TPP2_CAEEL
ID TPP2_CAEEL Reviewed; 1374 AA.
AC Q09541;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tripeptidyl-peptidase 2;
DE Short=TPP2;
DE EC=3.4.14.10 {ECO:0000250|UniProtKB:P29144};
DE AltName: Full=Tripeptidyl aminopeptidase;
DE AltName: Full=Tripeptidyl peptidase II;
DE Short=TPPII;
GN Name=tpp-2; ORFNames=F21H12.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17932511; DOI=10.1038/sj.embor.7401086;
RA McKay R.M., McKay J.P., Suh J.M., Avery L., Graff J.M.;
RT "Tripeptidyl peptidase II promotes fat formation in a conserved fashion.";
RL EMBO Rep. 8:1183-1189(2007).
CC -!- FUNCTION: Component of the proteolytic cascade acting downstream of the
CC 26S proteasome in the ubiquitin-proteasome pathway (By similarity). Has
CC a role in regulation of fat storage. {ECO:0000250,
CC ECO:0000269|PubMed:17932511}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000250|UniProtKB:P29144};
CC -!- TISSUE SPECIFICITY: Expressed in intestinal fat-storing cells and some
CC head neurons. {ECO:0000269|PubMed:17932511}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes reduced fat
CC storage but does not affect feeding behavior.
CC {ECO:0000269|PubMed:17932511}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; FO080717; CCD66120.1; -; Genomic_DNA.
DR PIR; T16129; T16129.
DR RefSeq; NP_495221.1; NM_062820.3.
DR AlphaFoldDB; Q09541; -.
DR SMR; Q09541; -.
DR BioGRID; 39359; 8.
DR STRING; 6239.F21H12.6; -.
DR MEROPS; S08.A56; -.
DR EPD; Q09541; -.
DR PaxDb; Q09541; -.
DR PeptideAtlas; Q09541; -.
DR PRIDE; Q09541; -.
DR EnsemblMetazoa; F21H12.6.1; F21H12.6.1; WBGene00017686.
DR GeneID; 174018; -.
DR KEGG; cel:CELE_F21H12.6; -.
DR UCSC; F21H12.6; c. elegans.
DR CTD; 174018; -.
DR WormBase; F21H12.6; CE01917; WBGene00017686; tpp-2.
DR eggNOG; KOG1114; Eukaryota.
DR GeneTree; ENSGT00390000014623; -.
DR HOGENOM; CLU_003084_1_0_1; -.
DR InParanoid; Q09541; -.
DR OMA; SLRDFQC; -.
DR OrthoDB; 156304at2759; -.
DR PhylomeDB; Q09541; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q09541; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017686; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0010884; P:positive regulation of lipid storage; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR022229; Peptidase_S8A_TPPII.
DR InterPro; IPR034051; TPP_II_domain.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Hydrolase; Protease; Reference proteome; Serine protease.
FT CHAIN 1..1374
FT /note="Tripeptidyl-peptidase 2"
FT /id="PRO_0000076427"
FT DOMAIN 62..558
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 93
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 314
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 499
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1374 AA; 151089 MW; 6937C862AED1E7FB CRC64;
MIVIRNWQRI SYLSFCRFST RSLSIQQFQK TPLLLVVRQQ GSARLKMTSS PPEIVPQQPL
DALLLNKTDT EQEIFLTKYP NYDGRDILIA ILDTGVDPSL PGMQVTTTGE RKMFDVIDCS
GAGDVDTSIT RTVKDGVIEG ISGRKLAIPE KWKCPTGQYH VGLKPIFELY TKGVKSRVIS
ERKEDVVGPS HNIAASEALK QLTEHEKVVG GTSEKTSDKW AREDFACKVD FLKSMASVAD
VGPVADVVTW HDGEMWRVCI DTSFRGRLGL GNVLGTFRET GDYAYLTNKD SVVYTVRVSP
DGNLTEIVVP SGAHGSHVAG IAAANYPDNP QKNGLAPGAK ILSLNIGDHR LGAMETGQAM
TRAFNMCAEL NVDIINMSFG EGTHLPDVGR VIEEARRLIN RRGVIYVCSA GNQGPALSTV
GAPGGTTTGV IGIGAYLTSE SADTLYGVYK PVESSIYPWS SRGPCQDGKL GVSLVAPAAA
FAGVPQYCRQ SMQMMNGTSM SSPNAAGNVA CMLSGLKQNN LKWTPYTVRM ALENTAYMLP
HIESFSQGQG MIKIATAYEK LSEILVNKVF PPRLTHFEIN VSNHCKKSKG VYVREPNWNG
PQEFTIGVEP IFQNHLSDNN LPAISFEKQI ILQSTAPWVS HPQTMFVVAQ ERTMVVTVDA
SKAPKGANYT EIVGIDTADP SLGPIFRIPV TVINPEKVAV DQYTSRLVGK SGVTERRFVE
VPSWATSAKI TLRSTNKDEM DRFTLHTVYI EDDKCSRNTE TQKIQGPIGN EWSKSITVQG
GKTLEACVVR AWSRGKNPVD VDMTIDFFGV KKPTSISLIH GATNTPIRFQ AAPTKSIDVS
PSISLKSLVV SLKPQSAKVE PLGPRDMFLT SGLQINRLLL TYQLKVQKPS EVQLQLAGLT
PYLYESPVDC VLFQIFGANK SFVGASSSYP DRWTQKLEKG DYTIQAQIRY PDDQVLQGMK
ELPLLVHVKL GNKISVDLAA SASDATLGKE CKFAGKALLP NQEMTVYAMN IADDKLPKTI
VPTSGSFLAG TFSALKDSDL SDVDKSEVIY FLSEYSTRPT KGLSMVTTKK DTNQNQEMTD
AIRDLEVSWV QKLTDEKAAK EFFEACLQKY PDHLPLLQNR VKQLMQAKLV DQTPENVQKI
IELCGQILQI TKPNETLQFS SVKQEHDDDL LTVDKWLALT GGSEDQRKDV VKLISQFEER
KKSIILALQA LSSLEQDIEV RKSKFDVPAS LRFGGITPLI FGGKQGEVIN KKSEGYEALK
SKSEQIDATV SEELKKLDSN WTGNQFYVKL LVWLSADDTK TALISAKHAA ALGQFGRCAK
LLNKAGDELK SSATDSQAVD TSLAEVCESL EWNHLATHFK NSALIKNRTS YRLF
