ID   CATC_MACFA              Reviewed;         463 AA.
AC   Q60HG6;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Dipeptidyl peptidase 1;
DE            EC=3.4.14.1;
DE   AltName: Full=Cathepsin C;
DE   AltName: Full=Cathepsin J;
DE   AltName: Full=Dipeptidyl peptidase I;
DE            Short=DPP-I;
DE            Short=DPPI;
DE   AltName: Full=Dipeptidyl transferase;
DE   Contains:
DE     RecName: Full=Dipeptidyl peptidase 1 exclusion domain chain;
DE     AltName: Full=Dipeptidyl peptidase I exclusion domain chain;
DE   Contains:
DE     RecName: Full=Dipeptidyl peptidase 1 heavy chain;
DE     AltName: Full=Dipeptidyl peptidase I heavy chain;
DE   Contains:
DE     RecName: Full=Dipeptidyl peptidase 1 light chain;
DE     AltName: Full=Dipeptidyl peptidase I light chain;
DE   Flags: Precursor;
GN   Name=CTSC; ORFNames=QnpA-12394;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RA   Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Thiol protease. Has dipeptidylpeptidase activity. Active
CC       against a broad range of dipeptide substrates composed of both polar
CC       and hydrophobic amino acids. Proline cannot occupy the P1 position and
CC       arginine cannot occupy the P2 position of the substrate. Can act as
CC       both an exopeptidase and endopeptidase. Activates serine proteases such
CC       as elastase, cathepsin G and granzymes A and B.
CC       {ECO:0000250|UniProtKB:P53634}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except
CC         when Xaa is Arg or Lys, or Yaa or Zaa is Pro.; EC=3.4.14.1;
CC         Evidence={ECO:0000250|UniProtKB:P53634};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000250|UniProtKB:P53634};
CC       Note=Binds 1 Cl(-) ion per heavy chain. {ECO:0000250|UniProtKB:P53634};
CC   -!- SUBUNIT: Tetramer of heterotrimers consisting of exclusion domain,
CC       heavy- and light chains. {ECO:0000250|UniProtKB:P53634}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P53634}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC       ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; AB125161; BAD51949.1; -; mRNA.
DR   RefSeq; NP_001270292.1; NM_001283363.1.
DR   AlphaFoldDB; Q60HG6; -.
DR   SMR; Q60HG6; -.
DR   STRING; 9541.ENSMFAP00000017123; -.
DR   MEROPS; C01.070; -.
DR   GlyCosmos; Q60HG6; 4 sites, No reported glycans.
DR   eggNOG; KOG1543; Eukaryota.
DR   OrthoDB; 5475703at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02621; Peptidase_C1A_CathepsinC; 1.
DR   Gene3D; 2.40.128.80; Cathepsin C, exclusion domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR039412; CatC.
DR   InterPro; IPR014882; CathepsinC_exc.
DR   InterPro; IPR036496; CathepsinC_exc_dom_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR   PANTHER; PTHR12411:SF942; DIPEPTIDYL PEPTIDASE 1; 1.
DR   Pfam; PF08773; CathepsinC_exc; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF75001; Dipeptidyl peptidase I (cathepsin C), exclusion domain; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   2: Evidence at transcript level;
KW   Chloride; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
KW   Reference proteome; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   CHAIN           25..134
FT                   /note="Dipeptidyl peptidase 1 exclusion domain chain"
FT                   /id="PRO_0000026342"
FT   PROPEP          135..230
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT                   /id="PRO_0000026343"
FT   CHAIN           231..394
FT                   /note="Dipeptidyl peptidase 1 heavy chain"
FT                   /evidence="ECO:0000250, ECO:0000250|UniProtKB:P53634"
FT                   /id="PRO_0000026344"
FT   CHAIN           395..463
FT                   /note="Dipeptidyl peptidase 1 light chain"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT                   /id="PRO_0000026345"
FT   ACT_SITE        258
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        405
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        427
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   BINDING         302
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   BINDING         304
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   BINDING         347
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..118
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   DISULFID        54..136
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   DISULFID        255..298
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   DISULFID        291..331
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   DISULFID        321..337
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
SQ   SEQUENCE   463 AA;  51866 MW;  3C66F6C23F8160B4 CRC64;
     MGVGPASLLA ALLLLLSGDR AVRCDTPANC TYLDLLGTWV FQVGSSGSLR DVNCSVMGPP
     EKKVVVHLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK WFAFFKYKEE GIKVTIYCNE
     TMTGWVHDVL GRNWACFTGK KVGTASENVY VNTAHLKNSQ EKYSNRLYKY DHNFVKAINA
     IQKSWTATTY MEYETLTLGD MIKRSGGHSR KIPRPKPTPL TAEIQQKILH LPTSWDWRNV
     HGINFVSPVR NQASCGSCYS FASVGMLEAR IRILTNNSQT PILSSQEVVS CSQYAQGCEG
     GFPYLTAGKY AQDFGLVEEA CFPYTGTDSP CKMKEDCFRY YSSEYHYVGG FYGGCNEALM
     KLELVYHGPL AVAFEVYDDF LHYQNGIYHH TGLRDPFNPF ELTNHAVLLV GYGTDSASGM
     DYWIVKNSWG TSWGEDGYFR IRRGTDECAI ESIAVAATPI PKL
//