ID   TPP1_DICDI              Reviewed;         600 AA.
AC   Q55CT0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Tripeptidyl-peptidase 1;
DE            Short=TPP-1;
DE            EC=3.4.14.9;
DE   AltName: Full=Tripeptidyl aminopeptidase;
DE   AltName: Full=Tripeptidyl-peptidase I;
DE            Short=TPP-I;
DE   Flags: Precursor;
GN   Name=tpp1; ORFNames=DDB_G0269914;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Serine protease with tripeptidyl-peptidase I activity.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal tripeptide from a polypeptide, but
CC         also has endopeptidase activity.; EC=3.4.14.9;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: Activated by autocatalytic proteolytical processing upon
CC       acidification. N-glycosylation is required for processing and activity
CC       (By similarity). {ECO:0000250}.
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DR   EMBL; AAFI02000005; EAL72307.1; -; Genomic_DNA.
DR   RefSeq; XP_646401.1; XM_641309.1.
DR   AlphaFoldDB; Q55CT0; -.
DR   SMR; Q55CT0; -.
DR   STRING; 44689.Q55CT0; -.
DR   MEROPS; S53.003; -.
DR   GlyCosmos; Q55CT0; 5 sites, No reported glycans.
DR   PaxDb; 44689-DDB0234303; -.
DR   EnsemblProtists; EAL72307; EAL72307; DDB_G0269914.
DR   GeneID; 8617356; -.
DR   KEGG; ddi:DDB_G0269914; -.
DR   dictyBase; DDB_G0269914; tpp1.
DR   eggNOG; ENOG502QR6D; Eukaryota.
DR   HOGENOM; CLU_013783_5_1_1; -.
DR   InParanoid; Q55CT0; -.
DR   OMA; VTITPDC; -.
DR   PhylomeDB; Q55CT0; -.
DR   PRO; PR:Q55CT0; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IDA:dictyBase.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IMP:dictyBase.
DR   GO; GO:0019954; P:asexual reproduction; IMP:dictyBase.
DR   GO; GO:0044351; P:macropinocytosis; IMP:dictyBase.
DR   GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR   GO; GO:0006508; P:proteolysis; ISS:dictyBase.
DR   GO; GO:1902349; P:response to chloroquine; IMP:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; IMP:dictyBase.
DR   CDD; cd04056; Peptidases_S53; 1.
DR   CDD; cd11377; Pro-peptidase_S53; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   PANTHER; PTHR14218:SF15; TRIPEPTIDYL-PEPTIDASE 1; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Calcium; Disulfide bond; Glycoprotein; Hydrolase;
KW   Metal-binding; Protease; Reference proteome; Secreted; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..220
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000327570"
FT   CHAIN           221..600
FT                   /note="Tripeptidyl-peptidase 1"
FT                   /id="PRO_0000327571"
FT   DOMAIN          248..600
FT                   /note="Peptidase S53"
FT   ACT_SITE        318
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        322
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        514
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         559
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         560
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         579
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         581
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        411..570
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   600 AA;  67296 MW;  D9E97C1279BC9C18 CRC64;
     MNIKFNLIII ILFILFISNV NCKKIKNKKH LTPQRLRRFV EHSKPISLNK KVWKITEIEN
     IFSAQIELTF GIRQRNIVEL EDFVWRVSDP NDSLYGSYKT FEEIKEWVKP LDESIDAVKN
     WLIENDINEF TVTKSGDFIR TIVSIDKAEE LLSVRYNKMV HKLSKQSFFR SLDPYTIPRE
     LYDHIDFIGG VNHLPLLSPR PKESSGSAGG GGGGKVNGIG YELESLRNNK QIKSFNDKKV
     AARNGDPYLS PDLIRKEMNV SQTSTNSTHL GNSQAIAQFL KEYFSPSDLK IFQYRFGLEP
     SQVDNIIGPN QNLNPGIETA LDIQYIMAMA PDVPTWIVST GGLHEGQEPF LDWLVDLSSN
     PKLPLVHSIS YGDDESSIGL AYTDRVDTEF KKYAAMGRTI VFSSGDFGVG CNDDCDSFSP
     GWPASSRFVL AVGGVIKKKD GSIIGDEISG GGFSNYFSRP WYQVDECSSY IEWLNGSLSS
     FYNQSGRGFP DISSFSENVV ILYKDKLMPI GGTSASAPII AGLLSLINDQ RLQKNQSPIG
     LFNPLLYKIA RDHPNSFLDI DFGENNYKCC TNGFKSKSGW DPVTGLGLPN FDELVKYCLE
//