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 27-MAR-2024, entry version 225. 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; RX DOI=10.1002/(sici)1098-1004(1998)11:4<333::aid-humu18>3.0.co;2-g; 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; RX DOI=10.1002/(sici)1098-1004(1999)14:1<87::aid-humu14>3.0.co;2-n; 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-MET-GLY-489 DELINS ILE-ALA, AND CHARACTERIZATION OF RP VARIANT MPS2 488-MET-GLY-489 DELINS ILE-ALA. 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 CC acid-2-sulfate)-(1->4)-2,5 anhydromannose-6-sulfate CC {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; 34. DR MINT; P22304; -. DR STRING; 9606.ENSP00000339801; -. DR DrugBank; DB09301; Chondroitin sulfate. DR Allergome; 9623; Hom s Idursulfase. DR GlyCosmos; P22304; 7 sites, No reported glycans. DR GlyGen; P22304; 8 sites, 3 N-linked glycans (2 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; 9606-ENSP00000339801; -. DR PeptideAtlas; 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; 360 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 AGR; HGNC:5389; -. 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; HVFTRAY; -. DR OrthoDB; 2964021at2759; -. DR PhylomeDB; P22304; -. DR TreeFam; TF323156; -. DR BioCyc; MetaCyc:HS00286-MONOMER; -. 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 776 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 165 other cell types or tissues. DR ExpressionAtlas; P22304; baseline and differential. 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:0030209; P:dermatan sulfate catabolic process; IEA:Ensembl. DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IDA:UniProtKB. DR GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; IEA:Ensembl. DR CDD; cd16030; iduronate-2-sulfatase; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR InterPro; IPR035874; IDS. DR InterPro; IPR024607; Sulfatase_CS. DR InterPro; IPR000917; Sulfatase_N. DR PANTHER; PTHR45953; IDURONATE 2-SULFATASE; 1. DR PANTHER; PTHR45953:SF1; IDURONATE 2-SULFATASE; 1. DR Pfam; PF00884; Sulfatase; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. DR PROSITE; PS00523; SULFATASE_1; 1. DR PROSITE; PS00149; SULFATASE_2; 1. DR Genevisible; P22304; HS. 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; dbSNP:rs2089497431)" 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; dbSNP:rs2089497300)" 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; uncertain 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; dbSNP:rs2089378583)" 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; dbSNP:rs2089343220)" 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 /evidence="ECO:0000269|PubMed:12794697" 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; dbSNP:rs2089303696)" 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 //