TPP1_PONAB
ID TPP1_PONAB Reviewed; 564 AA.
AC Q5RFL1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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; Synonyms=CLN2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I
CC activity. May act as a non-specific lysosomal peptidase which generates
CC tripeptides from the breakdown products produced by lysosomal
CC proteinases. Requires substrates with an unsubstituted N-terminus (By
CC similarity). {ECO:0000250|UniProtKB:Q9EQV6}.
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;
CC Evidence={ECO:0000250|UniProtKB:O14773};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:O14773};
CC -!- SUBUNIT: Monomer. Interacts with CLN5. Interacts with CLN3 (By
CC similarity). {ECO:0000250|UniProtKB:O14773}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:O14773}.
CC Melanosome {ECO:0000250|UniProtKB:O14773}.
CC -!- PTM: Activated by autocatalytic proteolytical processing upon
CC acidification. N-glycosylation is required for processing and activity
CC (By similarity). {ECO:0000250|UniProtKB:O14773}.
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DR EMBL; CR857144; CAH89446.1; -; mRNA.
DR RefSeq; NP_001124619.1; NM_001131147.1.
DR AlphaFoldDB; Q5RFL1; -.
DR SMR; Q5RFL1; -.
DR STRING; 9601.ENSPPYP00000004053; -.
DR MEROPS; S53.003; -.
DR GeneID; 100440001; -.
DR KEGG; pon:100440001; -.
DR CTD; 1200; -.
DR eggNOG; ENOG502QR6D; Eukaryota.
DR InParanoid; Q5RFL1; -.
DR OrthoDB; 1294880at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0035727; F:lysophosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0120146; F:sulfatide binding; ISS:UniProtKB.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045453; P:bone resorption; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 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; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR Pfam; PF00082; Peptidase_S8; 1.
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 2: Evidence at transcript level;
KW Autocatalytic cleavage; Calcium; Disulfide bond; Glycoprotein; Hydrolase;
KW Lysosome; Metal-binding; Protease; Reference proteome; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT PROPEP 20..195
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT /id="PRO_0000027382"
FT CHAIN 196..564
FT /note="Tripeptidyl-peptidase 1"
FT /id="PRO_0000027383"
FT DOMAIN 199..564
FT /note="Peptidase S53"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT ACT_SITE 475
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT BINDING 518
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT BINDING 540
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT BINDING 544
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..122
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT DISULFID 365..527
FT /evidence="ECO:0000250|UniProtKB:O14773"
FT DISULFID 523..538
FT /evidence="ECO:0000250|UniProtKB:O14773"
SQ SEQUENCE 564 AA; 61238 MW; 381FDB588837B0F1 CRC64;
MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT FALRQQNVER
LSELVQAVSD PSSPQYGKYL TLENVADLVR PSPLTLHTVQ KWLLAAGAQK CHSVITQDFL
TCWLSIRQAE LLLPGAEFHH YVGGPTETHV VRSPHPYQLP QALAPHVDFV GGLHRFPPTS
SLRQHPEPQV TGTVGLHLGV TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL
AQFMRLFGGN FAHQASVARV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG
QEPFLQWLML LSNESALPHV HTVSYGDEED SLSSAYIQRV NTELMKAAAR GLTLLFASGD
SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFLEPFLTT NEIVDYISGG GFSNVFPRPS
YQEEAVTKFL SSSPHLPPSS YFNASGRAYP DVAALSDGYW VVSNRVPIPW VSGTSASTPV
FGGGILSLIN EHRILSGRPP LGFLNPRLYQ QHGAGLFDVT HGCHESCLDE EVEGQGFCSG
PGWDPVTGWG TPNFPALPKT LLNP
