ID   A0A2K5IJW4_COLAP        Unreviewed;       563 AA.
AC   A0A2K5IJW4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   22-FEB-2023, entry version 26.
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 (OCT-2022) 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}.
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DR   AlphaFoldDB; A0A2K5IJW4; -.
DR   STRING; 336983.ENSCANP00000016895; -.
DR   Ensembl; ENSCANT00000039836.1; ENSCANP00000016895.1; ENSCANG00000031868.1.
DR   OMA; HDEMKRM; -.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW.
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   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
//