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Q01634 (IDUA_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-L-iduronidase

EC=3.2.1.76
Gene names
Name:IDUA
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length655 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.1

Subunit structure

Monomer By similarity.

Subcellular location

Lysosome By similarity.

Tissue specificity

Detected in testis (at protein level). Expressed ubiquitously. Ref.1

Post-translational modification

A smaller 63 kDa protein probably arises from IDUA protein by proteolytic cleavage.

N-glycosylation contributes to substrate binding and is required for full enzymatic activity By similarity.

Involvement in disease

Defects in IDUA are the cause of mucopolysaccharidosis type I (MPS I). Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 39 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

dermatan sulfate catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-iduronidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Chain26 – 655630Alpha-L-iduronidase
PRO_0000012199

Regions

Region304 – 3052Substrate binding By similarity

Sites

Active site1811Proton donor By similarity
Active site2981Nucleophile By similarity
Binding site901Substrate By similarity
Binding site1801Substrate By similarity
Binding site2631Substrate By similarity
Binding site3481Substrate By similarity
Binding site3621Substrate By similarity

Amino acid modifications

Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1891N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Disulfide bond540 ↔ 576 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q01634 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 294A56333FE7BBC9

FASTA65572,939
        10         20         30         40         50         60 
MRPPGPRAPG LALLAALLAA PRALAEAPHL VLVDAARALR PLRPFWRSTG FCPPLPHSQA 

        70         80         90        100        110        120 
DRYDLSWDQQ LNLAYVGAVP HGGIEQVRTH WLLELITARE SAGQGLSYNF THLDGYLDLL 

       130        140        150        160        170        180 
RENQLLPGFE LMGSPSQRFT DFEDKRQVLA WKELVSLLAR RYIGRYGLSY VSKWNFETWN 

       190        200        210        220        230        240 
EPDHHDFDNV TMTLQGFLNY YDACSEGLRA ASPALRFGGP GDSFHPWPRS PLCWGLLEHC 

       250        260        270        280        290        300 
HNGTNFFTGE LGVRLDYISL HKKGAGSSIY ILEQEQATVQ QIRRLFPKFA DTPVYNDEAD 

       310        320        330        340        350        360 
PLVGWALPQP WRADVTYAAM VVKVVAQHQN PPRANGSAAL RPALLSNDNA FLSFHPHPFT 

       370        380        390        400        410        420 
QRTLTARFQV NDTEPPHVQL LRKPVLTAMA LLALLDGRQL WAEVSRGGTV LDSNHTVGVL 

       430        440        450        460        470        480 
ASAHLPAGPR DAWRATVLLY ASDDTRAHAA RAVPVTLRLL GVPRGPGLVY VTLALDNPRC 

       490        500        510        520        530        540 
SPHGEWQRLG RPVFPTAEEF RRMRAAEDPV AEAPRPFPAS GRLTLSVELR LPSLLLLHVC 

       550        560        570        580        590        600 
ARPEKPPGPV TRLRALPLTR GQVLLVWSDE RVGSKCLWTY EIQFSADGEV YTPISRKPST 

       610        620        630        640        650 
FNLFVFSPES AVTSGSYRVR AVDYWARPGP FSTRVHYVEV PAPSGPPRPS DCERC 

« Hide

References

[1]"Cloning and characterization of cDNA encoding canine alpha-L-iduronidase. mRNA deficiency in mucopolysaccharidosis I dog."
Stoltzfus L.J., Sosa-Pineda B., Moskowitz S.M., Menon K.P., Dlott B., Hooper L., Teplow D.B., Shull R.M., Neufeld E.F.
J. Biol. Chem. 267:6570-6575(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
Tissue: Testis.
[2]"Architecture of the canine IDUA gene and mutation underlying canine mucopolysaccharidosis I."
Menon K.P., Tieu P.T., Neufeld E.F.
Genomics 14:763-768(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ROLE IN DISEASE.
Tissue: Fibroblast and Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L01058 Genomic DNA. No translation available.
L01059 Genomic DNA. No translation available.
L01060 Genomic DNA. No translation available.
L01061 Genomic DNA. No translation available.
L01065 Genomic DNA. Translation: AAA51456.1.
M81893 mRNA. Translation: AAA51455.1.
PIRA42420.

3D structure databases

ProteinModelPortalQ01634.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000024558.

Protein family/group databases

CAZyGH39. Glycoside Hydrolase Family 39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG74108.
HOVERGENHBG006121.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR003961. Fibronectin_type3.
IPR000514. Glyco_hydro_39.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01229. Glyco_hydro_39. 1 hit.
[Graphical view]
PRINTSPR00745. GLHYDRLASE39.
SUPFAMSSF49265. SSF49265. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS01027. GLYCOSYL_HYDROL_F39. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIDUA_CANFA
AccessionPrimary (citable) accession number: Q01634
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: December 11, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries