IDUA_MOUSE
ID IDUA_MOUSE Reviewed; 634 AA.
AC P48441; E9QM17;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Alpha-L-iduronidase;
DE EC=3.2.1.76;
DE Flags: Precursor;
GN Name=Idua;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=7698753; DOI=10.1006/geno.1994.1621;
RA Clarke L.A.;
RT "Murine alpha-L-iduronidase: cDNA isolation and expression.";
RL Genomics 24:311-316(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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:7698753};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7698753}.
CC -!- PTM: N-glycosylation contributes to substrate binding and is required
CC for full enzymatic activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 39 family. {ECO:0000305}.
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DR EMBL; L34111; AAC42044.1; -; mRNA.
DR EMBL; AC161813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A55683; A55683.
DR AlphaFoldDB; P48441; -.
DR SMR; P48441; -.
DR STRING; 10090.ENSMUSP00000071577; -.
DR CAZy; GH39; Glycoside Hydrolase Family 39.
DR GlyConnect; 2122; 5 N-Linked glycans (2 sites).
DR GlyGen; P48441; 2 sites, 5 N-linked glycans (2 sites).
DR PhosphoSitePlus; P48441; -.
DR MaxQB; P48441; -.
DR PaxDb; P48441; -.
DR PeptideAtlas; P48441; -.
DR PRIDE; P48441; -.
DR ProteomicsDB; 267254; -.
DR MGI; MGI:96418; Idua.
DR eggNOG; ENOG502QRES; Eukaryota.
DR InParanoid; P48441; -.
DR Reactome; R-MMU-2024096; HS-GAG degradation.
DR Reactome; R-MMU-2024101; CS/DS degradation.
DR ChiTaRS; Idua; mouse.
DR PRO; PR:P48441; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P48441; protein.
DR GO; GO:0030135; C:coated vesicle; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0003940; F:L-iduronidase activity; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1990079; P:cartilage homeostasis; IMP:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0048878; P:chemical homeostasis; IMP:MGI.
DR GO; GO:0030209; P:dermatan sulfate catabolic process; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0006027; P:glycosaminoglycan catabolic process; IDA:MGI.
DR GO; GO:0030211; P:heparin catabolic process; IDA:MGI.
DR GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0061037; P:negative regulation of cartilage development; IMP:MGI.
DR GO; GO:0090341; P:negative regulation of secretion of lysosomal enzymes; IDA:MGI.
DR GO; GO:0045780; P:positive regulation of bone resorption; IMP:MGI.
DR GO; GO:0120158; P:positive regulation of collagen catabolic process; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR Gene3D; 2.60.40.10; -; 1.
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; SSF51445; SSF51445; 1.
DR PROSITE; PS01027; GLYCOSYL_HYDROL_F39; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycosidase; Hydrolase; Lysosome; Reference proteome;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..634
FT /note="Alpha-L-iduronidase"
FT /id="PRO_0000012201"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10068"
FT ACT_SITE 289
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 295..296
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 531..567
FT /evidence="ECO:0000250"
FT CONFLICT 359
FT /note="F -> S (in Ref. 1; AAC42044)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="A -> G (in Ref. 1; AAC42044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 71254 MW; 41A8F5B036B360DB CRC64;
MLTFFAAFLA APLALAESPY LVRVDAARPL RPLLPFWRST GFCPPLPHDQ ADQYDLSWDQ
QLNLAYIGAV PHSGIEQVRI HWLLDLITAR KSPGQGLMYN FTHLDAFLDL LMENQLLPGF
ELMGSPSGYF TDFDDKQQVF EWKDLVSLLA RRYIGRYGLT HVSKWNFETW NEPDHHDFDN
VSMTTQGFLN YYDACSEGLR IASPTLKLGG PGDSFHPLPR SPMCWSLLGH CANGTNFFTG
EVGVRLDYIS LHKKGAGSSI AILEQEMAVV EQVQQLFPEF KDTPIYNDEA DPLVGWSLPQ
PWRADVTYAA LVVKVIAQHQ NLLFANSSSS MRYVLLSNDN AFLSYHPYPF SQRTLTARFQ
VNNTHPPHVQ LLRKPVLTVM GLMALLDGEQ LWAEVSKAGA VLDSNHTVGV LASTHHPEGS
AAAWSTTVLI YTSDDTHAHP NHSIPVTLRL RGVPPGLDLV YIVLYLDNQL SSPYSAWQHM
GQPVFPSAEQ FRRMRMVEDP VAEAPRPFPA RGRLTLHRKL PVPSLLLVHV CTRPLKPPGQ
VSRLRALPLT HGQLILVWSD ERVGSKCLWT YEIQFSQKGE EYAPINRRPS TFNLFVFSPD
TAVVSGSYRV RALDYWARPG PFSDPVTYLD VPAS
