CATC_PONAB
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-AUG-2022, entry version 75.
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. 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; 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 PRIDE; Q5RB02; -.
DR GeneID; 100172530; -.
DR KEGG; pon:100172530; -.
DR CTD; 1075; -.
DR eggNOG; KOG1543; Eukaryota.
DR InParanoid; Q5RB02; -.
DR OrthoDB; 1275401at2759; -.
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; -; 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; Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome;
KW 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_0000260307"
FT PROPEP 135..230
FT /evidence="ECO:0000250"
FT /id="PRO_0000260308"
FT CHAIN 231..394
FT /note="Dipeptidyl peptidase 1 heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260309"
FT CHAIN 395..463
FT /note="Dipeptidyl peptidase 1 light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260310"
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"
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
