Q6PTV2 · ASP1_TOXGO

  • Protein
    Aspartic protease 1
  • Gene
    ASP1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

162050100150200250300350400450500550600
TypeIDPosition(s)Description
Active site293
Active site476

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentfood vacuole
Cellular Componentmembrane
Molecular Functionaspartic-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartic protease 1
  • EC number
  • Short names
    TgASP1
  • Alternative names
    • Toxomepsin 1

Gene names

    • Name
      ASP1

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • RH
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Conoidasida > Coccidia > Eucoccidiorida > Eimeriorina > Sarcocystidae > Toxoplasma

Accessions

  • Primary accession
    Q6PTV2

Organism-specific databases

Subcellular Location

Membrane
; Single-pass type II membrane protein
Vacuole
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).

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-110Cytoplasmic
Transmembrane111-131Helical; Signal-anchor for type II membrane protein
Topological domain132-620Lumenal

Keywords

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).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis27-31In tachyzoites, abnormal accumulation in the Golgi apparatus.

PTM/Processing

Features

Showing features for propeptide, chain, disulfide bond.

TypeIDPosition(s)Description
PropeptidePRO_00004568271-258
ChainPRO_0000456828259-620Aspartic protease 1
Disulfide bond513↔550

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).

Keywords

Expression

Developmental stage

Expressed in tachyzoites (at protein level) (PubMed:17547703, PubMed:21616070, PubMed:32051238).
Expressed in bradyzoites at higher levels (at protein level) (PubMed:32051238).

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region27-31Important for proper cellular trafficking
Region138-174Disordered
Compositional bias152-166Polar residues
Domain275-616Peptidase A1

Sequence similarities

Belongs to the peptidase A1 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    620
  • Mass (Da)
    67,137
  • Last updated
    2004-07-05 v1
  • Checksum
    CAACF31294C426FD
MSPSSRFRNLVSVDSSSQDFGKRSSLYASLLDSASVSSLPGICSTAEDRDVEDESWKDPSSSSHCAKTEGGACAFPRLNQVLSSLRDPMGVFSRAKRRRSLGKAVGLSTSVICVVALFGIVCLCLYGLVNFSFTSVETSPLDDPRNSPVMGELGNPQASTPSSARADTPARHDRQNQMFSPWSVQNEQFLGEDSDALPHAGPLFRSGVMVMPLRKMKSLRRIGWDKNTITVPDLQAHLVAALRMQEGLSKKDDGNLSGLSDGDDISIHDYMNSQYYTEIYVGSPGQKVRVVVDTGSSDLWVCSASCGILLNILHKTYNHGKSDTYHADGTPYHVQYASGPVGGFLSADDVALASLKTKNFLLAEAVDLKGLGTAFFFGKFDGILGMGFPSLATKGLKPFMQAAVEQNVVKNWVFVFYLASANGVDGELAIGGVDQERFIGDINFSPVVDFRYWMINTKGLKSDGDLIAPTTKMIIDSGTSLIVGPLDEVKRIATMMGAFSVPLMPEGMFFISCEKAKVLRDLQLEIEGQDYPIKIKDLLISASAAAGTPCLFGMMGLKALEGGRPTPQKNGFGIFPPSQLVASAKGPIGRTWILGDLFMRNVYTVFDYDNKQIGFARLKN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias152-166Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY580011
EMBL· GenBank· DDBJ
AAS90335.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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