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Protein

Tripeptidyl-peptidase 2

Gene

tpp-2

Organism
Caenorhabditis elegans
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 (By similarity). Has a role in regulation of fat storage.By similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei93 – 931Charge relay systemBy similarity
Active sitei314 – 3141Charge relay systemBy similarity
Active sitei499 – 4991Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

  • positive regulation of lipid storage Source: UniProtKB
  • proteolysis Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

ReactomeiR-CEL-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ09541.

Protein family/group databases

MEROPSiS08.A56.

Names & Taxonomyi

Protein namesi
Recommended name:
Tripeptidyl-peptidase 2 (EC:3.4.14.10)
Short name:
TPP2
Alternative name(s):
Tripeptidyl aminopeptidase
Tripeptidyl peptidase II
Short name:
TPPII
Gene namesi
Name:tpp-2
ORF Names:F21H12.6
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome II

Organism-specific databases

WormBaseiF21H12.6; CE01917; WBGene00017686; tpp-2.

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown causes reduced fat storage but does not affect feeding behavior.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13741374Tripeptidyl-peptidase 2PRO_0000076427Add
BLAST

Proteomic databases

EPDiQ09541.
PaxDbiQ09541.
PRIDEiQ09541.

Expressioni

Tissue specificityi

Expressed in intestinal fat-storing cells and some head neurons.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi6239.F21H12.6.

Structurei

3D structure databases

ProteinModelPortaliQ09541.
SMRiQ09541. Positions 311-554.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini89 – 559471Peptidase 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.
InParanoidiQ09541.
KOiK01280.
OMAiHANWSNS.
OrthoDBiEOG786H2B.
PhylomeDBiQ09541.

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.

Q09541-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIVIRNWQRI SYLSFCRFST RSLSIQQFQK TPLLLVVRQQ GSARLKMTSS
60 70 80 90 100
PPEIVPQQPL DALLLNKTDT EQEIFLTKYP NYDGRDILIA ILDTGVDPSL
110 120 130 140 150
PGMQVTTTGE RKMFDVIDCS GAGDVDTSIT RTVKDGVIEG ISGRKLAIPE
160 170 180 190 200
KWKCPTGQYH VGLKPIFELY TKGVKSRVIS ERKEDVVGPS HNIAASEALK
210 220 230 240 250
QLTEHEKVVG GTSEKTSDKW AREDFACKVD FLKSMASVAD VGPVADVVTW
260 270 280 290 300
HDGEMWRVCI DTSFRGRLGL GNVLGTFRET GDYAYLTNKD SVVYTVRVSP
310 320 330 340 350
DGNLTEIVVP SGAHGSHVAG IAAANYPDNP QKNGLAPGAK ILSLNIGDHR
360 370 380 390 400
LGAMETGQAM TRAFNMCAEL NVDIINMSFG EGTHLPDVGR VIEEARRLIN
410 420 430 440 450
RRGVIYVCSA GNQGPALSTV GAPGGTTTGV IGIGAYLTSE SADTLYGVYK
460 470 480 490 500
PVESSIYPWS SRGPCQDGKL GVSLVAPAAA FAGVPQYCRQ SMQMMNGTSM
510 520 530 540 550
SSPNAAGNVA CMLSGLKQNN LKWTPYTVRM ALENTAYMLP HIESFSQGQG
560 570 580 590 600
MIKIATAYEK LSEILVNKVF PPRLTHFEIN VSNHCKKSKG VYVREPNWNG
610 620 630 640 650
PQEFTIGVEP IFQNHLSDNN LPAISFEKQI ILQSTAPWVS HPQTMFVVAQ
660 670 680 690 700
ERTMVVTVDA SKAPKGANYT EIVGIDTADP SLGPIFRIPV TVINPEKVAV
710 720 730 740 750
DQYTSRLVGK SGVTERRFVE VPSWATSAKI TLRSTNKDEM DRFTLHTVYI
760 770 780 790 800
EDDKCSRNTE TQKIQGPIGN EWSKSITVQG GKTLEACVVR AWSRGKNPVD
810 820 830 840 850
VDMTIDFFGV KKPTSISLIH GATNTPIRFQ AAPTKSIDVS PSISLKSLVV
860 870 880 890 900
SLKPQSAKVE PLGPRDMFLT SGLQINRLLL TYQLKVQKPS EVQLQLAGLT
910 920 930 940 950
PYLYESPVDC VLFQIFGANK SFVGASSSYP DRWTQKLEKG DYTIQAQIRY
960 970 980 990 1000
PDDQVLQGMK ELPLLVHVKL GNKISVDLAA SASDATLGKE CKFAGKALLP
1010 1020 1030 1040 1050
NQEMTVYAMN IADDKLPKTI VPTSGSFLAG TFSALKDSDL SDVDKSEVIY
1060 1070 1080 1090 1100
FLSEYSTRPT KGLSMVTTKK DTNQNQEMTD AIRDLEVSWV QKLTDEKAAK
1110 1120 1130 1140 1150
EFFEACLQKY PDHLPLLQNR VKQLMQAKLV DQTPENVQKI IELCGQILQI
1160 1170 1180 1190 1200
TKPNETLQFS SVKQEHDDDL LTVDKWLALT GGSEDQRKDV VKLISQFEER
1210 1220 1230 1240 1250
KKSIILALQA LSSLEQDIEV RKSKFDVPAS LRFGGITPLI FGGKQGEVIN
1260 1270 1280 1290 1300
KKSEGYEALK SKSEQIDATV SEELKKLDSN WTGNQFYVKL LVWLSADDTK
1310 1320 1330 1340 1350
TALISAKHAA ALGQFGRCAK LLNKAGDELK SSATDSQAVD TSLAEVCESL
1360 1370
EWNHLATHFK NSALIKNRTS YRLF
Length:1,374
Mass (Da):151,089
Last modified:November 1, 1997 - v1
Checksum:i6937C862AED1E7FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080717 Genomic DNA. Translation: CCD66120.1.
PIRiT16129.
RefSeqiNP_495221.1. NM_062820.3.
UniGeneiCel.17531.

Genome annotation databases

EnsemblMetazoaiF21H12.6; F21H12.6; WBGene00017686.
GeneIDi174018.
KEGGicel:CELE_F21H12.6.
UCSCiF21H12.6. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080717 Genomic DNA. Translation: CCD66120.1.
PIRiT16129.
RefSeqiNP_495221.1. NM_062820.3.
UniGeneiCel.17531.

3D structure databases

ProteinModelPortaliQ09541.
SMRiQ09541. Positions 311-554.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F21H12.6.

Protein family/group databases

MEROPSiS08.A56.

Proteomic databases

EPDiQ09541.
PaxDbiQ09541.
PRIDEiQ09541.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF21H12.6; F21H12.6; WBGene00017686.
GeneIDi174018.
KEGGicel:CELE_F21H12.6.
UCSCiF21H12.6. c. elegans.

Organism-specific databases

CTDi174018.
WormBaseiF21H12.6; CE01917; WBGene00017686; tpp-2.

Phylogenomic databases

eggNOGiKOG1114. Eukaryota.
COG1404. LUCA.
GeneTreeiENSGT00390000014623.
HOGENOMiHOG000008178.
InParanoidiQ09541.
KOiK01280.
OMAiHANWSNS.
OrthoDBiEOG786H2B.
PhylomeDBiQ09541.

Enzyme and pathway databases

ReactomeiR-CEL-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ09541.

Miscellaneous databases

PROiQ09541.

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

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Tripeptidyl peptidase II promotes fat formation in a conserved fashion."
    McKay R.M., McKay J.P., Suh J.M., Avery L., Graff J.M.
    EMBO Rep. 8:1183-1189(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiTPP2_CAEEL
AccessioniPrimary (citable) accession number: Q09541
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.