mutagenesis and
RT expression.";
RL Hum. Mol. Genet. 1:755-757(1992).
RN [16]
RP VARIANTS MPS2 ARG-86; ASP-94; ARG-120; PRO-221 AND GLY-422.
RX PubMed=8281149; DOI=10.1093/hmg/2.11.1871;
RA Bunge S., Steglich C., Zuther C., Beck M., Morris C.P., Schwinger E.,
RA Schinzel A., Hopwood J.J., Gal A.;
RT "Iduronate-2-sulfatase gene mutations in 16 patients with
RT mucopolysaccharidosis type II (Hunter syndrome).";
RL Hum. Mol. Genet. 2:1871-1875(1993).
RN [17]
RP VARIANTS MPS2 GLU-68; HIS-293; GLY-478 AND ARG-485.
RX PubMed=7981716; DOI=10.1002/humu.1380040206;
RA Schroeder W., Wulff K., Wehnert M., Seidlitz G., Herrmann F.H.;
RT "Mutations of the iduronate-2-sulfatase (IDS) gene in patients with Hunter
RT syndrome (mucopolysaccharidosis II).";
RL Hum. Mutat. 4:128-131(1994).
RN [18]
RP VARIANT MPS2 PRO-410.
RX PubMed=7866405; DOI=10.1002/humu.1380040406;
RA Ben-Simon-Schiff E., Bach G., Hopwood J.J., Abeliovich D.;
RT "Mutation analysis of Jewish Hunter patients in Israel.";
RL Hum. Mutat. 4:263-270(1994).
RN [19]
RP VARIANTS MPS2 TRP-132; TYR-229; ARG-358; HIS-469 AND CYS-523.
RX PubMed=7887413;
RA Jonsson J.J., Aronovich E.L., Braun S.E., Whitley C.B.;
RT "Molecular diagnosis of mucopolysaccharidosis type II (Hunter syndrome) by
RT automated sequencing and computer-assisted interpretation: toward mutation
RT mapping of the iduronate-2-sulfatase gene.";
RL Am. J. Hum. Genet. 56:597-607(1995).
RN [20]
RP VARIANTS MPS2 LEU-86; ASN-87; PRO-92; ASN-135; CYS-345 AND TRP-468.
RX PubMed=7728156; DOI=10.1002/humu.1380050114;
RA Popowska E., Rathmann M., Tylki-Szymanska A., Bunge S., Steglich C.,
RA Schwinger E., Gal A.;
RT "Mutations of the iduronate-2-sulfatase gene in 12 Polish patients with
RT mucopolysaccharidosis type II (Hunter syndrome).";
RL Hum. Mutat. 5:97-100(1995).
RN [21]
RP VARIANTS MPS2 PRO-48; SER-117 DEL; LEU-333; ARG-337; LEU-468 AND GLN-468.
RX PubMed=7581397; DOI=10.1002/humu.1380060206;
RA Sukegawa K., Tomatsu S., Fukao T., Iwata H., Song X.-Q., Yamada Y.,
RA Fukuda S., Isogai K., Orii T.;
RT "Mucopolysaccharidosis type II (Hunter disease): identification and
RT characterization of eight point mutations in the iduronate-2-sulfatase gene
RT in Japanese patients.";
RL Hum. Mutat. 6:136-143(1995).
RN [22]
RP VARIANT MPS2 VAL-346.
RX PubMed=7599640; DOI=10.1002/humu.1380050314;
RA Li P., Huffman P., Thompson J.N.;
RT "Mutations of the iduronate-2-sulfatase gene on a T146T background in three
RT patients with Hunter syndrome.";
RL Hum. Mutat. 5:272-274(1995).
RN [23]
RP VARIANTS MPS2 ASP-63; THR-85; GLN-86; CYS-88; HIS-88; CYS-108; SER-117 DEL;
RP VAL-125; ARG-134; PHE-184; ASN-252; LEU-333; ILE-347; ARG-403 AND GLN-468.
RX PubMed=8940265;
RA Rathmann M., Bunge S., Beck M., Kresse H., Tylki-Szymanska A., Gal A.;
RT "Mucopolysaccharidosis type II (Hunter syndrome): mutation 'hot spots' in
RT the iduronate-2-sulfatase gene.";
RL Am. J. Hum. Genet. 59:1202-1209(1996).
RN [24]
RP VARIANTS MPS2 LEU-333 AND ASP-346.
RX PubMed=8566953; DOI=10.1007/bf02265265;
RA Olsen T.C., Eiken H.G., Knappskog P.M., Kase B.F., Mansson J.-E., Boman H.,
RA Apold J.;
RT "Mutations in the iduronate-2-sulfatase gene in five Norwegians with Hunter
RT syndrome.";
RL Hum. Genet. 97:198-203(1996).
RN [25]
RP VARIANTS MPS2 ASP-63; ARG-86; GLY-95; PRO-205; TRP-468 AND GLN-468.
RX PubMed=8664909;
RX DOI=10.1002/(sici)1098-1004(1996)7:1<76::aid-humu14>3.0.co;2-p;
RA Goldenfum S.L., Young E., Michelakakis H., Tsagarakis S., Winchester B.;
RT "Mutation analysis in 20 patients with Hunter disease.";
RL Hum. Mutat. 7:76-78(1996).
RN [26]
RP VARIANTS MPS2 LEU-333 AND GLY-334.
RX PubMed=8830188; DOI=10.1007/bf01799358;
RA Li P., Thompson J.N.;
RT "Detection of four novel mutations in the iduronate-2-sulphatase gene by
RT single-strand conformation polymorphism analysis of genomic amplicons.";
RL J. Inherit. Metab. Dis. 19:93-94(1996).
RN [27]
RP VARIANTS MPS2 ASP-63; THR-347; GLN-468 AND LEU-468.
RX PubMed=9222763;
RX DOI=10.1002/(sici)1098-1004(1997)10:1<71::aid-humu10>3.0.co;2-x;
RA Villani G.R.D., Balzano N., Grosso M., Salvadore F., Izzo P., di Natale P.;
RT "Mucopolysaccharidosis type II: identification of six novel mutations in
RT Italian patients.";
RL Hum. Mutat. 10:71-75(1997).
RN [28]
RP VARIANT MPS2 GLN-468.
RX PubMed=9375851;
RX DOI=10.1002/(sici)1098-1004(1997)10:5<361::aid-humu5>3.0.co;2-i;
RA Sukegawa K., Song X.-Q., Masuno M., Fukao T., Shimozawa N., Fukuda S.,
RA Isogai K., Nishio H., Matsuo M., Tomatsu S., Kondo N., Orii T.;
RT "Hunter disease in a girl caused by R468Q mutation in the iduronate-2-
RT sulfatase gene and skewed inactivation of the X chromosome carrying the
RT normal allele.";
RL Hum. Mutat. 10:361-367(1997).
RN [29]
RP VARIANTS MPS2 PHE-73; THR-118 DEL; HIS-121; TRP-132; ARG-336; LYS-341;
RP GLN-347; TRP-468; GLN-468; LYS-521 AND VAL-521.
RX PubMed=9266380; DOI=10.1023/a:1005335624386;
RA Lissens W., Seneca S., Liebaers I.;
RT "Molecular analysis in 23 Hunter disease families.";
RL J. Inherit. Metab. Dis. 20:453-456(1997).
RN [30]
RP VARIANTS MPS2 ASN-45; TYR-115; LEU-228; ARG-266; LYS-434; LYS-485 AND
RP CYS-502.
RX PubMed=9875019; DOI=10.1136/adc.79.3.237;
RA Vafiadaki E., Cooper A., Heptinstall L.E., Hatton C.E., Thornley M.,
RA Wraith J.E.;
RT "Mutation analysis in 57 unrelated patients with MPS II.";
RL Arch. Dis. Child. 79:237-241(1998).
RN [31]
RP VARIANTS MPS2 ASN-71; SER-85; THR-85; LEU-86; GLY-88; HIS-88; PHE-89;
RP SER-108; SER-117 DEL; ILE-118; ARG-121; ASP-138; HIS-148; ARG-229; LEU-333;
RP ASN-334; ARG-335; GLU-336; ARG-339; ARG-403; LEU-467; GLN-468; TRP-468;
RP ARG-480; GLN-480; LEU-480 AND SER-490.
RX PubMed=9660053; DOI=10.1111/j.1399-0004.1998.tb02746.x;
RA Froissart R., Maire I., Millat G., Cudry S., Birot A.-M., Bonnet V.,
RA Bouton O., Bozon D.;
RT "Identification of iduronate sulfatase gene alterations in 70 unrelated
RT Hunter patients.";
RL Clin. Genet. 53:362-368(1998).
RN [32]
RP VARIANTS MPS2 ASP-54; ASP-63; GLU-79; CYS-88; LEU-88; HIS-88; ARG-102;
RP PRO-159; SER-196; GLY-198; GLU-224; LEU-333; ASP-340; TYR-432; GLN-468;
RP TYR-478 AND ARG-485.
RX PubMed=9921913; DOI=10.1007/s004390050901;
RA Karsten S., Voskoboeva E., Tishkanina S., Pettersson U., Krasnopolskaya X.,
RA Bondeson M.-L.;
RT "Mutational spectrum of the iduronate-2-sulfatase (IDS) gene in 36
RT unrelated Russian MPS II patients.";
RL Hum. Genet. 103:732-735(1998).
RN [33]
RP VARIANTS MPS2 LEU-86; HIS-88; PRO-88; ILE-118 AND HIS-266.
RX PubMed=10215411;
RA Balzano N., Villani G.R.D., Grosso M., Izzo P., di Natale P.;
RT "Detection of four novel mutations in the iduronate-2-sulfatase gene.";
RL Hum. Mutat. 11:333-333(1998).
RN [34]
RP VARIANTS MPS2 THR-85; HIS-88; ILE-349 AND VAL-521.
RX PubMed=9452044; DOI=10.1002/humu.1380110123;
RA Gort L., Coll M.J., Chabas A.;
RT "Mutations in the iduronate-2-sulfatase gene in 12 Spanish patients with
RT Hunter disease.";
RL Hum. Mutat. Suppl. 1:S66-S68(1998).
RN [35]
RP VARIANTS MPS2 PHE-143; TRP-184; VAL-269 AND HIS-348.
RX PubMed=10671065;
RX DOI=10.1002/(sici)1098-1004(1998)12:6<433::aid-humu12>3.0.co;2-m;
RA Karsten S.L., Voskoboeva E., Carlberg B.-M., Kleijer W.J., Toennesen T.,
RA Pettersson U., Bondeson M.-L.;
RT "Identification of 9 novel gene mutations in 19 unrelated Hunter syndrome
RT (Mucopolysaccharidosis type II) patients.";
RL Hum. Mutat. 12:433-433(1998).
RN [36]
RP VARIANTS MPS2 PRO-48; THR-85; LEU-86; PRO-182; SER-196; ASP-225; MET-227;
RP ASN-308; PRO-314; LEU-333; ARG-337; ILE-349; GLN-468; LEU-468 AND TRP-468.
RX PubMed=9501270; DOI=10.1023/a:1005363414792;
RA Isogai K., Sukegawa K., Tomatsu S., Fukao T., Song X.-Q., Yamada Y.,
RA Fukuda S., Orii T., Kondo N.;
RT "Mutation analysis in the iduronate-2-sulphatase gene in 43 Japanese
RT patients with mucopolysaccharidosis type II (Hunter disease).";
RL J. Inherit. Metab. Dis. 21:60-70(1998).
RN [37]
RP VARIANTS MPS2 THR-228; ARG-229; LEU-231; GLU-308; ALA-309 AND CYS-313.
RX PubMed=9762601; DOI=10.1023/a:1005432600871;
RA Gort L., Chabas A., Coll M.J.;
RT "Hunter disease in the Spanish population: molecular analysis in 31
RT families.";
RL J. Inherit. Metab. Dis. 21:655-661(1998).
RN [38]
RP VARIANTS MPS2 PHE-143; LYS-341; TYR-342 AND PHE-491.
RX PubMed=10220152;
RX DOI=10.1002/(sici)1098-1004(1999)13:4<338::aid-humu15>3.0.co;2-3;
RA Vallance H.D., Bernard L., Rashed M., Chiu D., Le G., Toone J.,
RA Applegarth D.A., Coulter-Mackie M.;
RT "Identification of 6 new mutations in the iduronate sulfatase gene.";
RL Hum. Mutat. 13:338-338(1999).
RN [39]
RP VARIANTS MPS2 ASN-264; PRO-465 AND TRP-468.
RX PubMed=10447264;
RA Hartog C., Fryer A., Upadhyaya M.;
RT "Mutation analysis of iduronate-2-sulphatase gene in 24 patients with
RT Hunter syndrome: characterisation of 6 novel mutations.";
RL Hum. Mutat. 14:87-87(1999).
RN [40]
RP VARIANTS MPS2 ARG-71; GLU-82; THR-85; CYS-88; ARG-95 DEL; GLN-468; TRP-468
RP AND VAL-521.
RX PubMed=9950361;
RA Li P., Bellows A.B., Thompson J.N.;
RT "Molecular basis of iduronate-2-sulphatase gene mutations in patients with
RT mucopolysaccharidosis type II (Hunter syndrome).";
RL J. Med. Genet. 36:21-27(1999).
RN [41]
RP CHARACTERIZATION OF VARIANTS MPS2 HIS-88; PRO-88; ILE-118 AND GLN-468,
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10838181; DOI=10.1016/s0925-4439(00)00006-5;
RA Villani G.R.D., Daniele A., Balzano N., Di Natale P.;
RT "Expression of five iduronate-2-sulfatase site-directed mutations.";
RL Biochim. Biophys. Acta 1501:71-80(2000).
RN [42]
RP VARIANT MPS2 PRO-41, AND CHARACTERIZATION OF VARIANT MPS2 PRO-41.
RX PubMed=11015461; DOI=10.1136/jmg.37.10.e29;
RA Cudry S., Tigaud I., Froissart R., Bonnet V., Maire I., Bozon D.;
RT "MPS II in females: molecular basis of two different cases.";
RL J. Med. Genet. 37:E29-E29(2000).
RN [43]
RP VARIANTS MPS2 SER-117 DEL; ILE-265 AND THR-347, CHARACTERIZATION OF
RP VARIANTS MPS2 SER-117 DEL; ILE-265 AND THR-347, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RX PubMed=11731225; DOI=10.1016/s0925-4439(01)00075-8;
RA Bonuccelli G., Di Natale P., Corsolini F., Villani G., Regis S.,
RA Filocamo M.;
RT "The effect of four mutations on the expression of iduronate-2-sulfatase in
RT mucopolysaccharidosis type II.";
RL Biochim. Biophys. Acta 1537:233-238(2001).
RN [44]
RP VARIANTS MPS2 CYS-88; THR-95; ILE-181; ARG-422; LEU-467; GLN-468 AND
RP TRP-468.
RX PubMed=11683780; DOI=10.1034/j.1399-0004.2001.600412.x;
RA Moreira da Silva I., Froissart R., Marques dos Santos H., Caseiro C.,
RA Maire I., Bozon D.;
RT "Molecular basis of mucopolysaccharidosis type II in Portugal:
RT identification of four novel mutations.";
RL Clin. Genet. 60:316-318(2001).
RN [45]
RP VARIANT MPS2 488-ILE-ALA-489, AND CHARACTERIZATION OF VARIANT MPS2
RP 488-ILE-ALA-489.
RX PubMed=12794697; DOI=10.1002/ajmg.a.10215;
RA Ricci V., Filocamo M., Regis S., Corsolini F., Stroppiano M., Di Duca M.,
RA Gatti R.;
RT "Expression studies of two novel in CIS-mutations identified in an
RT intermediate case of Hunter syndrome.";
RL Am. J. Med. Genet. A 120:84-87(2003).
RN [46]
RP VARIANTS MPS2 LEU-41 DEL; TYR-117; PRO-259 AND ILE-299.
RX PubMed=12655569; DOI=10.1002/humu.9128;
RA Kim C.H., Hwang H.Z., Song S.M., Paik K.H., Kwon E.K., Moon K.B.,
RA Yoon J.H., Han C.K., Jin D.-K.;
RT "Mutational spectrum of the iduronate 2 sulfatase gene in 25 unrelated
RT Korean Hunter syndrome patients: identification of 13 novel mutations.";
RL Hum. Mutat. 21:449-450(2003).
RN [47]
RP VARIANTS MPS2 VAL-82 AND VAL-140, AND CHARACTERIZATION OF VARIANTS MPS2
RP VAL-82 AND VAL-140.
RX PubMed=16699754; DOI=10.1007/s00109-006-0057-1;
RA Lualdi S., Pittis M.G., Regis S., Parini R., Allegri A.E., Furlan F.,
RA Bembi B., Filocamo M.;
RT "Multiple cryptic splice sites can be activated by IDS point mutations
RT generating misspliced transcripts.";
RL J. Mol. Med. 84:692-700(2006).
CC -!- FUNCTION: Lysosomal enzyme involved in the degradation pathway of
CC dermatan sulfate and heparan sulfate. {ECO:0000269|PubMed:10838181,
CC ECO:0000269|PubMed:11731225, ECO:0000269|PubMed:28593992}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the 2-sulfate groups of the L-iduronate 2-
CC sulfate units of dermatan sulfate, heparan sulfate and heparin.;
CC EC=3.1.6.13; Evidence={ECO:0000269|PubMed:10838181,
CC ECO:0000269|PubMed:11731225, ECO:0000269|PubMed:28593992};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:28593992};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:28593992};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=327 uM for O-(alpha-L-idopyranosyluronic acid-2-sulfate)-(1->4)-
CC 2,5 anhydromannose-6-sulfate {ECO:0000269|PubMed:10838181};
CC -!- SUBUNIT: Monomer (PubMed:28593992). The 58-kDa mature form is composed
CC of two chains resulting from proteolitic processing, the 42-kDa chain
CC and the 14-kDa chain that remain stably associated and form the 58-kDa
CC intermediate form which is enzymatically active (PubMed:28593992).
CC {ECO:0000269|PubMed:28593992}.
CC -!- INTERACTION:
CC P22304; Q8NBJ7: SUMF2; NbExp=2; IntAct=EBI-2687288, EBI-723091;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:10838181}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=P22304-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P22304-2; Sequence=VSP_006301, VSP_006302;
CC Name=3;
CC IsoId=P22304-3; Sequence=VSP_039116, VSP_039117;
CC -!- TISSUE SPECIFICITY: Liver, kidney, lung, and placenta.
CC -!- PTM: Synthesized as a 75-kDa precursor form in the endoplasmic
CC reticulum (ER), and then processed by proteolytic cleavage through
CC various intermediates to yield a 55-kDa mature form, with the release
CC of an 18 kDa polypeptide. {ECO:0000269|PubMed:7626005}.
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|UniProtKB:P15289}.
CC -!- DISEASE: Mucopolysaccharidosis 2 (MPS2) [MIM:309900]: An X-linked
CC lysosomal storage disease characterized by intracellular accumulation
CC of heparan sulfate and dermatan sulfate and their excretion in urine.
CC Most children with MPS2 have a severe form with early somatic
CC abnormalities including skeletal deformities, hepatosplenomegaly, and
CC progressive cardiopulmonary deterioration. A prominent feature is
CC neurological damage that presents as developmental delay and
CC hyperactivity but progresses to intellectual disability and dementia.
CC They die before 15 years of age, usually as a result of obstructive
CC airway disease or cardiac failure. In contrast, those with a mild form
CC of MPS2 may survive into adulthood, with attenuated somatic
CC complications and often without intellectual disability.
CC {ECO:0000269|PubMed:10215411, ECO:0000269|PubMed:10220152,
CC ECO:0000269|PubMed:10447264, ECO:0000269|PubMed:10671065,
CC ECO:0000269|PubMed:10838181, ECO:0000269|PubMed:11015461,
CC ECO:0000269|PubMed:11683780, ECO:0000269|PubMed:11731225,
CC ECO:0000269|PubMed:12655569, ECO:0000269|PubMed:12794697,
CC ECO:0000269|PubMed:1284597, ECO:0000269|PubMed:1303211,
CC ECO:0000269|PubMed:16699754, ECO:0000269|PubMed:7581397,
CC ECO:0000269|PubMed:7599640, ECO:0000269|PubMed:7728156,
CC ECO:0000269|PubMed:7866405, ECO:0000269|PubMed:7887413,
CC ECO:0000269|PubMed:7981716, ECO:0000269|PubMed:8281149,
CC ECO:0000269|PubMed:8566953, ECO:0000269|PubMed:8664909,
CC ECO:0000269|PubMed:8830188, ECO:0000269|PubMed:8940265,
CC ECO:0000269|PubMed:9222763, ECO:0000269|PubMed:9266380,
CC ECO:0000269|PubMed:9375851, ECO:0000269|PubMed:9452044,
CC ECO:0000269|PubMed:9501270, ECO:0000269|PubMed:9660053,
CC ECO:0000269|PubMed:9762601, ECO:0000269|PubMed:9875019,
CC ECO:0000269|PubMed:9921913, ECO:0000269|PubMed:9950361}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M58342; AAA63197.1; -; mRNA.
DR EMBL; L13329; AAA16877.1; -; Genomic_DNA.
DR EMBL; L13321; AAA16877.1; JOINED; Genomic_DNA.
DR EMBL; L13322; AAA16877.1; JOINED; Genomic_DNA.
DR EMBL; L13323; AAA16877.1; JOINED; Genomic_DNA.
DR EMBL; L13324; AAA16877.1; JOINED; Genomic_DNA.
DR EMBL; L13325; AAA16877.1; JOINED; Genomic_DNA.
DR EMBL; L13326; AAA16877.1; JOINED; Genomic_DNA.
DR EMBL; L13327; AAA16877.1; JOINED; Genomic_DNA.
DR EMBL; L13328; AAA16877.1; JOINED; Genomic_DNA.
DR EMBL; L04586; AAA59192.1; -; Genomic_DNA.
DR EMBL; L04578; AAA59192.1; JOINED; Genomic_DNA.
DR EMBL; L04579; AAA59192.1; JOINED; Genomic_DNA.
DR EMBL; L04580; AAA59192.1; JOINED; Genomic_DNA.
DR EMBL; L04581; AAA59192.1; JOINED; Genomic_DNA.
DR EMBL; L04583; AAA59192.1; JOINED; Genomic_DNA.
DR EMBL; L04582; AAA59192.1; JOINED; Genomic_DNA.
DR EMBL; L04584; AAA59192.1; JOINED; Genomic_DNA.
DR EMBL; L04585; AAA59192.1; JOINED; Genomic_DNA.
DR EMBL; L40586; AAA92014.1; -; mRNA.
DR EMBL; AC233288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471171; EAW61282.1; -; Genomic_DNA.
DR EMBL; CH471171; EAW61281.1; -; Genomic_DNA.
DR EMBL; CH471171; EAW61283.1; -; Genomic_DNA.
DR EMBL; BC006170; AAH06170.1; -; mRNA.
DR EMBL; AF011889; AAC77828.1; -; Genomic_DNA.
DR CCDS; CCDS14685.1; -. [P22304-1]
DR CCDS; CCDS14686.1; -. [P22304-2]
DR PIR; A47535; KJHUID.
DR RefSeq; NP_000193.1; NM_000202.7. [P22304-1]
DR RefSeq; NP_001160022.1; NM_001166550.3.
DR RefSeq; NP_006114.1; NM_006123.4. [P22304-2]
DR PDB; 5FQL; X-ray; 2.30 A; A=26-550.
DR PDB; 6IOZ; X-ray; 3.10 A; A=34-550.
DR PDBsum; 5FQL; -.
DR PDBsum; 6IOZ; -.
DR AlphaFoldDB; P22304; -.
DR SMR; P22304; -.
DR BioGRID; 109649; 145.
DR IntAct; P22304; 31.
DR MINT; P22304; -.
DR STRING; 9606.ENSP00000339801; -.
DR DrugBank; DB09301; Chondroitin sulfate.
DR Allergome; 9623; Hom s Idursulfase.
DR GlyGen; P22304; 8 sites.
DR iPTMnet; P22304; -.
DR PhosphoSitePlus; P22304; -.
DR BioMuta; IDS; -.
DR DMDM; 124174; -.
DR EPD; P22304; -.
DR jPOST; P22304; -.
DR MassIVE; P22304; -.
DR MaxQB; P22304; -.
DR PaxDb; P22304; -.
DR PeptideAtlas; P22304; -.
DR PRIDE; P22304; -.
DR ProteomicsDB; 53975; -. [P22304-1]
DR ProteomicsDB; 53976; -. [P22304-2]
DR ProteomicsDB; 53977; -. [P22304-3]
DR TopDownProteomics; P22304-3; -. [P22304-3]
DR Antibodypedia; 35279; 329 antibodies from 33 providers.
DR DNASU; 3423; -.
DR Ensembl; ENST00000340855.11; ENSP00000339801.6; ENSG00000010404.18. [P22304-1]
DR Ensembl; ENST00000370441.8; ENSP00000359470.4; ENSG00000010404.18. [P22304-2]
DR Ensembl; ENST00000466323.5; ENSP00000418264.1; ENSG00000010404.18. [P22304-3]
DR GeneID; 3423; -.
DR KEGG; hsa:3423; -.
DR MANE-Select; ENST00000340855.11; ENSP00000339801.6; NM_000202.8; NP_000193.1.
DR UCSC; uc011mxe.3; human. [P22304-1]
DR CTD; 3423; -.
DR DisGeNET; 3423; -.
DR GeneCards; IDS; -.
DR GeneReviews; IDS; -.
DR HGNC; HGNC:5389; IDS.
DR HPA; ENSG00000010404; Tissue enriched (brain).
DR MalaCards; IDS; -.
DR MIM; 300823; gene.
DR MIM; 309900; phenotype.
DR neXtProt; NX_P22304; -.
DR OpenTargets; ENSG00000010404; -.
DR Orphanet; 217093; Mucopolysaccharidosis type 2, attenuated form.
DR Orphanet; 217085; Mucopolysaccharidosis type 2, severe form.
DR PharmGKB; PA29636; -.
DR VEuPathDB; HostDB:ENSG00000010404; -.
DR eggNOG; KOG3867; Eukaryota.
DR GeneTree; ENSGT00940000156803; -.
DR HOGENOM; CLU_006332_9_0_1; -.
DR InParanoid; P22304; -.
DR OMA; PHLDAFA; -.
DR OrthoDB; 1353742at2759; -.
DR PhylomeDB; P22304; -.
DR TreeFam; TF323156; -.
DR BioCyc; MetaCyc:HS00286-MON; -.
DR BRENDA; 3.1.6.13; 2681.
DR PathwayCommons; P22304; -.
DR Reactome; R-HSA-2024096; HS-GAG degradation.
DR Reactome; R-HSA-2024101; CS/DS degradation.
DR Reactome; R-HSA-2206296; MPS II - Hunter syndrome.
DR SABIO-RK; P22304; -.
DR SignaLink; P22304; -.
DR BioGRID-ORCS; 3423; 5 hits in 700 CRISPR screens.
DR ChiTaRS; IDS; human.
DR GeneWiki; Iduronate-2-sulfatase; -.
DR GenomeRNAi; 3423; -.
DR Pharos; P22304; Tbio.
DR PRO; PR:P22304; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P22304; protein.
DR Bgee; ENSG00000010404; Expressed in right frontal lobe and 163 other tissues.
DR ExpressionAtlas; P22304; baseline and differential.
DR Genevisible; P22304; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004423; F:iduronate-2-sulfatase activity; IDA:UniProtKB.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IDA:UniProtKB.
DR CDD; cd16030; iduronate-2-sulfatase; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR035874; IDS.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 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 3D-structure; Alternative splicing; Calcium; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW Metal-binding; Mucopolysaccharidosis; Reference proteome; Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..33
FT /evidence="ECO:0000269|PubMed:2122463"
FT /id="PRO_0000033428"
FT CHAIN 34..455
FT /note="Iduronate 2-sulfatase 42 kDa chain"
FT /id="PRO_0000033429"
FT CHAIN 456..550
FT /note="Iduronate 2-sulfatase 14 kDa chain"
FT /id="PRO_0000033430"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000269|Ref.13"
FT ACT_SITE 138
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:1303211,
FT ECO:0007744|PDB:5FQL"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT MOD_RES 84
FT /note="3-oxoalanine (Cys)"
FT /evidence="ECO:0000269|Ref.13"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218, ECO:0000269|Ref.13,
FT ECO:0007744|PDB:5FQL"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT DISULFID 171..184
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT DISULFID 422..432
FT /evidence="ECO:0000269|Ref.13, ECO:0007744|PDB:5FQL"
FT VAR_SEQ 294..312
FT /note="RKIRQSYFASVSYLDTQVG -> EDQSSTGFRLKTSSTRKYK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039116"
FT VAR_SEQ 313..550
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039117"
FT VAR_SEQ 337..343
FT /note="WALGEHG -> FLMRTNT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8530090"
FT /id="VSP_006301"
FT VAR_SEQ 344..550
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8530090"
FT /id="VSP_006302"
FT VARIANT 41
FT /note="L -> P (in MPS2; mild form; increase in enzyme
FT activity observed in transfected cells)"
FT /evidence="ECO:0000269|PubMed:11015461"
FT /id="VAR_026915"
FT VARIANT 41
FT /note="Missing (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:12655569"
FT /id="VAR_026914"
FT VARIANT 45
FT /note="D -> N (in MPS2)"
FT /evidence="ECO:0000269|PubMed:9875019"
FT /id="VAR_007313"
FT VARIANT 48
FT /note="R -> P (in MPS2; mild form; dbSNP:rs1569560528)"
FT /evidence="ECO:0000269|PubMed:7581397,
FT ECO:0000269|PubMed:9501270"
FT /id="VAR_007314"
FT VARIANT 54
FT /note="Y -> D (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9921913"
FT /id="VAR_007315"
FT VARIANT 63
FT /note="N -> D (in MPS2; mild/intermediate form;
FT dbSNP:rs193302909)"
FT /evidence="ECO:0000269|PubMed:8664909,
FT ECO:0000269|PubMed:8940265, ECO:0000269|PubMed:9222763,
FT ECO:0000269|PubMed:9921913"
FT /id="VAR_007316"
FT VARIANT 68
FT /note="A -> E (in MPS2; severe)"
FT /evidence="ECO:0000269|PubMed:7981716"
FT /id="VAR_007317"
FT VARIANT 71
FT /note="S -> N (in MPS2; mild form; dbSNP:rs113993954)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026916"
FT VARIANT 71
FT /note="S -> R (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9950361"
FT /id="VAR_008998"
FT VARIANT 73
FT /note="L -> F (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9266380"
FT /id="VAR_026917"
FT VARIANT 79
FT /note="A -> E (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:9921913"
FT /id="VAR_007318"
FT VARIANT 82
FT /note="A -> E (in MPS2)"
FT /evidence="ECO:0000269|PubMed:9950361"
FT /id="VAR_008999"
FT VARIANT 82
FT /note="A -> V (in MPS2; no significant enzyme activity)"
FT /evidence="ECO:0000269|PubMed:16699754"
FT /id="VAR_026918"
FT VARIANT 85
FT /note="A -> S (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026919"
FT VARIANT 85
FT /note="A -> T (in MPS2; mild to severe forms;
FT dbSNP:rs113993949)"
FT /evidence="ECO:0000269|PubMed:8940265,
FT ECO:0000269|PubMed:9452044, ECO:0000269|PubMed:9501270,
FT ECO:0000269|PubMed:9660053, ECO:0000269|PubMed:9950361"
FT /id="VAR_007319"
FT VARIANT 86
FT /note="P -> L (in MPS2; intermediate to severe forms;
FT dbSNP:rs1557340280)"
FT /evidence="ECO:0000269|PubMed:10215411,
FT ECO:0000269|PubMed:7728156, ECO:0000269|PubMed:9501270,
FT ECO:0000269|PubMed:9660053"
FT /id="VAR_007320"
FT VARIANT 86
FT /note="P -> Q (in MPS2)"
FT /evidence="ECO:0000269|PubMed:8940265"
FT /id="VAR_007321"
FT VARIANT 86
FT /note="P -> R (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:8281149,
FT ECO:0000269|PubMed:8664909"
FT /id="VAR_007322"
FT VARIANT 87
FT /note="S -> N (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:7728156"
FT /id="VAR_007323"
FT VARIANT 88
FT /note="R -> C (in MPS2; severe form; dbSNP:rs398123249)"
FT /evidence="ECO:0000269|PubMed:11683780,
FT ECO:0000269|PubMed:8940265, ECO:0000269|PubMed:9921913,
FT ECO:0000269|PubMed:9950361"
FT /id="VAR_007324"
FT VARIANT 88
FT /note="R -> G (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026920"
FT VARIANT 88
FT /note="R -> H (in MPS2; intermediate/severe form; higher
FT affinity for the artificial substrate; poor transport to
FT lysosomes)"
FT /evidence="ECO:0000269|PubMed:10215411,
FT ECO:0000269|PubMed:10838181, ECO:0000269|PubMed:8940265,
FT ECO:0000269|PubMed:9452044, ECO:0000269|PubMed:9660053,
FT ECO:0000269|PubMed:9921913"
FT /id="VAR_007325"
FT VARIANT 88
FT /note="R -> L (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9921913"
FT /id="VAR_007326"
FT VARIANT 88
FT /note="R -> P (in MPS2; severe form; total absence of
FT residual activity; poor transport to lysosomes)"
FT /evidence="ECO:0000269|PubMed:10215411,
FT ECO:0000269|PubMed:10838181"
FT /id="VAR_007327"
FT VARIANT 89
FT /note="V -> F (in MPS2)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026921"
FT VARIANT 92
FT /note="L -> P (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:7728156"
FT /id="VAR_007328"
FT VARIANT 94
FT /note="G -> D (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:8281149"
FT /id="VAR_007329"
FT VARIANT 95
FT /note="R -> G (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:8664909"
FT /id="VAR_026922"
FT VARIANT 95
FT /note="R -> T (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:11683780"
FT /id="VAR_026923"
FT VARIANT 95
FT /note="Missing (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9950361"
FT /id="VAR_009000"
FT VARIANT 102
FT /note="L -> R (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:9921913"
FT /id="VAR_007330"
FT VARIANT 108
FT /note="Y -> C (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:8940265"
FT /id="VAR_007331"
FT VARIANT 108
FT /note="Y -> S (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026924"
FT VARIANT 115
FT /note="N -> Y (in MPS2)"
FT /evidence="ECO:0000269|PubMed:9875019"
FT /id="VAR_007332"
FT VARIANT 117
FT /note="S -> Y (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:12655569"
FT /id="VAR_026926"
FT VARIANT 117
FT /note="Missing (in MPS2; severe form; deleterious mutation;
FT results in an inactive enzyme; dbSNP:rs483352905)"
FT /evidence="ECO:0000269|PubMed:11731225,
FT ECO:0000269|PubMed:7581397, ECO:0000269|PubMed:8940265,
FT ECO:0000269|PubMed:9660053"
FT /id="VAR_026925"
FT VARIANT 118
FT /note="T -> I (in MPS2; mild to severe forms; greatly
FT reduced activity; poor transport to lysosomes)"
FT /evidence="ECO:0000269|PubMed:10215411,
FT ECO:0000269|PubMed:10838181, ECO:0000269|PubMed:9660053"
FT /id="VAR_007333"
FT VARIANT 118
FT /note="Missing (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9266380"
FT /id="VAR_026927"
FT VARIANT 120
FT /note="P -> H (in MPS2; mild form; dbSNP:rs193302911)"
FT /id="VAR_007334"
FT VARIANT 120
FT /note="P -> R (in MPS2; severe form; dbSNP:rs193302911)"
FT /evidence="ECO:0000269|PubMed:8281149"
FT /id="VAR_007335"
FT VARIANT 121
FT /note="Q -> H (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9266380"
FT /id="VAR_026928"
FT VARIANT 121
FT /note="Q -> R (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026929"
FT VARIANT 125
FT /note="E -> V (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:8940265"
FT /id="VAR_007336"
FT VARIANT 132
FT /note="S -> W (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:7887413,
FT ECO:0000269|PubMed:9266380"
FT /id="VAR_007337"
FT VARIANT 134
FT /note="G -> R (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:8940265"
FT /id="VAR_007338"
FT VARIANT 135
FT /note="K -> N (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:7728156"
FT /id="VAR_007339"
FT VARIANT 135
FT /note="K -> R (in MPS2; intermediate form;
FT dbSNP:rs104894861)"
FT /evidence="ECO:0000269|PubMed:1303211"
FT /id="VAR_007340"
FT VARIANT 138
FT /note="H -> D (in MPS2; mild/intermediate form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026930"
FT VARIANT 140
FT /note="G -> V (in MPS2; no significant enzyme activity)"
FT /evidence="ECO:0000269|PubMed:16699754"
FT /id="VAR_026931"
FT VARIANT 143
FT /note="S -> F (in MPS2)"
FT /evidence="ECO:0000269|PubMed:10220152,
FT ECO:0000269|PubMed:10671065"
FT /id="VAR_007341"
FT VARIANT 148
FT /note="D -> H (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026932"
FT VARIANT 159
FT /note="H -> P (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9921913"
FT /id="VAR_007342"
FT VARIANT 159
FT /note="Missing (in MPS2; intermediate form)"
FT /id="VAR_007343"
FT VARIANT 160
FT /note="P -> R (in MPS2; dbSNP:rs104894856)"
FT /id="VAR_007344"
FT VARIANT 181
FT /note="N -> I (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:11683780"
FT /id="VAR_026933"
FT VARIANT 182
FT /note="L -> P (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:9501270"
FT /id="VAR_026934"
FT VARIANT 184
FT /note="C -> F (in MPS2; mild/intermediate form)"
FT /evidence="ECO:0000269|PubMed:8940265"
FT /id="VAR_007345"
FT VARIANT 184
FT /note="C -> W (in MPS2)"
FT /evidence="ECO:0000269|PubMed:10671065"
FT /id="VAR_007346"
FT VARIANT 196
FT /note="L -> S (in MPS2; mild/intermediate form;
FT dbSNP:rs398123250)"
FT /evidence="ECO:0000269|PubMed:9501270,
FT ECO:0000269|PubMed:9921913"
FT /id="VAR_007347"
FT VARIANT 198
FT /note="D -> G (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:9921913"
FT /id="VAR_007348"
FT VARIANT 205
FT /note="A -> P (in MPS2; intermediate form;
FT dbSNP:rs864622779)"
FT /evidence="ECO:0000269|PubMed:8664909"
FT /id="VAR_026935"
FT VARIANT 221
FT /note="L -> P (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:8281149"
FT /id="VAR_007349"
FT VARIANT 224
FT /note="G -> E (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9921913"
FT /id="VAR_007350"
FT VARIANT 225
FT /note="Y -> D (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:9501270"
FT /id="VAR_007351"
FT VARIANT 227
FT /note="K -> M (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:9501270"
FT /id="VAR_026936"
FT VARIANT 227
FT /note="K -> Q (in MPS2; severe form)"
FT /id="VAR_007352"
FT VARIANT 228
FT /note="P -> L (in MPS2)"
FT /evidence="ECO:0000269|PubMed:9875019"
FT /id="VAR_007353"
FT VARIANT 228
FT /note="P -> T (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9762601"
FT /id="VAR_026937"
FT VARIANT 229
FT /note="H -> R (in MPS2; intermediate/severe form;
FT dbSNP:rs193302905)"
FT /evidence="ECO:0000269|PubMed:9660053,
FT ECO:0000269|PubMed:9762601"
FT /id="VAR_026938"
FT VARIANT 229
FT /note="H -> Y (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:7887413"
FT /id="VAR_007354"
FT VARIANT 231
FT /note="P -> L (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:9762601"
FT /id="VAR_026939"
FT VARIANT 252
FT /note="D -> N (in MPS2; dbSNP:rs146458524)"
FT /evidence="ECO:0000269|PubMed:8940265"
FT /id="VAR_007355"
FT VARIANT 259
FT /note="L -> P (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:12655569"
FT /id="VAR_026940"
FT VARIANT 264
FT /note="Y -> N (in MPS2)"
FT /evidence="ECO:0000269|PubMed:10447264"
FT /id="VAR_009001"
FT VARIANT 265
FT /note="N -> I (in MPS2; intermediate form; deleterious
FT mutation; residual activity of 7.5% of the wild-type)"
FT /evidence="ECO:0000269|PubMed:11731225"
FT /id="VAR_026941"
FT VARIANT 266
FT /note="P -> H (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:10215411"
FT /id="VAR_007356"
FT VARIANT 266
FT /note="P -> R (in MPS2)"
FT /evidence="ECO:0000269|PubMed:9875019"
FT /id="VAR_007357"
FT VARIANT 269
FT /note="D -> V (in MPS2; dbSNP:rs1085308006)"
FT /evidence="ECO:0000269|PubMed:10671065"
FT /id="VAR_007358"
FT VARIANT 293
FT /note="Q -> H (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:7981716"
FT /id="VAR_007359"
FT VARIANT 299
FT /note="S -> I (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:12655569"
FT /id="VAR_026942"
FT VARIANT 308
FT /note="D -> E (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:9762601"
FT /id="VAR_026943"
FT VARIANT 308
FT /note="D -> N (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:9501270"
FT /id="VAR_026944"
FT VARIANT 309
FT /note="T -> A (in MPS2; severe form; dbSNP:rs145807417)"
FT /evidence="ECO:0000269|PubMed:9762601"
FT /id="VAR_026945"
FT VARIANT 313
FT /note="R -> C (in MPS2; unknown pathological significance;
FT dbSNP:rs201048643)"
FT /evidence="ECO:0000269|PubMed:9762601"
FT /id="VAR_026946"
FT VARIANT 314
FT /note="L -> P (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9501270"
FT /id="VAR_026947"
FT VARIANT 333
FT /note="S -> L (in MPS2; severe form; dbSNP:rs104894853)"
FT /evidence="ECO:0000269|PubMed:7581397,
FT ECO:0000269|PubMed:8566953, ECO:0000269|PubMed:8830188,
FT ECO:0000269|PubMed:8940265, ECO:0000269|PubMed:9501270,
FT ECO:0000269|PubMed:9660053, ECO:0000269|PubMed:9921913"
FT /id="VAR_007360"
FT VARIANT 334
FT /note="D -> G (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:8830188"
FT /id="VAR_009002"
FT VARIANT 334
FT /note="D -> N (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026948"
FT VARIANT 335
FT /note="H -> R (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026949"
FT VARIANT 336
FT /note="G -> E (in MPS2; severe from)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026950"
FT VARIANT 336
FT /note="G -> R (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9266380"
FT /id="VAR_026951"
FT VARIANT 337
FT /note="W -> R (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:7581397,
FT ECO:0000269|PubMed:9501270"
FT /id="VAR_007361"
FT VARIANT 339
FT /note="L -> R (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026952"
FT VARIANT 340
FT /note="G -> D (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:9921913"
FT /id="VAR_007362"
FT VARIANT 341
FT /note="E -> K (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:10220152,
FT ECO:0000269|PubMed:9266380"
FT /id="VAR_008134"
FT VARIANT 342
FT /note="H -> Y (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:10220152"
FT /id="VAR_008135"
FT VARIANT 345
FT /note="W -> C (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:7728156"
FT /id="VAR_007363"
FT VARIANT 346
FT /note="A -> D (in MPS2; mild/severe form)"
FT /evidence="ECO:0000269|PubMed:8566953"
FT /id="VAR_007364"
FT VARIANT 346
FT /note="A -> V (in MPS2; mild/severe form)"
FT /evidence="ECO:0000269|PubMed:7599640"
FT /id="VAR_007365"
FT VARIANT 347
FT /note="K -> I (in MPS2)"
FT /evidence="ECO:0000269|PubMed:8940265"
FT /id="VAR_007366"
FT VARIANT 347
FT /note="K -> Q (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9266380"
FT /id="VAR_026953"
FT VARIANT 347
FT /note="K -> T (in MPS2; severe form; deleterious mutation
FT confirmed)"
FT /evidence="ECO:0000269|PubMed:11731225,
FT ECO:0000269|PubMed:9222763"
FT /id="VAR_007367"
FT VARIANT 348
FT /note="Y -> H (in MPS2)"
FT /evidence="ECO:0000269|PubMed:10671065"
FT /id="VAR_007368"
FT VARIANT 349
FT /note="S -> I (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9452044,
FT ECO:0000269|PubMed:9501270"
FT /id="VAR_007369"
FT VARIANT 358
FT /note="P -> R (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:7887413"
FT /id="VAR_007370"
FT VARIANT 403
FT /note="L -> R (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:8940265,
FT ECO:0000269|PubMed:9660053"
FT /id="VAR_007371"
FT VARIANT 410
FT /note="L -> P (in MPS2)"
FT /evidence="ECO:0000269|PubMed:7866405"
FT /id="VAR_026954"
FT VARIANT 422
FT /note="C -> G (in MPS2; mild form; dbSNP:rs199422229)"
FT /evidence="ECO:0000269|PubMed:1303211,
FT ECO:0000269|PubMed:8281149"
FT /id="VAR_007372"
FT VARIANT 422
FT /note="C -> R (in MPS2; severe form; dbSNP:rs199422229)"
FT /evidence="ECO:0000269|PubMed:11683780"
FT /id="VAR_026955"
FT VARIANT 432
FT /note="C -> Y (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9921913"
FT /id="VAR_007373"
FT VARIANT 434
FT /note="E -> K (in MPS2)"
FT /evidence="ECO:0000269|PubMed:9875019"
FT /id="VAR_007374"
FT VARIANT 465
FT /note="Q -> P (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:10447264"
FT /id="VAR_009003"
FT VARIANT 467
FT /note="P -> L (in MPS2; severe form; dbSNP:rs1602725808)"
FT /evidence="ECO:0000269|PubMed:11683780,
FT ECO:0000269|PubMed:9660053"
FT /id="VAR_026956"
FT VARIANT 468
FT /note="R -> G (in MPS2; mild to severe forms)"
FT /id="VAR_007375"
FT VARIANT 468
FT /note="R -> L (in MPS2; mild to severe forms;
FT dbSNP:rs113993946)"
FT /evidence="ECO:0000269|PubMed:7581397,
FT ECO:0000269|PubMed:9222763, ECO:0000269|PubMed:9501270"
FT /id="VAR_007376"
FT VARIANT 468
FT /note="R -> Q (in MPS2; severe/intermediate form; greatly
FT reduced activity; poor transport to lysosomes;
FT dbSNP:rs113993946)"
FT /evidence="ECO:0000269|PubMed:10838181,
FT ECO:0000269|PubMed:11683780, ECO:0000269|PubMed:7581397,
FT ECO:0000269|PubMed:8664909, ECO:0000269|PubMed:8940265,
FT ECO:0000269|PubMed:9222763, ECO:0000269|PubMed:9266380,
FT ECO:0000269|PubMed:9375851, ECO:0000269|PubMed:9501270,
FT ECO:0000269|PubMed:9660053, ECO:0000269|PubMed:9921913,
FT ECO:0000269|PubMed:9950361"
FT /id="VAR_007377"
FT VARIANT 468
FT /note="R -> W (in MPS2; mild to severe forms;
FT dbSNP:rs199422231)"
FT /evidence="ECO:0000269|PubMed:10447264,
FT ECO:0000269|PubMed:11683780, ECO:0000269|PubMed:1284597,
FT ECO:0000269|PubMed:7728156, ECO:0000269|PubMed:8664909,
FT ECO:0000269|PubMed:9266380, ECO:0000269|PubMed:9501270,
FT ECO:0000269|PubMed:9660053, ECO:0000269|PubMed:9950361"
FT /id="VAR_007378"
FT VARIANT 469
FT /note="P -> H (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:7887413"
FT /id="VAR_007379"
FT VARIANT 478
FT /note="D -> G (in MPS2; mild form; dbSNP:rs864622773)"
FT /evidence="ECO:0000269|PubMed:7981716"
FT /id="VAR_007380"
FT VARIANT 478
FT /note="D -> Y (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9921913"
FT /id="VAR_007381"
FT VARIANT 480
FT /note="P -> L (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026957"
FT VARIANT 480
FT /note="P -> Q (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026958"
FT VARIANT 480
FT /note="P -> R (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026959"
FT VARIANT 485
FT /note="I -> K (in MPS2)"
FT /evidence="ECO:0000269|PubMed:9875019"
FT /id="VAR_007382"
FT VARIANT 485
FT /note="I -> R (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:7981716,
FT ECO:0000269|PubMed:9921913"
FT /id="VAR_007383"
FT VARIANT 488..489
FT /note="MG -> IA (in MPS2; intermediate form; mutation A-489
FT confirmed as causative of MPS2)"
FT /id="VAR_026960"
FT VARIANT 490
FT /note="Y -> S (in MPS2; intermediate form)"
FT /evidence="ECO:0000269|PubMed:9660053"
FT /id="VAR_026961"
FT VARIANT 491
FT /note="S -> F (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:10220152"
FT /id="VAR_008136"
FT VARIANT 502
FT /note="W -> C (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9875019"
FT /id="VAR_007384"
FT VARIANT 502
FT /note="W -> S (in MPS2; dbSNP:rs199422228)"
FT /id="VAR_007385"
FT VARIANT 521
FT /note="E -> K (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9266380"
FT /id="VAR_026962"
FT VARIANT 521
FT /note="E -> V (in MPS2; severe form)"
FT /evidence="ECO:0000269|PubMed:9266380,
FT ECO:0000269|PubMed:9452044, ECO:0000269|PubMed:9950361"
FT /id="VAR_007386"
FT VARIANT 523
FT /note="Y -> C (in MPS2; mild form)"
FT /evidence="ECO:0000269|PubMed:7887413"
FT /id="VAR_007387"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:5FQL"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:5FQL"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 197..212
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6IOZ"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 229..235
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:5FQL"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 290..320
FT /evidence="ECO:0007829|PDB:5FQL"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:5FQL"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 395..402
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 406..413
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 457..460
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 462..469
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 495..506
FT /evidence="ECO:0007829|PDB:5FQL"
FT TURN 507..510
FT /evidence="ECO:0007829|PDB:5FQL"
FT STRAND 511..524
FT /evidence="ECO:0007829|PDB:5FQL"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:5FQL"
FT HELIX 542..548
FT /evidence="ECO:0007829|PDB:5FQL"
SQ SEQUENCE 550 AA; 61873 MW; EA1B713417280413 CRC64;
MPPPRTGRGL LWLGLVLSSV CVALGSETQA NSTTDALNVL LIIVDDLRPS LGCYGDKLVR
SPNIDQLASH SLLFQNAFAQ QAVCAPSRVS FLTGRRPDTT RLYDFNSYWR VHAGNFSTIP
QYFKENGYVT MSVGKVFHPG ISSNHTDDSP YSWSFPPYHP SSEKYENTKT CRGPDGELHA
NLLCPVDVLD VPEGTLPDKQ STEQAIQLLE KMKTSASPFF LAVGYHKPHI PFRYPKEFQK
LYPLENITLA PDPEVPDGLP PVAYNPWMDI RQREDVQALN ISVPYGPIPV DFQRKIRQSY
FASVSYLDTQ VGRLLSALDD LQLANSTIIA FTSDHGWALG EHGEWAKYSN FDVATHVPLI
FYVPGRTASL PEAGEKLFPY LDPFDSASQL MEPGRQSMDL VELVSLFPTL AGLAGLQVPP
RCPVPSFHVE LCREGKNLLK HFRFRDLEED PYLPGNPREL IAYSQYPRPS DIPQWNSDKP
SLKDIKIMGY SIRTIDYRYT VWVGFNPDEF LANFSDIHAG ELYFVDSDPL QDHNMYNDSQ
GGDLFQLLMP
