Q9R0T7 · TRY4_MOUSE

  • Protein
    Trypsin-4
  • Gene
    Try4
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Serine protease capable of autoactivation.

Catalytic activity

  • Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
    EC:3.4.21.4 (UniProtKB | ENZYME | Rhea)

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per subunit.

Activity regulation

Activated by autocatalytic cleavage (PubMed:23814066).
Cleavage by CTRC inhibits autoactivation (PubMed:23814066).

Features

Showing features for active site, binding site, site.

124620406080100120140160180200220240
TypeIDPosition(s)Description
Active site63Charge relay system
Binding site75Ca2+ (UniProtKB | ChEBI)
Binding site77Ca2+ (UniProtKB | ChEBI)
Binding site80Ca2+ (UniProtKB | ChEBI)
Site81-82Cleavage; by CTRC
Binding site82Ca2+ (UniProtKB | ChEBI)
Binding site85Ca2+ (UniProtKB | ChEBI)
Active site107Charge relay system
Site122-123Cleavage; by autolysis
Site150-151Cleavage; by CTRC
Site193-194Cleavage; by autolysis
Active site200Charge relay system

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 Componentcollagen-containing extracellular matrix
Cellular Componentextracellular space
Molecular Functionmetal ion binding
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Trypsin-4
  • EC number

Gene names

    • Name
      Try4
    • Synonyms
      T8
      , Td

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 129/SvJ
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9R0T7

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis122Slightly increases autoactivation.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, propeptide, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-15
PropeptidePRO_000045771916-23Activation peptide
ChainPRO_501509994424-246Trypsin-4
Disulfide bond48↔64
Disulfide bond139↔206
Disulfide bond171↔185
Disulfide bond196↔220

Post-translational modification

Proteolytically cleaved and activated by an autocatalytic mechanism (PubMed:23814066).
Cleavage by CTRC inhibits autoactivation (PubMed:23814066).

Keywords

Proteomic databases

Expression

Tissue specificity

Expressed in the pancreas, lung and kidney.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain24-244Peptidase S1

Sequence similarities

Belongs to the peptidase S1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    246
  • Mass (Da)
    26,274
  • Last updated
    2000-05-01 v1
  • Checksum
    B6A9F4C99079633F
MRALLFLALVGAAVAFPVDDDDKIVGGYTCRENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEGNEQFVNSAKIIKHPNFNSRTLNNDIMLIKLASPVTLNARVATVALPSSCAPAGTQCLISGWGNTLSFGVNNPDLLQCLDAPLLPQADCEASYPGKITNNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCALKDNPGVYTKVCNYVDWIQNTIAAN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB017032
EMBL· GenBank· DDBJ
BAA74761.1
EMBL· GenBank· DDBJ
Genomic DNA
AE000664
EMBL· GenBank· DDBJ
AAB69056.1
EMBL· GenBank· DDBJ
Genomic DNA
AK003064
EMBL· GenBank· DDBJ
BAB22542.1
EMBL· GenBank· DDBJ
mRNA
AK008667
EMBL· GenBank· DDBJ
BAB25821.1
EMBL· GenBank· DDBJ
mRNA
BC061135
EMBL· GenBank· DDBJ
AAH61135.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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