TPP1_DICDI
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 03-AUG-2022, entry version 102.
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 (Slime mold).
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.DDB0234303; -.
DR MEROPS; S53.003; -.
DR PaxDb; Q55CT0; -.
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; HDEMKRM; -.
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; -; 1.
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 Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF52743; SSF52743; 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
