CATC_MACFA
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 03-AUG-2022, entry version 71.
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. 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; AB125161; BAD51949.1; -; mRNA.
DR RefSeq; NP_001270292.1; NM_001283363.1.
DR AlphaFoldDB; Q60HG6; -.
DR SMR; Q60HG6; -.
DR STRING; 9541.XP_005579363.1; -.
DR MEROPS; C01.070; -.
DR GeneID; 102137896; -.
DR CTD; 1075; -.
DR eggNOG; KOG1543; Eukaryota.
DR OrthoDB; 1275401at2759; -.
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; -; 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_0000026342"
FT PROPEP 135..230
FT /evidence="ECO:0000250"
FT /id="PRO_0000026343"
FT CHAIN 231..394
FT /note="Dipeptidyl peptidase 1 heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026344"
FT CHAIN 395..463
FT /note="Dipeptidyl peptidase 1 light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026345"
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 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"
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; 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
