ID A0A2K5IJW4_COLAP Unreviewed; 563 AA. AC A0A2K5IJW4; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 03-MAY-2023, entry version 27. 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:ENSCANP00000016895.1, ECO:0000313|Proteomes:UP000233080}; RN [1] {ECO:0000313|Ensembl:ENSCANP00000016895.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2023) 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 AlphaFoldDB; A0A2K5IJW4; -. DR STRING; 336983.ENSCANP00000016895; -. DR Ensembl; ENSCANT00000039836.1; ENSCANP00000016895.1; ENSCANG00000031868.1. DR OMA; YARSVCN; -. DR Proteomes; UP000233080; Unplaced. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. 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:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 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 4: Predicted; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE- KW ProRule:PRU01032}; Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01032}; KW Lysosome {ECO:0000256|ARBA:ARBA00023228}; 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 BINDING 517 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 518 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 541 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032" FT BINDING 543 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" 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 //