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Protein

Tripeptidyl-peptidase 2

Gene

Tpp2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity).By similarity

Catalytic activityi

Release of an N-terminal tripeptide from a polypeptide.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441Charge relay systemBy similarity
Active sitei264 – 2641Charge relay systemBy similarity
Active sitei449 – 4491Charge relay systemBy similarity

GO - Molecular functioni

  • aminopeptidase activity Source: UniProtKB-KW
  • peptide binding Source: RGD
  • serine-type endopeptidase activity Source: InterPro
  • tripeptidyl-peptidase activity Source: RGD

GO - Biological processi

  • proteolysis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

ReactomeiR-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiS08.A56.

Names & Taxonomyi

Protein namesi
Recommended name:
Tripeptidyl-peptidase 2 (EC:3.4.14.10)
Short name:
TPP-2
Alternative name(s):
Tripeptidyl aminopeptidase
Tripeptidyl-peptidase II
Short name:
TPP-II
Gene namesi
Name:Tpp2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi621584. Tpp2.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Translocates to the nucleus in responce to gamma-irradiation.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4675.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 12491248Tripeptidyl-peptidase 2PRO_0000076424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei401 – 4011N6-acetyllysineBy similarity
Modified residuei915 – 9151PhosphoserineBy similarity
Cross-linki1005 – 1005Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki1013 – 1013Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ64560.
PRIDEiQ64560.

PTM databases

iPTMnetiQ64560.

Expressioni

Gene expression databases

GenevisibleiQ64560. RN.

Interactioni

Protein-protein interaction databases

BioGridi249673. 1 interaction.
IntActiQ64560. 1 interaction.
STRINGi10116.ENSRNOP00000015393.

Chemistry

BindingDBiQ64560.

Structurei

3D structure databases

ProteinModelPortaliQ64560.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 509470Peptidase S8Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family.Curated
Contains 1 peptidase S8 domain.Curated

Phylogenomic databases

eggNOGiKOG1114. Eukaryota.
COG1404. LUCA.
GeneTreeiENSGT00390000014623.
HOGENOMiHOG000008178.
HOVERGENiHBG017992.
InParanoidiQ64560.
KOiK01280.
OMAiHANWSNS.
OrthoDBiEOG786H2B.

Family and domain databases

Gene3Di3.40.50.200. 2 hits.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR022229. Peptidase_S8A_TPPII.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 2 hits.
PfamiPF00082. Peptidase_S8. 1 hit.
PF12580. TPPII. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 2 hits.
PROSITEiPS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64560-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATAATEEPF PFHGLLPKKE TGASSFLCRY PEYDGRGVLI AVLDTGVDPG
60 70 80 90 100
APGMQVTTDG KPKIIDIIDT TGSGDVNTAT EVEPKDGEIT GLSGRVLKIP
110 120 130 140 150
ANWTNPSGKY HIGIKNGYDF YPKALKERIQ KERKEKIWDP IHRVALAEAC
160 170 180 190 200
RKQEEFDIAN NGSSQANKLI KEELQSQVEL LNSFEKKYSD PGPVYDCLVW
210 220 230 240 250
HDGETWRACV DSNENGDLGK STVLRNYKEA QEYGSFGTAE MLNYSVNIYD
260 270 280 290 300
DGNLLSIVTS GGAHGTHVAS IAAGHFPEEP ERNGVAPGAQ ILSIKIGDTR
310 320 330 340 350
LSTMETGTGL IRAMIEVINH KCDLVNYSYG EATHWPNSGR ICEVINEAVW
360 370 380 390 400
KHNTIYVSSA GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMVAEYSLRE
410 420 430 440 450
KLPANQYTWS SRGPSADGAL GVSISAPGGA IASVPNWTLR GTQLMNGTSM
460 470 480 490 500
SSPNACGGIA LVLSGLKANN VDYTVHSVRR ALENTAIKAD NIEVFAQGHG
510 520 530 540 550
IIQVDKAYDY LIQNTSFANR LGFTVTVGNN RGIYLRDPVQ VAAPSDHGVG
560 570 580 590 600
IEPVFPENTE NSEKISFQLH LALTSNSSWV QCPSHLELMN QCRHINIRVD
610 620 630 640 650
PRGLREGLHY TEVCGYDIAS PNAGPLFRVP ITAVIAAKVN ESSHYDLAFT
660 670 680 690 700
DVHFKPGQIR RHFVEVPEGA TWAEVTVCSC SSEVSAKFVL HAVQLVKQRA
710 720 730 740 750
YRSHEFYKFC SLPEKGTLIE AFPVLGGKAI EFCIARWWAS LSDVNIDYTI
760 770 780 790 800
SFHGIVCTAP QLNIHASEGI NRFDVQSSLK YEDLAPCITL KSWVQTLRPV
810 820 830 840 850
NAKTRPLGSR DVLPNNRQLY EMVLTYSFHQ PKSGEVTPSC PLLCELLYES
860 870 880 890 900
EFDSQLWIIF DQNKRQMGSG DAYPHQYSLK LEKGDYTIRL QIRHEQISDL
910 920 930 940 950
DRLKDLPFIV SHRLSNTLSL DIHENHSLAL LGKKKSSSLT LPPKYNQPFF
960 970 980 990 1000
VTSLPDDKIP KGAGPGCYLA GSLTLSKTEL GKKADVIPVH YYLIPPPTKT
1010 1020 1030 1040 1050
KNGSKDKEKD SEKEKDLKEE FTEALRDLKI QWMTKLDSTD IYNELKETYP
1060 1070 1080 1090 1100
AYLPLYVARL HQLDAEKERM KRLNEIVDAA NAVISHIDQT ALAVYIAMKT
1110 1120 1130 1140 1150
DPRPDAATIK NDMDKQKSTL VDALCRKGCA LADHLLHAQP HDGAAAGDAE
1160 1170 1180 1190 1200
AKEEEGESTL ESLSETYWET TKWTDLFDTK VLTFAYKHAL VNKMYGRGLK
1210 1220 1230 1240
FATKLVEEKP TKENWKNCIQ LMKLLGWTHC ASFTENWLPI MYPPDYCVF
Length:1,249
Mass (Da):138,293
Last modified:January 23, 2007 - v3
Checksum:iF4A41664028AAB2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50194 mRNA. Translation: AAA93458.1.
PIRiS68431.
RefSeqiNP_112399.1. NM_031137.1.
UniGeneiRn.28991.

Genome annotation databases

EnsembliENSRNOT00000015393; ENSRNOP00000015393; ENSRNOG00000011194.
ENSRNOT00000078220; ENSRNOP00000074045; ENSRNOG00000011194.
ENSRNOT00000085267; ENSRNOP00000074556; ENSRNOG00000011194.
GeneIDi81815.
KEGGirno:81815.
UCSCiRGD:621584. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50194 mRNA. Translation: AAA93458.1.
PIRiS68431.
RefSeqiNP_112399.1. NM_031137.1.
UniGeneiRn.28991.

3D structure databases

ProteinModelPortaliQ64560.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249673. 1 interaction.
IntActiQ64560. 1 interaction.
STRINGi10116.ENSRNOP00000015393.

Chemistry

BindingDBiQ64560.
ChEMBLiCHEMBL4675.

Protein family/group databases

MEROPSiS08.A56.

PTM databases

iPTMnetiQ64560.

Proteomic databases

PaxDbiQ64560.
PRIDEiQ64560.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015393; ENSRNOP00000015393; ENSRNOG00000011194.
ENSRNOT00000078220; ENSRNOP00000074045; ENSRNOG00000011194.
ENSRNOT00000085267; ENSRNOP00000074556; ENSRNOG00000011194.
GeneIDi81815.
KEGGirno:81815.
UCSCiRGD:621584. rat.

Organism-specific databases

CTDi7174.
RGDi621584. Tpp2.

Phylogenomic databases

eggNOGiKOG1114. Eukaryota.
COG1404. LUCA.
GeneTreeiENSGT00390000014623.
HOGENOMiHOG000008178.
HOVERGENiHBG017992.
InParanoidiQ64560.
KOiK01280.
OMAiHANWSNS.
OrthoDBiEOG786H2B.

Enzyme and pathway databases

ReactomeiR-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ64560.

Gene expression databases

GenevisibleiQ64560. RN.

Family and domain databases

Gene3Di3.40.50.200. 2 hits.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR022229. Peptidase_S8A_TPPII.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 2 hits.
PfamiPF00082. Peptidase_S8. 1 hit.
PF12580. TPPII. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 2 hits.
PROSITEiPS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization and inhibition of a cholecystokinin-inactivating serine peptidase."
    Rose C., Vargas F., Facchinetti P., Bourgeat P., Bambal R.B., Bishop P.B., Chan S.M., Moore A.N., Ganellin C.R., Schwartz J.C.
    Nature 380:403-409(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.

Entry informationi

Entry nameiTPP2_RAT
AccessioniPrimary (citable) accession number: Q64560
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.