ID   CATC_MOUSE              Reviewed;         462 AA.
AC   P97821; O08853;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   02-SEP-2026, entry version 193.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=9099719; DOI=10.1074/jbc.272.16.10695;
RA   Pham C.T.N., Armstrong R.J., Zimonjic D.B., Popescu N.C., Payan D.G.,
RA   Ley T.J.;
RT   "Molecular cloning, chromosomal localization, and expression of murine
RT   dipeptidyl peptidase I.";
RL   J. Biol. Chem. 272:10695-10703(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=9130590; DOI=10.1016/s0167-4781(97)00021-3;
RA   McGuire M.J., Lipsky P.E., Thiele D.L.;
RT   "Cloning and characterization of the cDNA encoding mouse dipeptidyl
RT   peptidase I (cathepsin C).";
RL   Biochim. Biophys. Acta 1351:267-273(1997).
RN   [3]
RP   SEQUENCE REVISION.
RA   McGuire M.J., Lipsky P.E., Francisco N.M.C., Thiele D.L.;
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- TISSUE SPECIFICITY: Broadly distributed, but higher levels found in
CC       lung, liver, kidney and spleen. Lower levels found in testis and brain.
CC       {ECO:0000269|PubMed:9099719}.
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; U89269; AAB49457.1; -; mRNA.
DR   EMBL; U74683; AAB58400.3; -; mRNA.
DR   EMBL; BC067063; AAH67063.1; -; mRNA.
DR   CCDS; CCDS21438.1; -.
DR   RefSeq; NP_034112.3; NM_009982.6.
DR   AlphaFoldDB; P97821; -.
DR   SMR; P97821; -.
DR   BioGRID; 198969; 3.
DR   FunCoup; P97821; 1023.
DR   IntAct; P97821; 1.
DR   MINT; P97821; -.
DR   STRING; 10090.ENSMUSP00000032779; -.
DR   BindingDB; P97821; -.
DR   ChEMBL; CHEMBL3454; -.
DR   GuidetoPHARMACOLOGY; 2344; -.
DR   MEROPS; C01.070; -.
DR   GlyCosmos; P97821; 3 sites, No reported glycans.
DR   GlyGen; P97821; 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P97821; -.
DR   PhosphoSitePlus; P97821; -.
DR   SwissPalm; P97821; -.
DR   jPOST; P97821; -.
DR   PaxDb; 10090-ENSMUSP00000032779; -.
DR   PeptideAtlas; P97821; -.
DR   ProteomicsDB; 265550; -.
DR   Antibodypedia; 31473; 287 antibodies from 32 providers.
DR   DNASU; 13032; -.
DR   Ensembl; ENSMUST00000032779.12; ENSMUSP00000032779.6; ENSMUSG00000030560.18.
DR   GeneID; 13032; -.
DR   KEGG; mmu:13032; -.
DR   UCSC; uc009ifu.2; mouse.
DR   AGR; MGI:109553; -.
DR   CTD; 1075; -.
DR   MGI; MGI:109553; Ctsc.
DR   VEuPathDB; HostDB:ENSMUSG00000030560; -.
DR   eggNOG; KOG1543; Eukaryota.
DR   GeneTree; ENSGT00940000155787; -.
DR   HOGENOM; CLU_048219_0_0_1; -.
DR   InParanoid; P97821; -.
DR   OMA; NAVQKSW; -.
DR   OrthoDB; 3789175at2759; -.
DR   PhylomeDB; P97821; -.
DR   BRENDA; 3.4.14.1; 3474.
DR   Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 13032; 2 hits in 79 CRISPR screens.
DR   PRO; PR:P97821; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P97821; protein.
DR   Bgee; ENSMUSG00000030560; Expressed in left lung lobe and 242 other cell types or tissues.
DR   ExpressionAtlas; P97821; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISO:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0031404; F:chloride ion binding; ISO:GO_Central.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IDA:MGI.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:GO_Central.
DR   GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; IGI:MGI.
DR   GO; GO:0019902; F:phosphatase binding; ISO:GO_Central.
DR   GO; GO:0051087; F:protein-folding chaperone binding; ISO:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0031642; P:negative regulation of myelination; IDA:MGI.
DR   GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IGI:MGI.
DR   GO; GO:1903980; P:positive regulation of microglial cell activation; IDA:MGI.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR   GO; GO:0001913; P:T cell mediated cytotoxicity; IGI:UniProtKB.
DR   CDD; cd02621; Peptidase_C1A_CathepsinC; 1.
DR   FunFam; 2.40.128.80:FF:000001; Dipeptidyl peptidase 1; 1.
DR   FunFam; 3.90.70.10:FF:000062; Dipeptidyl peptidase 1; 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   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   1: Evidence at protein 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                   /evidence="ECO:0000250|UniProtKB:P53634"
FT                   /id="PRO_0000026346"
FT   PROPEP          135..230
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT                   /id="PRO_0000026347"
FT   CHAIN           231..393
FT                   /note="Dipeptidyl peptidase 1 heavy chain"
FT                   /id="PRO_0000026348"
FT   CHAIN           394..462
FT                   /note="Dipeptidyl peptidase 1 light chain"
FT                   /id="PRO_0000026349"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10088"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT   BINDING         301
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   BINDING         303
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   BINDING         346
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        275
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        254..297
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   DISULFID        290..330
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
FT   DISULFID        320..336
FT                   /evidence="ECO:0000250|UniProtKB:P53634"
SQ   SEQUENCE   462 AA;  52376 MW;  56574B38D7DF4710 CRC64;
     MGPWTHSLRA VLLLVLLGVC TVRSDTPANC TYPDLLGTWV FQVGPRSSRS DINCSVMEAT
     EEKVVVHLKK LDTAYDELGN SGHFTLIYNQ GFEIVLNDYK WFAFFKYEVR GHTAISYCHE
     TMTGWVHDVL GRNWACFVGK KVESHIEKVN MNAAHLGGLQ ERYSERLYTH NHNFVKAINT
     VQKSWTATAY KEYEKMSLRD LIRRSGHSQR IPRPKPAPMT DEIQQQILNL PESWDWRNVQ
     GVNYVSPVRN QESCGSCYSF ASMGMLEARI RILTNNSQTP ILSPQEVVSC SPYAQGCDGG
     FPYLIAGKYA QDFGVVEESC FPYTAKDSPC KPRENCLRYY SSDYYYVGGF YGGCNEALMK
     LELVKHGPMA VAFEVHDDFL HYHSGIYHHT GLSDPFNPFE LTNHAVLLVG YGRDPVTGIE
     YWIIKNSWGS NWGESGYFRI RRGTDECAIE SIAVAAIPIP KL
//