IDUA_CANLF
ID IDUA_CANLF Reviewed; 655 AA.
AC Q01634;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Alpha-L-iduronidase;
DE EC=3.2.1.76;
DE Flags: Precursor;
GN Name=IDUA;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE,
RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=1551868; DOI=10.1016/s0021-9258(19)50465-3;
RA Stoltzfus L.J., Sosa-Pineda B., Moskowitz S.M., Menon K.P., Dlott B.,
RA Hooper L., Teplow D.B., Shull R.M., Neufeld E.F.;
RT "Cloning and characterization of cDNA encoding canine alpha-L-iduronidase.
RT mRNA deficiency in mucopolysaccharidosis I dog.";
RL J. Biol. Chem. 267:6570-6575(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ROLE IN DISEASE.
RC TISSUE=Fibroblast, and Testis;
RX PubMed=1339393; DOI=10.1016/s0888-7543(05)80182-x;
RA Menon K.P., Tieu P.T., Neufeld E.F.;
RT "Architecture of the canine IDUA gene and mutation underlying canine
RT mucopolysaccharidosis I.";
RL Genomics 14:763-768(1992).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of unsulfated alpha-L-iduronosidic linkages in
CC dermatan sulfate.; EC=3.2.1.76;
CC Evidence={ECO:0000269|PubMed:1551868};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in testis (at protein level). Expressed
CC ubiquitously. {ECO:0000269|PubMed:1551868}.
CC -!- PTM: A smaller 63 kDa protein probably arises from IDUA protein by
CC proteolytic cleavage.
CC -!- PTM: N-glycosylation contributes to substrate binding and is required
CC for full enzymatic activity. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in IDUA are the cause of mucopolysaccharidosis
CC type I (MPS I).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 39 family. {ECO:0000305}.
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DR EMBL; L01058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L01059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L01060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L01061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L01065; AAA51456.1; -; Genomic_DNA.
DR EMBL; M81893; AAA51455.1; -; mRNA.
DR PIR; A42420; A42420.
DR AlphaFoldDB; Q01634; -.
DR SMR; Q01634; -.
DR STRING; 9612.ENSCAFP00000024558; -.
DR CAZy; GH39; Glycoside Hydrolase Family 39.
DR PaxDb; Q01634; -.
DR Ensembl; ENSCAFT00040006532; ENSCAFP00040005648; ENSCAFG00040003433.
DR eggNOG; ENOG502QRES; Eukaryota.
DR InParanoid; Q01634; -.
DR Reactome; R-CFA-2024096; HS-GAG degradation.
DR Reactome; R-CFA-2024101; CS/DS degradation.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0003940; F:L-iduronidase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030209; P:dermatan sulfate catabolic process; ISS:UniProtKB.
DR GO; GO:0030211; P:heparin catabolic process; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR000514; Glyco_hydro_39.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF01229; Glyco_hydro_39; 1.
DR PRINTS; PR00745; GLHYDRLASE39.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01027; GLYCOSYL_HYDROL_F39; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..25
FT CHAIN 26..655
FT /note="Alpha-L-iduronidase"
FT /id="PRO_0000012199"
FT ACT_SITE 181
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10068"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 304..305
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 540..576
FT /evidence="ECO:0000250"
SQ SEQUENCE 655 AA; 72939 MW; 294A56333FE7BBC9 CRC64;
MRPPGPRAPG LALLAALLAA PRALAEAPHL VLVDAARALR PLRPFWRSTG FCPPLPHSQA
DRYDLSWDQQ LNLAYVGAVP HGGIEQVRTH WLLELITARE SAGQGLSYNF THLDGYLDLL
RENQLLPGFE LMGSPSQRFT DFEDKRQVLA WKELVSLLAR RYIGRYGLSY VSKWNFETWN
EPDHHDFDNV TMTLQGFLNY YDACSEGLRA ASPALRFGGP GDSFHPWPRS PLCWGLLEHC
HNGTNFFTGE LGVRLDYISL HKKGAGSSIY ILEQEQATVQ QIRRLFPKFA DTPVYNDEAD
PLVGWALPQP WRADVTYAAM VVKVVAQHQN PPRANGSAAL RPALLSNDNA FLSFHPHPFT
QRTLTARFQV NDTEPPHVQL LRKPVLTAMA LLALLDGRQL WAEVSRGGTV LDSNHTVGVL
ASAHLPAGPR DAWRATVLLY ASDDTRAHAA RAVPVTLRLL GVPRGPGLVY VTLALDNPRC
SPHGEWQRLG RPVFPTAEEF RRMRAAEDPV AEAPRPFPAS GRLTLSVELR LPSLLLLHVC
ARPEKPPGPV TRLRALPLTR GQVLLVWSDE RVGSKCLWTY EIQFSADGEV YTPISRKPST
FNLFVFSPES AVTSGSYRVR AVDYWARPGP FSTRVHYVEV PAPSGPPRPS DCERC
