ID   CATC_CANLF              Reviewed;         435 AA.
AC   O97578;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 129.
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 1;
DE     AltName: Full=Dipeptidyl peptidase I heavy chain 1;
DE   Contains:
DE     RecName: Full=Dipeptidyl peptidase 1 heavy chain 2;
DE     AltName: Full=Dipeptidyl peptidase I heavy chain 2;
DE   Contains:
DE     RecName: Full=Dipeptidyl peptidase 1 heavy chain 3;
DE     AltName: Full=Dipeptidyl peptidase I heavy chain 3;
DE   Contains:
DE     RecName: Full=Dipeptidyl peptidase 1 heavy chain 4;
DE     AltName: Full=Dipeptidyl peptidase I heavy chain 4;
DE   Contains:
DE     RecName: Full=Dipeptidyl peptidase 1 light chain;
DE     AltName: Full=Dipeptidyl peptidase I light chain;
DE   Flags: Precursor; Fragment;
GN   Name=CTSC;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-8 AND 199-208.
RC   TISSUE=Mast cell;
RX   PubMed=9624139; DOI=10.1074/jbc.273.25.15514;
RA   Wolters P.J., Raymond W.W., Blount J.L., Caughey G.H.;
RT   "Regulated expression, processing, and secretion of dog mast cell
RT   dipeptidyl peptidase I.";
RL   J. Biol. Chem. 273:15514-15520(1998).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5. Active over a broad pH range.;
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   -!- PTM: The N-terminus of the heavy chain is heterogeneously processed to
CC       produce four different chains.
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; AF060171; AAD02704.1; -; mRNA.
DR   RefSeq; NP_001182763.1; NM_001195834.1.
DR   AlphaFoldDB; O97578; -.
DR   SMR; O97578; -.
DR   STRING; 9615.ENSCAFP00000006531; -.
DR   BindingDB; O97578; -.
DR   ChEMBL; CHEMBL3879833; -.
DR   MEROPS; C01.070; -.
DR   GlyCosmos; O97578; 4 sites, No reported glycans.
DR   PaxDb; 9612-ENSCAFP00000037626; -.
DR   GeneID; 403458; -.
DR   KEGG; cfa:403458; -.
DR   CTD; 1075; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   InParanoid; O97578; -.
DR   OrthoDB; 5475703at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Chloride; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Lysosome; Protease; Reference proteome; Thiol protease; Zymogen.
FT   CHAIN           1..109
FT                   /note="Dipeptidyl peptidase 1 exclusion domain chain"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT                   /id="PRO_0000026331"
FT   PROPEP          110..199
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT                   /id="PRO_0000026332"
FT   CHAIN           200..366
FT                   /note="Dipeptidyl peptidase 1 heavy chain 1"
FT                   /id="PRO_0000026333"
FT   CHAIN           201..366
FT                   /note="Dipeptidyl peptidase 1 heavy chain 2"
FT                   /id="PRO_0000026334"
FT   CHAIN           203..366
FT                   /note="Dipeptidyl peptidase 1 heavy chain 3"
FT                   /id="PRO_0000026335"
FT   CHAIN           204..366
FT                   /note="Dipeptidyl peptidase 1 heavy chain 4"
FT                   /id="PRO_0000026336"
FT   CHAIN           367..435
FT                   /note="Dipeptidyl peptidase 1 light chain"
FT                   /id="PRO_0000026337"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        377
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        399
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   BINDING         275
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   BINDING         277
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   BINDING         319
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        6..93
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   DISULFID        29..111
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   DISULFID        228..271
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   DISULFID        264..304
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   DISULFID        294..309
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   NON_TER         1
SQ   SEQUENCE   435 AA;  49412 MW;  A80BC7C68CAB0727 CRC64;
     DTPANCTHPE LLGTWVFQVG PAGSRSVNCS VMGPPEKKVV VHLEKLDTAY DNFGNTGHFT
     IIYNQGFEIV LNDYKWFAFF KYKEEGHKVT SYCNETMTGW VHDVLGRNWA CFTGTKMGTT
     SEKAKVNTKH IERLQENNSN RLYKYNYEFV KAINTIQKSW TATRYIEYET LTLRDMMTRV
     GGRKIPRPKP TPLTAEIHEE ISRLPTSWDW RNVRGTNFVS PVRNQASCGS CYAFASTAML
     EARIRILTNN TQTPILSPQE IVSCSQYAQG CEGGFPYLIA GKYAQDFGLV EEACFPYAGS
     DSPCKPNDCF RYYSSEYYYV GGFYGACNEA LMKLELVRHG PMAVAFEVYD DFFHYQKGIY
     YHTGLRDPFN PFELTNHAVL LVGYGTDSAS GMDYWIVKNS WGSRWGEDGY FRIRRGTDEC
     AIESIAVAAT PIPKL
//