O02467 · ASPG_SPOFR
- ProteinN(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids320 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.
Catalytic activity
- H2O + N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = H+ + L-aspartate + N-acetyl-beta-D-glucosaminylamine
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 184 | Nucleophile | ||||
Sequence: T | ||||||
Binding site | 212-215 | substrate | ||||
Sequence: RVGD | ||||||
Binding site | 235-238 | substrate | ||||
Sequence: TGNG |
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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Aspect | Term | |
---|---|---|
Cellular Component | lysosome | |
Molecular Function | asparaginase activity | |
Molecular Function | beta-aspartyl-peptidase activity | |
Molecular Function | N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameN(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase
- EC number
- Alternative names
- Cleaved into 2 chains
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Lepidoptera > Glossata > Ditrysia > Noctuoidea > Noctuidae > Amphipyrinae > Spodoptera
Accessions
- Primary accessionO02467
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000002345 | 1-183 | Glycosylasparaginase alpha chain | |||
Sequence: EKNMPIVITTWSFTNASQKAWEVLKDEGKALDAVEQGGIVCENEQCDRTVGYGGSPDEDGETTLDAFIMDGSTMNVGAVAALRRIKSAISVARHVMEYTTHSFLAGELATKFAVEMGFKEESLSTDESRELWSKWRFEKQCQPNFRKNVKPDPRKHCGPYHKKRNFVDYIHPEVFVVDQYNHD | ||||||
Glycosylation | 15 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 41↔46 | |||||
Sequence: CENEQC | ||||||
Disulfide bond | 141↔157 | |||||
Sequence: CQPNFRKNVKPDPRKHC | ||||||
Chain | PRO_0000002346 | 184-320 | Glycosylasparaginase beta chain | |||
Sequence: TIGMVAVDSKGDVAAGTSTNGAKFKIPGRVGDSPIPGAGAYADNTVGGAAATGNGDTMMRFLPSFLAVEEMRRGASPANAAKTAIKRISAHHPDFMGAVIALSKNGQYGAACNGIETFPFVVQDKTRKTFEVVTIKC | ||||||
Disulfide bond | 295↔320 | |||||
Sequence: CNGIETFPFVVQDKTRKTFEVVTIKC |
Post-translational modification
Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (Probable).
Keywords
- PTM
Interaction
Subunit
Heterotetramer of two alpha and two beta chains or heterodimer of an alpha and a beta chain.
Structure
Sequence
- Sequence statusFragment
- Length320
- Mass (Da)34,841
- Last updated1997-07-01 v1
- ChecksumD0C57ACA6F2A6183
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: E |