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(pGlu)LYENKPRRRPYIL + H2O
(pGlu)L + YENKPRRRPYIL
-
i.e. neurotensin, 15.0% degradation after 16 h
-
?
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
Ala-Ala-Phe-7-amido-4-carbamoylmethylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
Ala-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ala-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Ala-Ala-Pro-4-nitroanilide + H2O
Ala-Ala-Pro + 4-nitroaniline
-
-
-
-
?
Ala-Arg-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ala-Arg-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Ala-Asp-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ala-Asp-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Ala-His-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ala-His-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Ala-Nle-Leu-7-amido-4-carbamoylmethylcoumarin + H2O
Ala-Nle-Leu + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Ala-Nle-Nle-7-amido-4-carbamoylmethylcoumarin + H2O
Ala-Nle-Nle + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Ala-Nva-Nle-7-amido-4-carbamoylmethylcoumarin + H2O
Ala-Nva-Nle + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Ala-Phe-Pro-4-nitroanilide + H2O
Ala-Phe-Pro + 4-nitroaniline
-
-
-
-
?
Ala-Pro-Gly-Asp-Arg-Ile-Tyr-Val-His-Pro-Phe + H2O
Ala-Pro-Gly + Asp-Arg-Ile + Tyr-Val-His-Pro-Phe
SedB
-
-
?
Ala-Ser-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ala-Ser-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
amyloid-beta + H2O
?
AbetaCy3 peptides are released from the nanofibrils due to TPP1 activity
-
-
?
amyloid-beta1-42 + H2O
?
the 34 Abeta end of the substrate shows integrated peak areas for peptide fragments 21-34, 22-34, and 23-34, indicative of cleavage after residue L34. The most abundant cleavages occur after residues Y10, G33, L34, and A30, and these cleavages occur more rapidly at pH 3.0 than at pH 4.5, consistent with endopeptidase activity. Peptides ending at residues E11, L17, F20, G37, and G38, are detected with lower abundances. At later times, the abundance of some of the peptides may decrease due to further proteolysis by TPP1. TPP1 can proteolyze monomeric Abeta1-42 efficiently at acidic pH
-
-
?
angiotensin II + H2O
? + Asp-Arg-Val
-
-
-
-
?
Arg-Ala-Phe-7-amido-4-methylcoumarin + H2O
Arg-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Arg-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Arg-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Arg-Pro-Phe-7-amido-4-carbamoylmethylcoumarin + H2O
Arg-Pro-Phe + 7-amino-4-carbamoylmethylcoumarin
-
-
-
-
?
Asp-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Asp-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
Cholecystokinin + H2O
?
-
-
-
-
?
DRVYIHPF + H2O
DRV + YIHPF
DRVYIHPFHL + H2O
DRV + YIHPFHL
-
i.e. angiotensin I, 11.3% degradation after 16 h
-
?
epsilon-aminocaproyl-WFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] + H2O
epsilon-aminocaproyl-WF + FIQ-[N-(2,4-dinitrophenyl)-ethylenediamine]
-
-
-
?
GKPIPFFRLK + H2O
GKPIP + FFRLK
-
endo-type substrate, 24.5% degradation after 16 h
-
?
Gly-L-Pro-L-Met-2-anthraquinonyl hydrazide + H2O
Gly-L-Pro-L-Met + 2-anthraquinonyl hydrazine
-
-
-
-
?
Gly-L-Pro-L-Met-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O
?
Gly-L-Pro-L-Met-L-anthraquinonyl hydrazide + H2O
?
-
-
-
?
Gly-Lys-Pro-Ile-Pro-Phe-Phe-Arg-Leu-Lys + H2O
Gly-Lys-Pro-Ile-Pro-Phe + Phe-Arg-Leu-Lys
-
-
-
-
?
Gly-Pro-Ala 4-nitroanilide + H2O
Gly-Pro-Ala + 4-nitroaniline
-
at 20% the rate of Gly-Pro-Met 4-nitroanilide hydrolysis
-
-
?
Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
at 10% the rate of Gly-Pro-Met 4-methylcoumarin 7-amide hydrolysis
-
-
?
Gly-Pro-Leu 2-naphthylamide + H2O
Gly-Pro-Leu + 2-naphthylamine
Gly-Pro-Met 2-naphthylamide + H2O
Gly-Pro-Met + 2-naphthylamine
Gly-Pro-Met 4-nitroanilide + H2O
Gly-Pro-Met + 4-nitroaniline
-
-
-
-
?
Gly-Pro-Met-7-amido-4-methylcoumarin + H2O
Gly-Pro-Met + 7-amino-4-methylcoumarin
-
-
-
-
?
GNLWATGHFM-NH2 + H2O
GNL + WATGHFM-NH2
-
i.e. neuromedin B, complete degradation after 16 h
-
?
His-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
His-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
KWFFIQ-EDDnp + H2O
KWF + FIQ-EDDnp
KWFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] + H2O
KWF + FIQ-[N-(2,4-dinitrophenyl)-ethylenediamine]
-
-
-
?
L-Ala-L-Ala-L-Phe-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
L-Arg-L-Nle-L-Nle-7-amido-4-methylcoumarin + H2O
L-Arg-L-Nle-L-Nle + 7-amino-4-methylcoumarin
-
-
-
?
L-Asp-L-Ala-L-Phe-4-nitroanilide + H2O
L-Asp-L-Ala-L-Phe + 4-nitroaniline
-
-
-
?
Neuromedin B + H2O
?
-
-
-
-
?
Phe-Pro-Ala 2-naphthylamide + H2O
Phe-Pro-Ala + 2-naphthylamine
-
synthetic peptide modeled after NH2-terminal tripeptide sequence of the phenylalanyl monomer of bovine or rat growth hormone, fluorogenic substrate
-
?
Phe-Pro-Ala-4-nitroanilide + H2O
Phe-Pro-Ala + 4-nitroaniline
phenylalanyl monomer of bovine growth hormone + H2O
?
-
cleaves 11 tripeptides sequentially from the NH2-terminus
-
-
?
poly(Gly-Pro-Ala) + H2O
Gly-Pro-Ala
-
-
-
?
RVYIHPF + H2O
RVY + IHPF
-
i.e. angiotensin III, 95.0% degradation after 15 min
-
?
RWFFIQ-EDDnp + H2O
RWF + FIQ-EDDnp
RWFFIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] + H2O
RWF + FIQ-[N-(2,4-dinitrophenyl)-ethylenediamine]
FRET substrate
-
-
?
RWFVIQ-EDDnp + H2O
RWF + VIQ-EDDnp
RWFVIQ-[N-(2,4-dinitrophenyl)-ethylenediamine] + H2O
RWF + VIQ-[N-(2,4-dinitrophenyl)-ethylenediamine]
-
-
-
?
Ser-Ala-Phe-p-nitrophenylalanyl-Arg-Leu + H2O
Ser-Ala-Phe + p-nitrophenylalanyl-Arg-Leu
-
-
-
-
?
subunit C of mitochondrial ATP synthase + H2O
?
-
-
-
-
?
synthetic collagen-like polypetides + H2O
Gly-Pro-Xaa tripeptides
-
-
-
?
Val-Pro-Arg 4-nitroanilide + H2O
Val-Pro-Arg + 4-nitroaniline
-
at 11% the rate of Gly-Pro-Met 4-nitroanilide hydrolysis
-
-
?
YGGFLRKYP + H2O
YGG + FLRKYP
-
i.e. beta-neo-endorphin, 28% degradation after 16 h
-
?
[Ala-Ala-Phe]2-rhodamine 110 + H2O
[Ala-Ala-Phe]2 + rhodamine 110
-
specific substrate for determining TPP-I activity and intracellular localization in living cells
-
-
?
[Arg-Nle-Nle]2-rhodamine 110 + H2O
[Ala-Ala-Phe]2 + rhodamine 110
-
specific substrate for determining TPP-I activity and intracellular localization in living cells
-
-
?
glucagon + H2O
additional information
-
Ala-Ala-Ala-4-nitroanilide + H2O

Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Ala-4-nitroanilide + H2O
Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O

Ala-Ala-Phe + 4-nitroaniline
SedB
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
SedC
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
SedD
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Phe-4-nitroanilide + H2O
Ala-Ala-Phe + 4-nitroaniline
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O

Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
33.8% degradation within 60 min
-
-
?
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
-
-
?
DRVYIHPF + H2O

DRV + YIHPF
-
-
-
?
DRVYIHPF + H2O
DRV + YIHPF
-
i.e. angiotensin II, 18.2% degradation after 16 h
-
?
Gly-L-Pro-L-Met-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O

?
-
-
-
-
?
Gly-L-Pro-L-Met-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O
?
-
-
-
-
?
Gly-Pro-Leu 2-naphthylamide + H2O

Gly-Pro-Leu + 2-naphthylamine
-
25% of the activity with Gly-Pro-Met 2-naphthylamide, Ala-Ala-Phe-4-nitroanilide or Ala-Ala-Phe-7-amido-4-methylcoumarin
-
-
?
Gly-Pro-Leu 2-naphthylamide + H2O
Gly-Pro-Leu + 2-naphthylamine
-
at 30% the rate of Gly-Pro-Met 2-naphthylamide hydrolysis
-
-
?
Gly-Pro-Met 2-naphthylamide + H2O

Gly-Pro-Met + 2-naphthylamine
-
-
-
?
Gly-Pro-Met 2-naphthylamide + H2O
Gly-Pro-Met + 2-naphthylamine
-
-
-
-
?
Gly-Pro-Met 2-naphthylamide + H2O
Gly-Pro-Met + 2-naphthylamine
-
-
-
-
?
KWFFIQ-EDDnp + H2O

KWF + FIQ-EDDnp
rat spleen and kidney homogenates cleave only at F-F bond
-
-
?
KWFFIQ-EDDnp + H2O
KWF + FIQ-EDDnp
rat spleen and kidney homogenates cleave only at F-F bond
-
-
?
L-Ala-L-Ala-L-Phe-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O

?
-
-
-
-
?
L-Ala-L-Ala-L-Phe-4-hydrazino-N-hexyl-1,8-naphthalimide + H2O
?
-
-
-
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O

L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-L-Ala-L-Phe-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala-L-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
Phe-Pro-Ala-4-nitroanilide + H2O

Phe-Pro-Ala + 4-nitroaniline
SedB
-
-
?
Phe-Pro-Ala-4-nitroanilide + H2O
Phe-Pro-Ala + 4-nitroaniline
SedC
-
-
?
Phe-Pro-Ala-4-nitroanilide + H2O
Phe-Pro-Ala + 4-nitroaniline
SedD
-
-
?
RWFFIQ-EDDnp + H2O

RWF + FIQ-EDDnp
best substrate, rat spleen and kidney homogenates cleave only at F-F bond
-
-
?
RWFFIQ-EDDnp + H2O
RWF + FIQ-EDDnp
best substrate, rat spleen and kidney homogenates cleave only at F-F bond
-
-
?
RWFVIQ-EDDnp + H2O

RWF + VIQ-EDDnp
rat spleen and kidney homogenates cleave only at F-V bond
-
-
?
RWFVIQ-EDDnp + H2O
RWF + VIQ-EDDnp
rat spleen and kidney homogenates cleave only at F-V bond
-
-
?
glucagon + H2O

additional information
-
-
-
all nine tripeptides and the C-terminal pentapeptide are identified
?
additional information
?
-
-
no substrates are Ala-Phe-Pro-beta-naphthylamide (modeled after NH2-terminal tripeptide sequence of the alanyl monomer of bovine growth hormone), alanyl monomer of bovine growth hormone
-
-
?
additional information
?
-
-
no significant aminopeptidase activity
-
-
?
additional information
?
-
TPP1F is binding partner of Dictyostelium discoideum intracellular transmembrane protein GPHR, i.e. Golgi pH regulator. A region encompassing the DUF3735 (GPHR_N) domain of GPHR is responsible for the interaction. In TPP1F, the binding site is located in the prodomain of the protein. GPHR is present in subcellular membranous compartments reaching from endoplasmic reticulum membranes to membranes of the endo-lysosomal system
-
-
?
additional information
?
-
-
TPP1F is binding partner of Dictyostelium discoideum intracellular transmembrane protein GPHR, i.e. Golgi pH regulator. A region encompassing the DUF3735 (GPHR_N) domain of GPHR is responsible for the interaction. In TPP1F, the binding site is located in the prodomain of the protein. GPHR is present in subcellular membranous compartments reaching from endoplasmic reticulum membranes to membranes of the endo-lysosomal system
-
-
?
additional information
?
-
-
succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin, succinyl-Gly-Pro-Leu 4-methylcoumarin 7-amide, Gly-Pro-7-amido-4-methylcoumarin, Gly-7-amido-4-methylcoumarin, Pro-7-amido-4-methylcoumarin, Met-7-amido-4-methylcoumarin, Ala 7-amido-4-methylcoumarin, Phe-7-amido-4-methylcoumarin, or Leu-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
the enzyme removes tripeptides from the free N-termini of small polypeptides and also shows a minor endoprotease activity
-
-
?
additional information
?
-
-
absolute requirement for unsubstituted amino-terminus
-
-
?
additional information
?
-
-
involved in degradation of bone collagen
-
-
?
additional information
?
-
-
classical late infantile neuronal ceroid lipofuscinosis is an autosomal recessive disease caused by mutations in the CLN2 gene resulting in functional defects of the gene product tripeptidyl-peptidase I. This disease is associated with a progressive neurodegenerative course beginning at the age of two years with developmental stagnation, finally leading to a complete loss of motor function, vision and speech by the age of 10 years
-
-
?
additional information
?
-
-
elevated enzyme activity of tripeptidyl peptidase I and other lysosomal enzymes in Sjoegren's syndrome patients may play a role in tissue damage by accelerated breakdown of glycoproteins in lysosomes
-
-
?
additional information
?
-
-
TPP I is the predominant proteolytic enzyme responsible for the intracellular degradation of neuromedin B. The inability of cells from patients with late-infantile neuronal ceroid lipofuscinosis (CNL2) to degrade neuromedin B and other neuropeptides may contribute to the pathogenesis of the disease
-
-
?
additional information
?
-
-
determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates
-
-
?
additional information
?
-
-
prefers Leu, Phe and Nle at the P1 position, whereas Asn, His, Lys, Arg, Ser, Val, Ile, Thr, Gly and Pro are highly unfavored in this position, showing less than 1% of the activity of the best substrates
-
-
?
additional information
?
-
-
TPP I acts preferentially on small, unstructured oligopeptides of less than 5 kDa
-
-
?
additional information
?
-
validation and evaluation of a rapid and simple fluorometric tripeptidyl peptidase 1 (TPP1) assay using dried blood specimens to diagnose CLN2 disease
-
-
?
additional information
?
-
-
validation and evaluation of a rapid and simple fluorometric tripeptidyl peptidase 1 (TPP1) assay using dried blood specimens to diagnose CLN2 disease
-
-
?
additional information
?
-
-
dipeptidyl-peptidase I cannot functionally compensate for the loss of tripeptidyl-peptidase I
-
-
?
additional information
?
-
-
substrates not cleaved after 24 h of digestion: dynorphin, beta-casomorphin-7, Leu-enkephalin, Met-enkephalin, neurokinin-A, LVV-hemorphin, bradykinin
-
-
?
additional information
?
-
-
the enzymne cleaves tripeptides from synthetic substrates provided that the N-terminus is unsubstituted and the amino acid in the P1 position is not charged. The enzyme also cleaves small peptides, angiotensin II and glucagon, releasing tripeptides but does not appear to demonstrate any preference for amino acids on either side of the cleavage site. Substrates with a charged amino acid in the P1 position appear to be resistant to hydrolysis
-
-
?
additional information
?
-
-
an inherited deficiency of tripeptidyl peptidase I activity causes a fatal lysosomal storage disorder, classic late infantile neuronal ceroid lipofuscinosis, CLN2
-
-
?
additional information
?
-
development of fluorescence resonance energy transfer (FRET) peptides using tryptophan as the fluorophore to study TPP-I hydrolytic properties. Solvent kinetic isotope effects show the importance of the free N-terminus amino group of the substrates, whose absence results in a more complex solvent-dependent enzyme-substrate interaction and catalytic process. To investigate the exopeptidase activity of TPP-I, the randomized sequence MCA-GXXFXXQ-EDDnp is assayed and the products of hydrolysis analyzed by Edman degradation. TTP-I retains its N-terminus tripeptidase character even in randomized sequences and the preferences at the prime sites are similar to those reported for tripeptidyl amino peptidase
-
-
?
additional information
?
-
development of fluorescence resonance energy transfer (FRET) peptides using tryptophan as the fluorophore to study TPP-I hydrolytic properties. Solvent kinetic isotope effects show the importance of the free N-terminus amino group of the substrates, whose absence results in a more complex solvent-dependent enzyme-substrate interaction and catalytic process. To investigate the exopeptidase activity of TPP-I, the randomized sequence MCA-GXXFXXQ-EDDnp is assayed and the products of hydrolysis analyzed by Edman degradation. TTP-I retains its N-terminus tripeptidase character even in randomized sequences and the preferences at the prime sites are similar to those reported for tripeptidyl amino peptidase
-
-
?
additional information
?
-
-
N-terminal exopeptidase that removes tripeptide units provided the P3 residue is unsubstituted
-
-
?
additional information
?
-
-
Met-2-naphthylamide, succinyl-Gly-Pro-Met 2-naphthylamide, Pro-Met-7-amido-4-methylcoumarin, Met-7-amido-4-methylcoumarin, methoxysuccinyl-Gly-Pro-Met-7-amido-4-methylcoumarin, benzyloxy-Arg-Arg-7-amido-4-methylcoumarin, Arg-7-amido-4-methylcoumarin, Pro-Ala-4-nitroanilide, Ala 4-nitroanilide, tert-butyloxycarbonyl-Gly-Pro-Ala 4-nitroanilide, benzoyl-Val-Pro-Arg 4-nitroanilide
-
-
?
additional information
?
-
-
exopeptidase involved in intracellular (lysosomal) degradation of collagen fibrils
-
-
?
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