ID A0A2K5IJW4_COLAP Unreviewed; 563 AA. AC A0A2K5IJW4; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 25-MAY-2022, entry version 22. DE RecName: Full=Tripeptidyl-peptidase 1 {ECO:0000256|ARBA:ARBA00020254}; DE EC=3.4.14.9 {ECO:0000256|ARBA:ARBA00012067}; DE AltName: Full=Tripeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00032232}; DE AltName: Full=Tripeptidyl-peptidase I {ECO:0000256|ARBA:ARBA00032661}; OS Colobus angolensis palliatus (Peters' Angolan colobus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Colobinae; Colobus. OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000016895, ECO:0000313|Proteomes:UP000233080}; RN [1] {ECO:0000313|Ensembl:ENSCANP00000016895} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2018) to UniProtKB. 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 Evidence={ECO:0000256|ARBA:ARBA00000884}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01032}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PROSITE- CC ProRule:PRU01032}; CC -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000256|ARBA:ARBA00004223}. 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 STRING; 336983.ENSCANP00000016895; -. DR Ensembl; ENSCANT00000039836; ENSCANP00000016895; ENSCANG00000031868. DR OMA; HDEMKRM; -. DR Proteomes; UP000233080; Unplaced. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0045121; C:membrane raft; IEA:Ensembl. DR GO; GO:0055037; C:recycling endosome; IEA:Ensembl. DR GO; GO:0035727; F:lysophosphatidic acid binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0120146; F:sulfatide binding; IEA:Ensembl. DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC. DR GO; GO:0045453; P:bone resorption; IEA:Ensembl. DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl. DR GO; GO:1905146; P:lysosomal protein catabolic process; IEA:Ensembl. DR GO; GO:0007040; P:lysosome organization; IEA:Ensembl. DR GO; GO:0007399; P:nervous system development; IEA:Ensembl. DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl. DR GO; GO:0043171; P:peptide catabolic process; IEA:Ensembl. DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IEA:Ensembl. 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 4: Predicted; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE- KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU01032}; Protease {ECO:0000256|PROSITE-ProRule:PRU01032}; KW Reference proteome {ECO:0000313|Proteomes:UP000233080}; KW Serine protease {ECO:0000256|PROSITE-ProRule:PRU01032}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..563 FT /note="Tripeptidyl-peptidase 1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014368675" FT DOMAIN 199..563 FT /note="Peptidase S53" FT /evidence="ECO:0000259|PROSITE:PS51695" FT ACT_SITE 272 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT ACT_SITE 276 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT ACT_SITE 475 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT METAL 517 FT /note="Calcium" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT METAL 518 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT METAL 541 FT /note="Calcium; via carbonyl oxygen" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT METAL 543 FT /note="Calcium" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" SQ SEQUENCE 563 AA; 61279 MW; AF4CAE9A18AEFF65 CRC64; MGLQACLLGL FALILSGKCS YSPEPDQRRT LPPGWVSLGR ADPEEELSLT FALRQQNLER LSELVQAVSD PNSPQYGKYL TLENVADLVR PSPLTLHTVQ KWLLAAGAQK CHSVITQDFL TCWLSIRQAE LLLPGAQFHH YVGGPTETHV VRSPRPYQLP QALAPHVDFV GGLHRFPPTS SLRQRPEPQV TGTVGLHLGV TPSVIRKRYN LTSQDVGSGT SNNSQACAQF LEQYFHDSDL AQFMRLFGGN FAHQASVTRV VGQQGRGRAG IEASLDVQYL MSAGANISTW VYSSPGRHEG QEPFLQWLIL LSNESALPHV HTVSYGDEED SLSSAYIQRV NTELMKAAAR GLTLLFASGD SGAGCWSVSG RHQFRPTFPA SSPYVTTVGG TSFQEPFLIT NEIVDYISGG GFSNVFPRPS YQEEAVAKFL SSSPHLPPSS YFNASGRAYP DVAALSDGYW VVSNRVPIPW VSGTSASTPV FGGLLSLINE HRILSGRPPL GFLNPRLYHQ HGAGLFDVTH GCHESCLDDE VEGQGFCSGP GWDPVTGWGT PNFPALLKTL LNP //