CATC_BOVIN
ID CATC_BOVIN Reviewed; 463 AA.
AC Q3ZCJ8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiol protease. Has dipeptidylpeptidase activity. Can act as
CC both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a
CC role in the generation of cytotoxic lymphocyte effector function (By
CC 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 -!- SUBUNIT: Tetramer of heterotrimers consisting of exclusion domain,
CC heavy- and light chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
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; BC102115; AAI02116.1; -; mRNA.
DR RefSeq; NP_001028789.1; NM_001033617.2.
DR AlphaFoldDB; Q3ZCJ8; -.
DR SMR; Q3ZCJ8; -.
DR STRING; 9913.ENSBTAP00000014735; -.
DR BindingDB; Q3ZCJ8; -.
DR ChEMBL; CHEMBL1075050; -.
DR MEROPS; C01.070; -.
DR PaxDb; Q3ZCJ8; -.
DR PeptideAtlas; Q3ZCJ8; -.
DR PRIDE; Q3ZCJ8; -.
DR GeneID; 352958; -.
DR KEGG; bta:352958; -.
DR CTD; 1075; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; Q3ZCJ8; -.
DR OrthoDB; 1275401at2759; -.
DR BRENDA; 3.4.14.1; 908.
DR PRO; PR:Q3ZCJ8; -.
DR Proteomes; UP000009136; 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:0031638; P:zymogen activation; IDA:UniProtKB.
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 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"
FT CHAIN 25..134
FT /note="Dipeptidyl peptidase 1 exclusion domain chain"
FT /id="PRO_0000238121"
FT PROPEP 135..230
FT /evidence="ECO:0000250"
FT /id="PRO_0000238122"
FT CHAIN 231..394
FT /note="Dipeptidyl peptidase 1 heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000238123"
FT CHAIN 395..463
FT /note="Dipeptidyl peptidase 1 light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000238124"
FT ACT_SITE 258
FT /evidence="ECO:0000250"
FT ACT_SITE 405
FT /evidence="ECO:0000250"
FT ACT_SITE 427
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
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 144
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"
FT DISULFID 54..136
FT /evidence="ECO:0000250"
FT DISULFID 255..298
FT /evidence="ECO:0000250"
FT DISULFID 291..331
FT /evidence="ECO:0000250"
FT DISULFID 321..337
FT /evidence="ECO:0000250"
SQ SEQUENCE 463 AA; 51949 MW; 5602557E041FB29C CRC64;
MGPWSGSRLV ALLLLVYGAG SVRGDTPANC TYPDLLGTWV FQVGSSGSQR DVNCSVMGPP
EKKVVVHLKK LDTAYDDFGN SGHFTIIYNQ GFEIVLNDYK WFAFFKYKEE GGKVTSYCHE
TMTGWVHDVL GRNRACFTGR KTGNTSENVN VNTARLAGLE ETYSNRLYRY NHDFVKAINA
IQKSWTAAPY MEYETLTLKE MIRRGGGHSR RIPRPKPAPI TAEIQKKILH LPTSWDWRNV
HGINFVTPVR NQGSCGSCYS FASMGMMEAR IRILTNNTQT PILSPQEVVS CSQYAQGCEG
GFPYLIAGKY AQDFGLVEED CFPYTGTDSP CRLKEGCFRY YSSEYHYVGG FYGGCNEALM
KLELVHQGPM AVAFEVYDDF LHYRKGVYHH TGLRDPFNPF ELTNHAVLLV GYGTDAASGL
DYWIVKNSWG TSWGENGYFR IRRGTDECAI ESIALAATPI PKL
