ID A0A2K5IK61_COLAP Unreviewed; 555 AA.
AC A0A2K5IK61;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, 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:ENSCANP00000016916.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000016916.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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};
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DR AlphaFoldDB; A0A2K5IK61; -.
DR Ensembl; ENSCANT00000039857.1; ENSCANP00000016916.1; ENSCANG00000031868.1.
DR Proteomes; UP000233080; Unplaced.
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 Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
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}.
FT DOMAIN 191..555
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT ACT_SITE 467
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 509
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 510
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 533
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
FT BINDING 535
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01032"
SQ SEQUENCE 555 AA; 60562 MW; 6BE6DD3F966F7BAD CRC64;
MILPKVSAPN LEPSMTNIFH LHPNQSWVSL GRADPEEELS LTFALRQQNL ERLSELVQAV
SDPNSPQYGK YLTLENVADL VRPSPLTLHT VQKWLLAAGA QKCHSVITQD FLTCWLSIRQ
AELLLPGAQF HHYVGGPTET HVVRSPRPYQ LPQALAPHVD FVGGLHRFPP TSSLRQRPEP
QVTGTVGLHL GVTPSVIRKR YNLTSQDVGS GTSNNSQACA QFLEQYFHDS DLAQFMRLFG
GNFAHQASVT RVVGQQGRGR AGIEASLDVQ YLMSAGANIS TWVYSSPGRH EGQEPFLQWL
ILLSNESALP HVHTVSYGDE EDSLSSAYIQ RVNTELMKAA ARGLTLLFAS GDSGAGCWSV
SGRHQFRPTF PASSPYVTTV GGTSFQEPFL ITNEIVDYIS GGGFSNVFPR PSYQEEAVAK
FLSSSPHLPP SSYFNASGRA YPDVAALSDG YWVVSNRVPI PWVSGTSAST PVFGGLLSLI
NEHRILSGRP PLGFLNPRLY HQHGAGLFDV THGCHESCLD DEVEGQGFCS GPGWDPVTGW
GTPNFPALLK TLLNP
//
