Q6PTV2 · ASP1_TOXGO
- ProteinAspartic protease 1
- GeneASP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids620 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Aspartyl protease which is dispensable for protein degradation in the vacuolar compartment (VAC) or for tachyzoite and bradyzoite viability.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 293 | |||||
Sequence: D | ||||||
Active site | 476 | |||||
Sequence: D |
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 | food vacuole | |
Cellular Component | membrane | |
Molecular Function | aspartic-type endopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAspartic protease 1
- EC number
- Short namesTgASP1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Conoidasida > Coccidia > Eucoccidiorida > Eimeriorina > Sarcocystidae > Toxoplasma
Accessions
- Primary accessionQ6PTV2
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type II membrane protein
Note: In non-dividing tachyzoites, localizes to punctate structures in the apical end of the parasite which correspond to a lysosome-like organelle known as the vacuolar compartment (VAC) (PubMed:17547703, PubMed:32051238).
Does not localizes to secretory organelles, including micronemes, rhoptries and dense granules (PubMed:17547703).
In dividing tachyzoites, transiently localizes to the nascent inner membrane complex (IMC) of daughter cells (PubMed:17547703).
Does not localizes to secretory organelles, including micronemes, rhoptries and dense granules (PubMed:17547703).
In dividing tachyzoites, transiently localizes to the nascent inner membrane complex (IMC) of daughter cells (PubMed:17547703).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-110 | Cytoplasmic | ||||
Sequence: MSPSSRFRNLVSVDSSSQDFGKRSSLYASLLDSASVSSLPGICSTAEDRDVEDESWKDPSSSSHCAKTEGGACAFPRLNQVLSSLRDPMGVFSRAKRRRSLGKAVGLSTS | ||||||
Transmembrane | 111-131 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: VICVVALFGIVCLCLYGLVNF | ||||||
Topological domain | 132-620 | Lumenal | ||||
Sequence: SFTSVETSPLDDPRNSPVMGELGNPQASTPSSARADTPARHDRQNQMFSPWSVQNEQFLGEDSDALPHAGPLFRSGVMVMPLRKMKSLRRIGWDKNTITVPDLQAHLVAALRMQEGLSKKDDGNLSGLSDGDDISIHDYMNSQYYTEIYVGSPGQKVRVVVDTGSSDLWVCSASCGILLNILHKTYNHGKSDTYHADGTPYHVQYASGPVGGFLSADDVALASLKTKNFLLAEAVDLKGLGTAFFFGKFDGILGMGFPSLATKGLKPFMQAAVEQNVVKNWVFVFYLASANGVDGELAIGGVDQERFIGDINFSPVVDFRYWMINTKGLKSDGDLIAPTTKMIIDSGTSLIVGPLDEVKRIATMMGAFSVPLMPEGMFFISCEKAKVLRDLQLEIEGQDYPIKIKDLLISASAAAGTPCLFGMMGLKALEGGRPTPQKNGFGIFPPSQLVASAKGPIGRTWILGDLFMRNVYTVFDYDNKQIGFARLKN |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No defect in tachyzoite replication (PubMed:21616070, PubMed:32051238).
Food ingestion and turnover of autophagosomes are normal (PubMed:32051238).
Normal tachyzoites conversion into bradyzoites (PubMed:32051238).
No defect in secretory organelles and inner membrane complex (IMC) biogenesis (PubMed:21616070).
No defect in virulence in a BALB/c mouse infection model (PubMed:21616070).
Food ingestion and turnover of autophagosomes are normal (PubMed:32051238).
Normal tachyzoites conversion into bradyzoites (PubMed:32051238).
No defect in secretory organelles and inner membrane complex (IMC) biogenesis (PubMed:21616070).
No defect in virulence in a BALB/c mouse infection model (PubMed:21616070).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 27-31 | In tachyzoites, abnormal accumulation in the Golgi apparatus. | ||||
Sequence: YASLL → AASAA |
PTM/Processing
Features
Showing features for propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000456827 | 1-258 | ||||
Sequence: MSPSSRFRNLVSVDSSSQDFGKRSSLYASLLDSASVSSLPGICSTAEDRDVEDESWKDPSSSSHCAKTEGGACAFPRLNQVLSSLRDPMGVFSRAKRRRSLGKAVGLSTSVICVVALFGIVCLCLYGLVNFSFTSVETSPLDDPRNSPVMGELGNPQASTPSSARADTPARHDRQNQMFSPWSVQNEQFLGEDSDALPHAGPLFRSGVMVMPLRKMKSLRRIGWDKNTITVPDLQAHLVAALRMQEGLSKKDDGNLSG | ||||||
Chain | PRO_0000456828 | 259-620 | Aspartic protease 1 | |||
Sequence: LSDGDDISIHDYMNSQYYTEIYVGSPGQKVRVVVDTGSSDLWVCSASCGILLNILHKTYNHGKSDTYHADGTPYHVQYASGPVGGFLSADDVALASLKTKNFLLAEAVDLKGLGTAFFFGKFDGILGMGFPSLATKGLKPFMQAAVEQNVVKNWVFVFYLASANGVDGELAIGGVDQERFIGDINFSPVVDFRYWMINTKGLKSDGDLIAPTTKMIIDSGTSLIVGPLDEVKRIATMMGAFSVPLMPEGMFFISCEKAKVLRDLQLEIEGQDYPIKIKDLLISASAAAGTPCLFGMMGLKALEGGRPTPQKNGFGIFPPSQLVASAKGPIGRTWILGDLFMRNVYTVFDYDNKQIGFARLKN | ||||||
Disulfide bond | 513↔550 | |||||
Sequence: CEKAKVLRDLQLEIEGQDYPIKIKDLLISASAAAGTPC |
Post-translational modification
Proteolytically cleaved into the soluble active mature form by, at least, cysteine protease CPL (PubMed:17547703, PubMed:32051238).
Undergoes at least four processing steps; the first cleavage removes the propeptide resulting in the production of a soluble 45 kDa protein, which is further processed into a 35 kDa form followed by an additional processing into the final active 30 kDa form (PubMed:17547703, PubMed:32051238).
Undergoes at least four processing steps; the first cleavage removes the propeptide resulting in the production of a soluble 45 kDa protein, which is further processed into a 35 kDa form followed by an additional processing into the final active 30 kDa form (PubMed:17547703, PubMed:32051238).
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 27-31 | Important for proper cellular trafficking | ||||
Sequence: YASLL | ||||||
Region | 138-174 | Disordered | ||||
Sequence: TSPLDDPRNSPVMGELGNPQASTPSSARADTPARHDR | ||||||
Compositional bias | 152-166 | Polar residues | ||||
Sequence: ELGNPQASTPSSARA | ||||||
Domain | 275-616 | Peptidase A1 | ||||
Sequence: YYTEIYVGSPGQKVRVVVDTGSSDLWVCSASCGILLNILHKTYNHGKSDTYHADGTPYHVQYASGPVGGFLSADDVALASLKTKNFLLAEAVDLKGLGTAFFFGKFDGILGMGFPSLATKGLKPFMQAAVEQNVVKNWVFVFYLASANGVDGELAIGGVDQERFIGDINFSPVVDFRYWMINTKGLKSDGDLIAPTTKMIIDSGTSLIVGPLDEVKRIATMMGAFSVPLMPEGMFFISCEKAKVLRDLQLEIEGQDYPIKIKDLLISASAAAGTPCLFGMMGLKALEGGRPTPQKNGFGIFPPSQLVASAKGPIGRTWILGDLFMRNVYTVFDYDNKQIGFA |
Sequence similarities
Belongs to the peptidase A1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length620
- Mass (Da)67,137
- Last updated2004-07-05 v1
- ChecksumCAACF31294C426FD
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 152-166 | Polar residues | ||||
Sequence: ELGNPQASTPSSARA |