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Database: UniProt
Entry: TPP1_PANTR
LinkDB: TPP1_PANTR
Original site: TPP1_PANTR 
ID   TPP1_PANTR              Reviewed;         563 AA.
AC   Q5IS74;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 99.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA   Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA   Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT   "Accelerated evolution of nervous system genes in the origin of Homo
RT   sapiens.";
RL   Cell 119:1027-1040(2004).
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; AY665254; AAV74292.1; -; mRNA.
DR   RefSeq; NP_001013025.1; NM_001013007.1.
DR   SMR; Q5IS74; -.
DR   STRING; 9598.ENSPTRP00000005774; -.
DR   MEROPS; S53.003; -.
DR   PaxDb; Q5IS74; -.
DR   PRIDE; Q5IS74; -.
DR   Ensembl; ENSPTRT00000006261; ENSPTRP00000005774; ENSPTRG00000003299.
DR   GeneID; 450999; -.
DR   KEGG; ptr:450999; -.
DR   CTD; 1200; -.
DR   VGNC; VGNC:10187; TPP1.
DR   eggNOG; ENOG410IICY; Eukaryota.
DR   eggNOG; COG4934; LUCA.
DR   GeneTree; ENSGT00390000008684; -.
DR   HOGENOM; HOG000171253; -.
DR   InParanoid; Q5IS74; -.
DR   KO; K01279; -.
DR   OMA; FDVTEGC; -.
DR   OrthoDB; 1294880at2759; -.
DR   TreeFam; TF333497; -.
DR   Proteomes; UP000002277; Chromosome 11.
DR   Bgee; ENSPTRG00000003299; Expressed in 6 organ(s), highest expression level in adult mammalian kidney.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
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:0008240; F:tripeptidyl-peptidase activity; IBA:GO_Central.
DR   GO; GO:0045453; P:bone resorption; ISS:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
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_0000027380.
FT   CHAIN       196    563       Tripeptidyl-peptidase 1.
FT                                /FTId=PRO_0000027381.
FT   DOMAIN      199    563       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       517    517       Calcium. {ECO:0000250|UniProtKB:O14773}.
FT   METAL       518    518       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:O14773}.
FT   METAL       539    539       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:O14773}.
FT   METAL       541    541       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:O14773}.
FT   METAL       543    543       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    526       {ECO:0000250|UniProtKB:O14773}.
FT   DISULFID    522    537       {ECO:0000250|UniProtKB:O14773}.
SQ   SEQUENCE   563 AA;  61295 MW;  F8B1991276E8F361 CRC64;
     MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT FALRQQNVER
     LSELVQAVSD PSSPQYGKYL TLENVADLVR PSPLTLRTVQ KWLLAAGARK CHSVITQDFL
     TCWLSIRQAE LLLPGAEFHH YVGGPTETHV VRSPHPYQLP QALAPHVDFV GGLHRFPPTS
     SLRQRPEPQV TGTVGLHLGV TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL
     AQFMRLFGGN FAHQASVARV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG
     QEPFLQWLML LSNESALPHV HTVSYGDDED SLSSAYIQRV NTELMKAAAR GLTLLFASGD
     SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFQEPFLIT NEIVDYISGG GFSNVFPRPS
     YQEEAVTKFL SSSPHLPPSS YFNASGRAYP DVAALSDGYW VVSNRVPIPW VSGTSASTPV
     FGGILSLINE HRILSGRPPL GFLNPRLYQQ HGAGLFDVTR GCHESCLDEE VEGQGFCSGP
     GWDPVTGWGT PNFPALLKTL LNP
//
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