P48441 · IDUA_MOUSE
- ProteinAlpha-L-iduronidase
- GeneIdua
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids634 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
Catalytic activity
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 44 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 46 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 48 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 81 | alpha-L-iduronate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 171 | alpha-L-iduronate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 172 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 172 | alpha-L-iduronate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 254 | alpha-L-iduronate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 289 | Nucleophile | ||||
Sequence: E | ||||||
Binding site | 289 | alpha-L-iduronate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 295 | alpha-L-iduronate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 296 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 339 | alpha-L-iduronate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 353 | alpha-L-iduronate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-L-iduronidase
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP48441
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MLTFFAAFLAAPLALA | ||||||
Chain | PRO_0000012201 | 17-634 | Alpha-L-iduronidase | |||
Sequence: ESPYLVRVDAARPLRPLLPFWRSTGFCPPLPHDQADQYDLSWDQQLNLAYIGAVPHSGIEQVRIHWLLDLITARKSPGQGLMYNFTHLDAFLDLLMENQLLPGFELMGSPSGYFTDFDDKQQVFEWKDLVSLLARRYIGRYGLTHVSKWNFETWNEPDHHDFDNVSMTTQGFLNYYDACSEGLRIASPTLKLGGPGDSFHPLPRSPMCWSLLGHCANGTNFFTGEVGVRLDYISLHKKGAGSSIAILEQEMAVVEQVQQLFPEFKDTPIYNDEADPLVGWSLPQPWRADVTYAALVVKVIAQHQNLLFANSSSSMRYVLLSNDNAFLSYHPYPFSQRTLTARFQVNNTHPPHVQLLRKPVLTVMGLMALLDGEQLWAEVSKAGAVLDSNHTVGVLASTHHPEGSAAAWSTTVLIYTSDDTHAHPNHSIPVTLRLRGVPPGLDLVYIVLYLDNQLSSPYSAWQHMGQPVFPSAEQFRRMRMVEDPVAEAPRPFPARGRLTLHRKLPVPSLLLVHVCTRPLKPPGQVSRLRALPLTHGQLILVWSDERVGSKCLWTYEIQFSQKGEEYAPINRRPSTFNLFVFSPDTAVVSGSYRVRALDYWARPGPFSDPVTYLDVPAS | ||||||
Glycosylation | 100 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 180 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 233 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 326 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 362 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 405 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 441 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 531↔567 | |||||
Sequence: CTRPLKPPGQVSRLRALPLTHGQLILVWSDERVGSKC |
Post-translational modification
N-glycosylation contributes to substrate binding and is required for full enzymatic activity.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length634
- Mass (Da)71,254
- Last updated2011-07-27 v2
- Checksum41A8F5B036B360DB
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 359 | in Ref. 1; AAC42044 | ||||
Sequence: F → S | ||||||
Sequence conflict | 423 | in Ref. 1; AAC42044 | ||||
Sequence: A → G |
Keywords
- Technical term