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P35475 (IDUA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-L-iduronidase

EC=3.2.1.76
Gene names
Name:IDUA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length653 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate. Ref.5 Ref.6

Subunit structure

Monomer. Ref.6

Subcellular location

Lysosome.

Tissue specificity

Ubiquitous.

Post-translational modification

N-glycosylation at Asn-372 contributes to substrate binding and is required for full enzymatic activity.

Involvement in disease

Mucopolysaccharidosis 1H (MPS1H) [MIM:607014]: A severe form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. Patients with MPS1H usually present, within the first year of life, a combination of hepatosplenomegaly, skeletal deformities, corneal clouding and severe mental retardation. Obstructive airways disease, respiratory infection and cardiac complications usually result in death before 10 years of age.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Mucopolysaccharidosis 1H/S (MPS1H/S) [MIM:607015]: A form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. MPS1H/S represents an intermediate phenotype of the MPS1 clinical spectrum. It is characterized by relatively little neurological involvement, but most of the somatic symptoms described for severe MPS1 develop in the early to mid-teens, causing considerable loss of mobility.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.15 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23

Mucopolysaccharidosis 1S (MPS1S) [MIM:607016]: A mild form of mucopolysaccharidosis type 1, a rare lysosomal storage disease characterized by progressive physical deterioration with urinary excretion of dermatan sulfate and heparan sulfate. Patients with MPS1S may have little or no neurological involvement, normal stature and life span, but present development of joints stiffness, mild hepatosplenomegaly, aortic valve disease and corneal clouding.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.15 Ref.16 Ref.21 Ref.22 Ref.23

Sequence similarities

Belongs to the glycosyl hydrolase 39 family.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Mucopolysaccharidosis
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

chemical homeostasis

Inferred from electronic annotation. Source: Ensembl

chondroitin sulfate catabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate metabolic process

Traceable author statement. Source: Reactome

dermatan sulfate catabolic process

Inferred from direct assay Ref.5. Source: UniProtKB

disaccharide metabolic process

Traceable author statement PubMed 2470345. Source: ProtInc

glycosaminoglycan catabolic process

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

lysosome organization

Inferred from electronic annotation. Source: Ensembl

skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcoated vesicle

Inferred from electronic annotation. Source: Ensembl

lysosomal lumen

Traceable author statement. Source: Reactome

   Molecular_functionL-iduronidase activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 653626Alpha-L-iduronidase
PRO_0000012200

Regions

Region305 – 3062Substrate binding

Sites

Active site1821Proton donor Ref.5
Active site2991Nucleophile Ref.5
Binding site911Substrate
Binding site1811Substrate
Binding site2641Substrate
Binding site3491Substrate
Binding site3631Substrate

Amino acid modifications

Glycosylation1101N-linked (GlcNAc...) Ref.4 Ref.5 Ref.6
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Ref.5 Ref.6
Glycosylation4151N-linked (GlcNAc...) Ref.5 Ref.6
Glycosylation4511N-linked (GlcNAc...) Ref.6
Disulfide bond541 ↔ 577 Ref.5 Ref.6

Natural variations

Natural variant16 – 194Missing in MPS1H.
VAR_003349
Natural variant331H → Q. Ref.1 Ref.2 Ref.13 Ref.23
Corresponds to variant rs10794537 [ dbSNP | Ensembl ].
VAR_003350
Natural variant511G → D in MPS1H. Ref.12 Ref.23
VAR_003351
Natural variant751A → T in MPS1H. Ref.7 Ref.12
VAR_003352
Natural variant761Y → C in MPS1S. Ref.23
VAR_066215
Natural variant791A → V in MPS1H/S; reduction of activity and protein levels. Ref.22
VAR_020975
Natural variant821H → P in MPS1H/S. Ref.8
VAR_003353
Natural variant821H → Q Reduction of protein levels. Ref.22
Corresponds to variant rs148775298 [ dbSNP | Ensembl ].
VAR_020976
Natural variant841G → R in MPS1H/S. Ref.23
VAR_066216
Natural variant891R → Q in MPS1S; in Japanese 21% of alleles. Ref.9 Ref.21
VAR_003354
Natural variant891R → W in MPS1S. Ref.16 Ref.23
VAR_003355
Natural variant1031T → P in MPS1H; uncertain pathological role. Ref.23
VAR_066217
Natural variant1051R → Q. Ref.22 Ref.23
Corresponds to variant rs3755955 [ dbSNP | Ensembl ].
VAR_003356
Natural variant1161G → R.
Corresponds to variant rs148946496 [ dbSNP | Ensembl ].
VAR_003357
Natural variant1331M → I in MPS1H. Ref.21
VAR_020977
Natural variant1781E → K in MPS1H/S. Ref.23
VAR_066218
Natural variant1821E → K in MPS1H. Ref.21
VAR_020978
Natural variant1881F → L in MPS1H/S; associated with R-423. Ref.23
VAR_066219
Natural variant2081G → D in MPS1H. Ref.21
VAR_020979
Natural variant2181L → P in MPS1H. Ref.12
VAR_003358
Natural variant2191G → E in MPS1S. Ref.23
VAR_066220
Natural variant2381L → Q in MPS1H/S. Ref.22
VAR_020980
Natural variant2601S → F in MPS1H/S. Ref.21
VAR_020981
Natural variant2651G → R in MPS1H/S. Ref.23
VAR_066221
Natural variant2761E → K in MPS1H/S and MPS1S. Ref.23
VAR_066222
Natural variant2791V → A.
VAR_003359
Natural variant3001A → T in IDUA pseudodeficiency. Ref.17
VAR_017435
Natural variant3061W → L in MPS1S. Ref.23
VAR_066223
Natural variant3151D → Y in MPS1.
VAR_003360
Natural variant3271A → P in MPS1H and MPS1H/S. Ref.12 Ref.21 Ref.22 Ref.23
VAR_003361
Natural variant3461L → R in MPS1H/S; 0.4% of normal activity. Ref.20
VAR_017436
Natural variant3481N → K in MPS1S. Ref.23
VAR_066224
Natural variant349 – 3502Missing in MPS1H.
VAR_003363
Natural variant3491D → N in MPS1H.
VAR_003362
Natural variant3491D → Y in MPS1H. Ref.21
VAR_020982
Natural variant3501N → I in MPS1S. Ref.21
VAR_020983
Natural variant3611A → T. Ref.14 Ref.22 Ref.23
Corresponds to variant rs6831280 [ dbSNP | Ensembl ].
VAR_003364
Natural variant3631R → C in MPS1H/S; loss of activity. Ref.22
VAR_020984
Natural variant3661T → P in MPS1H. Ref.10
VAR_003365
Natural variant3801Q → R in MPS1H/S. Ref.21 Ref.22
VAR_003366
Natural variant3831R → H in MPS1S; 2-3% of normal activity. Ref.16 Ref.21
VAR_003367
Natural variant3851P → R in MPS1H. Ref.23
VAR_066225
Natural variant3881T → R in MPS1H. Ref.18
VAR_003368
Natural variant3961L → LALL in MPS1H.
VAR_003369
Natural variant3961L → P in MPS1. Ref.23
VAR_066226
Natural variant4091G → R in MPS1H. Ref.10
Corresponds to variant rs11934801 [ dbSNP | Ensembl ].
VAR_003370
Natural variant4231S → R in MPS1S and MPS1H/S; associated with L-188 in a patient with MPS1H/S; significant reduction of activity and protein levels. Ref.22 Ref.23
VAR_020985
Natural variant4361A → P in MPS1H/S. Ref.23
VAR_066227
Natural variant4451Missing in MPS1S. Ref.21
VAR_003371
Natural variant4491H → N. Ref.23
VAR_066228
Natural variant4541V → I. Ref.22 Ref.23
Corresponds to variant rs73066479 [ dbSNP | Ensembl ].
VAR_003372
Natural variant4891R → P in MPS1H. Ref.12
Corresponds to variant rs4690226 [ dbSNP | Ensembl ].
VAR_003373
Natural variant4901L → P in MPS1H/S and MPS1S. Ref.15 Ref.23
VAR_003374
Natural variant4921R → P in MPS1S. Ref.15 Ref.23
VAR_003375
Natural variant4961P → L in MPS1H/S. Ref.15
VAR_003376
Natural variant4961P → R in MPS1H/S. Ref.23
VAR_066229
Natural variant5041M → T in MPS1H/S. Ref.16
VAR_003377
Natural variant5331P → R in MPS1H and MPS1H/S; in 3% of the MPS1H patients; reduces catalytic activity and protein stability. Ref.5 Ref.11 Ref.21 Ref.22 Ref.23
VAR_003378
Natural variant5351L → F in MPS1H/S. Ref.23
VAR_066230
Natural variant5911A → T. Ref.23
VAR_066231
Natural variant6021F → I in MPS1H/S; reduction of activity and protein levels. Ref.22
VAR_020986
Natural variant6191R → G in MPS1H/S; 1.5% of normal activity. Ref.19
VAR_017437
Natural variant6261W → R in MPS1H/S. Ref.16
VAR_003379
Natural variant6281R → P in MPS1H/S. Ref.21
VAR_020987

Experimental info

Sequence conflict6221A → T in AAA51698. Ref.2

Secondary structure

..................................................................................................................... 653
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35475 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: 9D2399B22FD172BD

FASTA65372,670
        10         20         30         40         50         60 
MRPLRPRAAL LALLASLLAA PPVAPAEAPH LVHVDAARAL WPLRRFWRST GFCPPLPHSQ 

        70         80         90        100        110        120 
ADQYVLSWDQ QLNLAYVGAV PHRGIKQVRT HWLLELVTTR GSTGRGLSYN FTHLDGYLDL 

       130        140        150        160        170        180 
LRENQLLPGF ELMGSASGHF TDFEDKQQVF EWKDLVSSLA RRYIGRYGLA HVSKWNFETW 

       190        200        210        220        230        240 
NEPDHHDFDN VSMTMQGFLN YYDACSEGLR AASPALRLGG PGDSFHTPPR SPLSWGLLRH 

       250        260        270        280        290        300 
CHDGTNFFTG EAGVRLDYIS LHRKGARSSI SILEQEKVVA QQIRQLFPKF ADTPIYNDEA 

       310        320        330        340        350        360 
DPLVGWSLPQ PWRADVTYAA MVVKVIAQHQ NLLLANTTSA FPYALLSNDN AFLSYHPHPF 

       370        380        390        400        410        420 
AQRTLTARFQ VNNTRPPHVQ LLRKPVLTAM GLLALLDEEQ LWAEVSQAGT VLDSNHTVGV 

       430        440        450        460        470        480 
LASAHRPQGP ADAWRAAVLI YASDDTRAHP NRSVAVTLRL RGVPPGPGLV YVTRYLDNGL 

       490        500        510        520        530        540 
CSPDGEWRRL GRPVFPTAEQ FRRMRAAEDP VAAAPRPLPA GGRLTLRPAL RLPSLLLVHV 

       550        560        570        580        590        600 
CARPEKPPGQ VTRLRALPLT QGQLVLVWSD EHVGSKCLWT YEIQFSQDGK AYTPVSRKPS 

       610        620        630        640        650 
TFNLFVFSPD TGAVSGSYRV RALDYWARPG PFSDPVPYLE VPVPRGPPSP GNP 

« Hide

References

« Hide 'large scale' references
[1]"Human alpha-L-iduronidase: cDNA isolation and expression."
Scott H.S., Anson D.S., Orsborn A.M., Nelson P.V., Clements P.R., Morris C.P., Hopwood J.J.
Proc. Natl. Acad. Sci. U.S.A. 88:9695-9699(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-33.
Tissue: Liver.
[2]"Structure and sequence of the human alpha-L-iduronidase gene."
Scott H.S., Guo X.H., Hopwood J.J., Morris C.P.
Genomics 13:1311-1313(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-33.
[3]"Molecular genetics of mucopolysaccharidosis type I: diagnostic, clinical, and biological implications."
Scott H.S., Bunge S., Gal A., Clarke L.A., Morris C.P., Hopwood J.J.
Hum. Mutat. 6:288-302(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[4]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
Tissue: Liver.
[5]"Insights into mucopolysaccharidosis I from the structure and action of alpha-L-iduronidase."
Bie H., Yin J., He X., Kermode A.R., Goddard-Borger E.D., Withers S.G., James M.N.
Nat. Chem. Biol. 9:739-745(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 27-653 IN COMPLEX WITH IDURONATE ANALOGS, CATALYTIC ACTIVITY, ACTIVE SITE, CHARACTERIZATION OF VARIANT MPS1H ARG-533, DISULFIDE BOND, GLYCOSYLATION AT ASN-110; ASN-372 AND ASN-415.
[6]"Human alpha-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module."
Maita N., Tsukimura T., Taniguchi T., Saito S., Ohno K., Taniguchi H., Sakuraba H.
Proc. Natl. Acad. Sci. U.S.A. 110:14628-14633(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 27-653 IN COMPLEX WITH IDURONATE, CATALYTIC ACTIVITY, DISULFIDE BOND, SUBUNIT, GLYCOSYLATION AT ASN-110; ASN-372; ASN-415 AND ASN-451, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Mutation analysis of 19 North American mucopolysaccharidosis type I patients: identification of two additional frequent mutations."
Clarke L.A., Nelson P.V., Warrington C.L., Morris C.P., Hopwood J.J., Scott H.S.
Hum. Mutat. 3:275-282(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPS1H THR-75.
[8]"Two novel mutations causing mucopolysaccharidosis type I detected by single strand conformational analysis of the alpha-L-iduronidase gene."
Clark L.A., Scott H.S.
Hum. Mol. Genet. 2:1311-1312(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPS1H/S PRO-82.
[9]"Identification of mutations in the alpha-L-iduronidase gene (IDUA) that cause Hurler and Scheie syndromes."
Scott H.S., Litjens T., Nelson P.V., Thompson P.R., Brooks D.A., Hopwood J.J., Morris C.P.
Am. J. Hum. Genet. 53:973-986(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPS1S GLN-89.
[10]"Molecular analysis of Hurler syndrome in Druze and Muslim Arab patients in Israel: multiple allelic mutations of the IDUA gene in a small geographic area."
Bach G., Moskowitz S.M., Tieu P.T., Matynia A., Neufeld E.F.
Am. J. Hum. Genet. 53:330-338(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS1H PRO-366 AND ARG-409.
[11]"Alpha-L-iduronidase mutations (Q70X and P533R) associate with a severe Hurler phenotype."
Scott H.S., Litjens T., Nelson P.V., Brooks D.A., Hopwood J.J., Morris C.P.
Hum. Mutat. 1:333-339(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPS1H ARG-533.
[12]"Mucopolysaccharidosis type I: identification of 8 novel mutations and determination of the frequency of the two common alpha-L-iduronidase mutations (W402X and Q70X) among European patients."
Bunge S., Kleijer W.J., Steglich C., Beck M., Zuther C., Morris C.P., Schwinger E., Hopwood J.J., Scott H.S., Gal A.
Hum. Mol. Genet. 3:861-866(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS1H ASP-51; THR-75; PRO-218; PRO-327; PRO-489 AND 16-SER--ALA-19 DEL.
[13]"PCR detection of two RFLPs in exon I of the alpha-L-iduronidase (IDUA) gene."
Scott H.S., Litjens T., Hopwood J.J., Morris C.P.
Hum. Genet. 90:327-327(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLN-33.
[14]"Multiple polymorphisms within the alpha-L-iduronidase gene (IDUA): implications for a role in modification of MPS-I disease phenotype."
Scott H.S., Nelson P.V., Litjens T., Hopwood J.J., Morris C.P.
Hum. Mol. Genet. 2:1471-1473(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-361.
[15]"Four novel mutations underlying mild or intermediate forms of alpha-L-iduronidase deficiency (MPS IS and MPS IH/S)."
Tieu P.T., Bach G., Matynia A., Hwang M., Neufeld E.F.
Hum. Mutat. 6:55-59(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS1H/S PRO-490 AND LEU-496, VARIANT MPS1S PRO-492.
[16]"Mucopolysaccharidosis type I: identification of 13 novel mutations of the alpha-L-iduronidase gene."
Bunge S., Kleijer W.J., Steglich C., Beck M., Schwinger E., Gal A.
Hum. Mutat. 6:91-94(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS1S TRP-89 AND HIS-383, VARIANT MPS1H 349-ASP-ASN-350 DEL, VARIANTS MPS1H/S THR-504 AND ARG-626.
[17]"Molecular genetic defect underlying alpha-L-iduronidase pseudodeficiency."
Aronovich E.L., Pan D., Whitley C.B.
Am. J. Hum. Genet. 58:75-85(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT IDUA PSEUDODEFICIENCY THR-300.
[18]"A novel missense mutation in the human IDUA gene associated with a severe Hurler's phenotype."
Bartholomew D.W., McClellan J.M.
Hum. Mutat. 12:291-291(1998)
Cited for: VARIANT MPS1H ARG-388.
[19]"Mucopolysaccharidosis type I: characterization of novel mutations affecting alpha-L-iduronidase activity."
Lee-Chen G.J., Lin S.P., Tang Y.F., Chin Y.W.
Clin. Genet. 56:66-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPS1H/S GLY-619.
[20]"Identification and characterization of -3c-g acceptor splice site mutation in human alpha-L-iduronidase associated with mucopolysaccharidosis type IH/S."
Teng Y.N., Wang T.R., Hwu W.L., Lin S.P., Lee-Chen G.J.
Clin. Genet. 57:131-136(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MPS1H/S ARG-346.
[21]"Identification and characterization of 13 new mutations in mucopolysaccharidosis type I patients."
Matte U., Yogalingam G., Brooks D., Leistner S., Schwartz I., Lima L., Norato D.Y., Brum J.M., Beesley C., Winchester B., Giugliani R., Hopwood J.J.
Mol. Genet. Metab. 78:37-43(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS1H ILE-133; LYS-182; ASP-208; TYR-349 AND ARG-533, VARIANTS MPS1H/S PHE-260; PRO-327; ARG-380 AND PRO-628, VARIANTS MPS1S GLN-89; ILE-350; HIS-383 AND ASP-445 DEL.
[22]"Identification and molecular characterization of alpha-L-iduronidase mutations present in mucopolysaccharidosis type I patients undergoing enzyme replacement therapy."
Yogalingam G., Guo X.H., Muller V.J., Brooks D.A., Clements P.R., Kakkis E.D., Hopwood J.J.
Hum. Mutat. 24:199-207(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS1H/S VAL-79; GLN-238; PRO-327; CYS-363; ARG-380; ARG-533 AND ILE-602, VARIANT MPS1S ARG-423, VARIANTS GLN-82; GLN-105; THR-361 AND ILE-454, CHARACTERIZATION OF VARIANTS MPS1H/S VAL-79; GLN-238; CYS-363 AND ILE-602, CHARACTERIZATION OF VARIANT MPS1S ARG-423, CHARACTERIZATION OF VARIANT GLN-82.
[23]"IDUA mutational profiling of a cohort of 102 European patients with mucopolysaccharidosis type I: identification and characterization of 35 novel alpha-L-iduronidase (IDUA) alleles."
Bertola F., Filocamo M., Casati G., Mort M., Rosano C., Tylki-Szymanska A., Tuysuz B., Gabrielli O., Grossi S., Scarpa M., Parenti G., Antuzzi D., Dalmau J., Di Rocco M., Vici C.D., Okur I., Rosell J., Rovelli A. expand/collapse author list , Furlan F., Rigoldi M., Biondi A., Cooper D.N., Parini R.
Hum. Mutat. 32:E2189-E2210(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MPS1H/S ARG-84; LYS-178; LEU-188; ARG-265; LYS-276; ARG-423; PRO-436; ARG-496; ARG-533 AND PHE-535, VARIANTS MPS1H ASP-51; PRO-103; PRO-327 AND ARG-385, VARIANTS MPS1S CYS-76; TRP-89; GLU-219; LYS-276; LEU-306; LYS-348; PRO-490 AND PRO-492, VARIANT MPS1 PRO-396, VARIANTS GLN-33; GLN-105; THR-361; ASN-449; ILE-454 AND THR-591.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74715 mRNA. Translation: AAA81589.1.
M95740, M95739 Genomic DNA. Translation: AAA51698.1.
PIRS53645.
RefSeqNP_000194.2. NM_000203.4.
UniGeneHs.89560.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y24model-A36-522[»]
3W81X-ray2.30A27-653[»]
3W82X-ray2.76A27-653[»]
4KGJX-ray2.99A27-653[»]
4KGLX-ray2.70A27-653[»]
4KH2X-ray2.36A27-653[»]
4MJ2X-ray2.10A/B27-653[»]
4MJ4X-ray2.17A27-653[»]
ProteinModelPortalP35475.
SMRP35475. Positions 27-642.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP35475. 1 interaction.
MINTMINT-1397491.
STRING9606.ENSP00000247933.

Chemistry

DrugBankDB00090. Laronidase.

Protein family/group databases

CAZyGH39. Glycoside Hydrolase Family 39.

Polymorphism databases

DMDM92090608.

Proteomic databases

PaxDbP35475.
PRIDEP35475.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247933; ENSP00000247933; ENSG00000127415.
GeneID3425.
KEGGhsa:3425.
UCSCuc003gby.3. human.

Organism-specific databases

CTD3425.
GeneCardsGC04P000970.
H-InvDBHIX0200643.
HGNCHGNC:5391. IDUA.
HPACAB025901.
MIM252800. gene.
607014. phenotype.
607015. phenotype.
607016. phenotype.
neXtProtNX_P35475.
Orphanet93473. Hurler syndrome.
93476. Hurler-Scheie syndrome.
93474. Scheie syndrome.
PharmGKBPA29638.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3664.
HOGENOMHOG000007042.
HOVERGENHBG006121.
InParanoidP35475.
KOK01217.
OrthoDBEOG70088F.
PhylomeDBP35475.
TreeFamTF323228.

Enzyme and pathway databases

BioCycMetaCyc:HS05096-MONOMER.
BRENDA3.2.1.76. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKP35475.

Gene expression databases

ArrayExpressP35475.
BgeeP35475.
CleanExHS_IDUA.
GenevestigatorP35475.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000514. Glyco_hydro_39.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01229. Glyco_hydro_39. 1 hit.
[Graphical view]
PRINTSPR00745. GLHYDRLASE39.
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS01027. GLYCOSYL_HYDROL_F39. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi3425.
NextBio13508.
PROP35475.
SOURCESearch...

Entry information

Entry nameIDUA_HUMAN
AccessionPrimary (citable) accession number: P35475
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 4, 2006
Last modified: April 16, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries