CATC_CANLF
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 03-AUG-2022, entry version 121.
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. Can act as
CC both an exopeptidase and endopeptidase (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
CC Note=Binds 1 Cl(-) ion per heavy chain. {ECO:0000250};
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}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
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; 9612.ENSCAFP00000037626; -.
DR BindingDB; O97578; -.
DR ChEMBL; CHEMBL3879833; -.
DR MEROPS; C01.070; -.
DR PaxDb; O97578; -.
DR PRIDE; O97578; -.
DR GeneID; 403458; -.
DR KEGG; cfa:403458; -.
DR CTD; 1075; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; O97578; -.
DR OrthoDB; 1275401at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
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; -; 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; IPR000668; Peptidase_C1A_C.
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; SSF54001; 1.
DR SUPFAM; SSF75001; SSF75001; 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"
FT /id="PRO_0000026331"
FT PROPEP 110..199
FT /evidence="ECO:0000250"
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:0000250"
FT ACT_SITE 377
FT /evidence="ECO:0000250"
FT ACT_SITE 399
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 6..93
FT /evidence="ECO:0000250"
FT DISULFID 29..111
FT /evidence="ECO:0000250"
FT DISULFID 228..271
FT /evidence="ECO:0000250"
FT DISULFID 264..304
FT /evidence="ECO:0000250"
FT DISULFID 294..309
FT /evidence="ECO:0000250"
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
