Q64560 · TPP2_RAT
- ProteinTripeptidyl-peptidase 2
- GeneTpp2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1249 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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).
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
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 44 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 264 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 449 | Charge relay system | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | aminopeptidase activity | |
Molecular Function | identical protein binding | |
Molecular Function | peptide binding | |
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | tripeptidyl-peptidase activity | |
Biological Process | intracellular amino acid homeostasis | |
Biological Process | protein catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTripeptidyl-peptidase 2
- EC number
- Short namesTPP-2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ64560
Proteomes
Organism-specific databases
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000076424 | 2-1249 | Tripeptidyl-peptidase 2 | |||
Sequence: ATAATEEPFPFHGLLPKKETGASSFLCRYPEYDGRGVLIAVLDTGVDPGAPGMQVTTDGKPKIIDIIDTTGSGDVNTATEVEPKDGEITGLSGRVLKIPANWTNPSGKYHIGIKNGYDFYPKALKERIQKERKEKIWDPIHRVALAEACRKQEEFDIANNGSSQANKLIKEELQSQVELLNSFEKKYSDPGPVYDCLVWHDGETWRACVDSNENGDLGKSTVLRNYKEAQEYGSFGTAEMLNYSVNIYDDGNLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSYGEATHWPNSGRICEVINEAVWKHNTIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMVAEYSLREKLPANQYTWSSRGPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALVLSGLKANNVDYTVHSVRRALENTAIKADNIEVFAQGHGIIQVDKAYDYLIQNTSFANRLGFTVTVGNNRGIYLRDPVQVAAPSDHGVGIEPVFPENTENSEKISFQLHLALTSNSSWVQCPSHLELMNQCRHINIRVDPRGLREGLHYTEVCGYDIASPNAGPLFRVPITAVIAAKVNESSHYDLAFTDVHFKPGQIRRHFVEVPEGATWAEVTVCSCSSEVSAKFVLHAVQLVKQRAYRSHEFYKFCSLPEKGTLIEAFPVLGGKAIEFCIARWWASLSDVNIDYTISFHGIVCTAPQLNIHASEGINRFDVQSSLKYEDLAPCITLKSWVQTLRPVNAKTRPLGSRDVLPNNRQLYEMVLTYSFHQPKSGEVTPSCPLLCELLYESEFDSQLWIIFDQNKRQMGSGDAYPHQYSLKLEKGDYTIRLQIRHEQISDLDRLKDLPFIVSHRLSNTLSLDIHENHSLALLGKKKSSSLTLPPKYNQPFFVTSLPDDKIPKGAGPGCYLAGSLTLSKTELGKKADVIPVHYYLIPPPTKTKNGSKDKEKDSEKEKDLKEEFTEALRDLKIQWMTKLDSTDIYNELKETYPAYLPLYVARLHQLDAEKERMKRLNEIVDAANAVISHIDQTALAVYIAMKTDPRPDAATIKNDMDKQKSTLVDALCRKGCALADHLLHAQPHDGAAAGDAEAKEEEGESTLESLSETYWETTKWTDLFDTKVLTFAYKHALVNKMYGRGLKFATKLVEEKPTKENWKNCIQLMKLLGWTHCASFTENWLPIMYPPDYCVF | ||||||
Modified residue | 401 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 915 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-508 | Peptidase S8 | ||||
Sequence: PFPFHGLLPKKETGASSFLCRYPEYDGRGVLIAVLDTGVDPGAPGMQVTTDGKPKIIDIIDTTGSGDVNTATEVEPKDGEITGLSGRVLKIPANWTNPSGKYHIGIKNGYDFYPKALKERIQKERKEKIWDPIHRVALAEACRKQEEFDIANNGSSQANKLIKEELQSQVELLNSFEKKYSDPGPVYDCLVWHDGETWRACVDSNENGDLGKSTVLRNYKEAQEYGSFGTAEMLNYSVNIYDDGNLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSYGEATHWPNSGRICEVINEAVWKHNTIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMVAEYSLREKLPANQYTWSSRGPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALVLSGLKANNVDYTVHSVRRALENTAIKADNIEVFAQGHGIIQVDKAY | ||||||
Region | 998-1018 | Disordered | ||||
Sequence: TKTKNGSKDKEKDSEKEKDLK | ||||||
Compositional bias | 1001-1018 | Basic and acidic residues | ||||
Sequence: KNGSKDKEKDSEKEKDLK |
Sequence similarities
Belongs to the peptidase S8 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,249
- Mass (Da)138,293
- Last updated2007-01-23 v3
- ChecksumF4A41664028AAB2B
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2Q8D6 | A0A8L2Q8D6_RAT | Tpp2 | 1307 | ||
A0A8L2R8U1 | A0A8L2R8U1_RAT | Tpp2 | 1294 | ||
A0A8L2R9L9 | A0A8L2R9L9_RAT | Tpp2 | 1263 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1001-1018 | Basic and acidic residues | ||||
Sequence: KNGSKDKEKDSEKEKDLK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U50194 EMBL· GenBank· DDBJ | AAA93458.1 EMBL· GenBank· DDBJ | mRNA |