ID   CATC_PONAB              Reviewed;         463 AA.
AC   Q5RB02;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-MAY-2023, entry version 79.
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;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR858858; CAH91058.1; -; mRNA.
DR   RefSeq; NP_001125612.1; NM_001132140.1.
DR   AlphaFoldDB; Q5RB02; -.
DR   SMR; Q5RB02; -.
DR   STRING; 9601.ENSPPYP00000004292; -.
DR   MEROPS; C01.070; -.
DR   GlyCosmos; Q5RB02; 3 sites, No reported glycans.
DR   GeneID; 100172530; -.
DR   KEGG; pon:100172530; -.
DR   CTD; 1075; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   InParanoid; Q5RB02; -.
DR   OrthoDB; 5475703at2759; -.
DR   Proteomes; UP000001595; 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_0000260307"
FT   PROPEP          135..230
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT                   /id="PRO_0000260308"
FT   CHAIN           231..394
FT                   /note="Dipeptidyl peptidase 1 heavy chain"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT                   /id="PRO_0000260309"
FT   CHAIN           395..463
FT                   /note="Dipeptidyl peptidase 1 light chain"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT                   /id="PRO_0000260310"
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   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;  51870 MW;  EAB7D3A7CF82C09E CRC64;
     MGPGPASLLA ALLLLLSGDR AVRCDTPANC TYLDLLGTWV FQVGSSGSQR DVNCSVMGPQ
     EKKVVVHLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK WFAFFKYKEE GSKVTTYCNE
     TMTGWVHDVL GRNWACFTGK KVGTASENVY VNTAHLKNSQ EKYSNRLYKY DHNFVKAINA
     IQKSWTATTY KEYETLTLGD MIRRSGGHSR KIPRPKPAPL TAEIQQKVLH LPTSWDWRNI
     HGINFVSPVR NQASCGSCYS FASMGMLEAR IRILTSNSQT PILSPQEVVS CSQYAQGCEG
     GFPYLIAGKY AQDFGLVEEA CFPYTGTDSP CKMKEDCFRY YSSEYHYVGG FYGGCNEALM
     KLELVHHGPM AVAFEVYDDF LHYKKGIYHH TGLRDPFNPF ELTNHAVLLV GYGTDSASGM
     DYWIVKNSWG TGWGEDGYFR IRRGTDECAI ESIAVAATPI PKL
//