ID TPP1_BOVIN Reviewed; 563 AA. AC Q0V8B6; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 24-JAN-2024, entry version 87. 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 Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Heart ventricle; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BT026303; ABG81459.1; -; mRNA. DR EMBL; BC119827; AAI19828.1; -; mRNA. DR RefSeq; NP_001069186.1; NM_001075718.1. DR AlphaFoldDB; Q0V8B6; -. DR SMR; Q0V8B6; -. DR STRING; 9913.ENSBTAP00000062713; -. DR MEROPS; S53.003; -. DR GlyCosmos; Q0V8B6; 5 sites, No reported glycans. DR PaxDb; 9913-ENSBTAP00000020469; -. DR PeptideAtlas; Q0V8B6; -. DR GeneID; 515575; -. DR KEGG; bta:515575; -. DR CTD; 1200; -. DR eggNOG; ENOG502QR6D; Eukaryota. DR InParanoid; Q0V8B6; -. DR OrthoDB; 1405251at2759; -. DR Proteomes; UP000009136; 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:0004175; F:endopeptidase activity; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0120146; F:sulfatide binding; ISS:UniProtKB. DR GO; GO:0008240; F:tripeptidyl-peptidase activity; ISS:UniProtKB. DR GO; GO:0045453; P:bone resorption; ISS:UniProtKB. DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central. 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; Peptidase S8/S53 domain; 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 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 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_0000291586" FT CHAIN 196..563 FT /note="Tripeptidyl-peptidase 1" FT /id="PRO_0000291587" FT DOMAIN 199..563 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 517 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" 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 539 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:O14773" FT BINDING 541 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:O14773" FT BINDING 543 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..526 FT /evidence="ECO:0000250|UniProtKB:O14773" FT DISULFID 522..537 FT /evidence="ECO:0000250|UniProtKB:O14773" SQ SEQUENCE 563 AA; 61352 MW; 6D23396D375612C1 CRC64; MGPRSGLLGL FALFVAGKCS YSPEPDQQRR LPPGWVSLGR ADPEEELSLT FALRQQNVKR LSELVQAVSD PGSPRYGKYL TLEDVAELVR PSPLTLHTVQ KWLLAAGARN CHSVTTQDFL TCWLSVRQAE LLLSGAEFHH YVGGPAETHA VRSLHPYRLP KALAPHVDFV GGLHRFPPTS TLRQHPEPQV PGTVGLHLGV TPSVIRKRYN LTAQDVGSGT TNNSQACAQF LEQYFHDSDL AEFMRLFGGD FAHQASVARV VGQQGRGRAG IEASLDVEYL MSAGANISTW VYSSPGRHES QEPFLQWLLL LSNESALPYV HTVSYGDDED SLSSTYIQRV NTELMKAAAR GLTLLFASGD SGAGCWSVSG RHQFRPSFPA SSPYVTTVGG TSFQNPFRVT DEVVDYISGG GFSNVFPRPS YQEEAVTRYL SSSPHLPPSS YFNASGRAYP DVAALSDGYW VVSNHVPIPW VSGTSASTPV FGGLLSLINE HRILRGLPPL GFLNPRLYQK HGAGLFDVTR GCHESCLNEE VEGQGFCSGP GWDPVTGWGT PNFPALLKTL MNP //