ID   A0A2K5IJW4_COLAP        Unreviewed;       563 AA.
AC   A0A2K5IJW4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   07-APR-2021, entry version 18.
DE   RecName: Full=Tripeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00020562};
DE            EC=3.4.14.9 {ECO:0000256|ARBA:ARBA00012067};
DE   AltName: Full=Tripeptidyl-peptidase 1 {ECO:0000256|ARBA:ARBA00020254};
DE   AltName: Full=Tripeptidyl-peptidase I {ECO:0000256|ARBA:ARBA00020236};
GN   Name=TPP1 {ECO:0000313|Ensembl:ENSCANP00000016895};
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};
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DR   Ensembl; ENSCANT00000039836; ENSCANP00000016895; ENSCANG00000031868.
DR   GeneTree; ENSGT00390000008684; -.
DR   OMA; GCRHLGK; -.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
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 aminopeptidase"
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
//