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Database: UniProt
Entry: TPP1_PONAB
LinkDB: TPP1_PONAB
Original site: 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   08-MAY-2019, entry version 76.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
CC       generates tripeptides from the breakdown products produced by
CC       lysosomal proteinases. Requires substrates with an unsubstituted
CC       N-terminus (By similarity). {ECO:0000250|UniProtKB:Q9EQV6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal tripeptide from a polypeptide,
CC         but 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.
CC       {ECO:0000250|UniProtKB:O14773};
CC   -!- SUBUNIT: Monomer. Interacts with CLN5.
CC       {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
CC       activity (By similarity). {ECO:0000250|UniProtKB:O14773}.
DR   EMBL; CR857144; CAH89446.1; -; mRNA.
DR   RefSeq; NP_001124619.1; NM_001131147.1.
DR   SMR; Q5RFL1; -.
DR   STRING; 9601.ENSPPYP00000004053; -.
DR   MEROPS; S53.003; -.
DR   GeneID; 100440001; -.
DR   KEGG; pon:100440001; -.
DR   CTD; 1200; -.
DR   eggNOG; ENOG410IICY; Eukaryota.
DR   eggNOG; COG4934; LUCA.
DR   InParanoid; Q5RFL1; -.
DR   KO; K01279; -.
DR   OrthoDB; 1294880at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
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: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; IPR036852; Peptidase_S8/S53_dom_sf.
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   2: Evidence at transcript level;
KW   Autocatalytic cleavage; Calcium; Complete proteome; Disulfide bond;
KW   Glycoprotein; Hydrolase; Lysosome; Metal-binding; Protease;
KW   Reference proteome; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     19       {ECO:0000250|UniProtKB:O14773}.
FT   PROPEP       20    195       Removed in mature form.
FT                                {ECO:0000250|UniProtKB:O14773}.
FT                                /FTId=PRO_0000027382.
FT   CHAIN       196    564       Tripeptidyl-peptidase 1.
FT                                /FTId=PRO_0000027383.
FT   DOMAIN      199    564       Peptidase S53.
FT   ACT_SITE    272    272       Charge relay system.
FT                                {ECO:0000250|UniProtKB:O14773}.
FT   ACT_SITE    276    276       Charge relay system.
FT                                {ECO:0000250|UniProtKB:O14773}.
FT   ACT_SITE    475    475       Charge relay system.
FT                                {ECO:0000250|UniProtKB:O14773}.
FT   METAL       518    518       Calcium. {ECO:0000250|UniProtKB:O14773}.
FT   METAL       519    519       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:O14773}.
FT   METAL       540    540       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:O14773}.
FT   METAL       542    542       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:O14773}.
FT   METAL       544    544       Calcium. {ECO:0000250|UniProtKB:O14773}.
FT   CARBOHYD    210    210       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    222    222       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    286    286       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    313    313       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    443    443       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    111    122       {ECO:0000250|UniProtKB:O14773}.
FT   DISULFID    365    527       {ECO:0000250|UniProtKB:O14773}.
FT   DISULFID    523    538       {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
//
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