Q64560 · TPP2_RAT

  • Protein
    Tripeptidyl-peptidase 2
  • Gene
    Tpp2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Cytosolic tripeptidyl-peptidase that releases N-terminal tripeptides from polypeptides and is a component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. It plays an important role in intracellular amino acid homeostasis (By similarity).
Stimulates adipogenesis (By similarity).

Miscellaneous

The limitation of proteolytic products to tripeptides is achieved by tailoring the size of the substrate-binding cleft: the two negatively charged residues Glu-305 and Glu-331 that are blocking position P4 limit the number of residues that can be accommodated in the binding cleft and thus create a molecular ruler. At the same time, they orient substrates so that the tripeptides are removed exclusively from the N-terminus (By similarity).

Catalytic activity

  • Release of an N-terminal tripeptide from a polypeptide.
    EC:3.4.14.10 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

112491002003004005006007008009001,0001,1001,200
TypeIDPosition(s)Description
Active site44Charge relay system
Active site264Charge relay system
Active site449Charge relay system

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentnucleus
Molecular Functionaminopeptidase activity
Molecular Functionidentical protein binding
Molecular Functionpeptide binding
Molecular Functionserine-type endopeptidase activity
Molecular Functiontripeptidyl-peptidase activity
Biological Processintracellular amino acid homeostasis
Biological Processprotein catabolic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Tripeptidyl-peptidase 2
  • EC number
  • Short names
    TPP-2
  • Alternative names
    • Tripeptidyl aminopeptidase
    • Tripeptidyl-peptidase II (TPP-II)

Gene names

    • Name
      Tpp2

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q64560

Proteomes

Organism-specific databases

Subcellular Location

Note: Translocates to the nucleus in response to gamma-irradiation.

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00000764242-1249Tripeptidyl-peptidase 2
Modified residue401N6-acetyllysine
Modified residue915Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Chemistry

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain9-508Peptidase S8
Region998-1018Disordered
Compositional bias1001-1018Basic and acidic residues

Sequence similarities

Belongs to the peptidase S8 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,249
  • Mass (Da)
    138,293
  • Last updated
    2007-01-23 v3
  • Checksum
    F4A41664028AAB2B
MATAATEEPFPFHGLLPKKETGASSFLCRYPEYDGRGVLIAVLDTGVDPGAPGMQVTTDGKPKIIDIIDTTGSGDVNTATEVEPKDGEITGLSGRVLKIPANWTNPSGKYHIGIKNGYDFYPKALKERIQKERKEKIWDPIHRVALAEACRKQEEFDIANNGSSQANKLIKEELQSQVELLNSFEKKYSDPGPVYDCLVWHDGETWRACVDSNENGDLGKSTVLRNYKEAQEYGSFGTAEMLNYSVNIYDDGNLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSYGEATHWPNSGRICEVINEAVWKHNTIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMVAEYSLREKLPANQYTWSSRGPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALVLSGLKANNVDYTVHSVRRALENTAIKADNIEVFAQGHGIIQVDKAYDYLIQNTSFANRLGFTVTVGNNRGIYLRDPVQVAAPSDHGVGIEPVFPENTENSEKISFQLHLALTSNSSWVQCPSHLELMNQCRHINIRVDPRGLREGLHYTEVCGYDIASPNAGPLFRVPITAVIAAKVNESSHYDLAFTDVHFKPGQIRRHFVEVPEGATWAEVTVCSCSSEVSAKFVLHAVQLVKQRAYRSHEFYKFCSLPEKGTLIEAFPVLGGKAIEFCIARWWASLSDVNIDYTISFHGIVCTAPQLNIHASEGINRFDVQSSLKYEDLAPCITLKSWVQTLRPVNAKTRPLGSRDVLPNNRQLYEMVLTYSFHQPKSGEVTPSCPLLCELLYESEFDSQLWIIFDQNKRQMGSGDAYPHQYSLKLEKGDYTIRLQIRHEQISDLDRLKDLPFIVSHRLSNTLSLDIHENHSLALLGKKKSSSLTLPPKYNQPFFVTSLPDDKIPKGAGPGCYLAGSLTLSKTELGKKADVIPVHYYLIPPPTKTKNGSKDKEKDSEKEKDLKEEFTEALRDLKIQWMTKLDSTDIYNELKETYPAYLPLYVARLHQLDAEKERMKRLNEIVDAANAVISHIDQTALAVYIAMKTDPRPDAATIKNDMDKQKSTLVDALCRKGCALADHLLHAQPHDGAAAGDAEAKEEEGESTLESLSETYWETTKWTDLFDTKVLTFAYKHALVNKMYGRGLKFATKLVEEKPTKENWKNCIQLMKLLGWTHCASFTENWLPIMYPPDYCVF

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8L2Q8D6A0A8L2Q8D6_RATTpp21307
A0A8L2R8U1A0A8L2R8U1_RATTpp21294
A0A8L2R9L9A0A8L2R9L9_RATTpp21263

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1001-1018Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U50194
EMBL· GenBank· DDBJ
AAA93458.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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