CATC_MOUSE
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 03-AUG-2022, entry version 176.
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].
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. Can act as
CC both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a
CC role in the generation of cytotoxic lymphocyte effector function.
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.
CC -!- TISSUE SPECIFICITY: Broadly distributed, but higher levels found in
CC lung, liver, kidney and spleen. Lower levels found in testis and brain.
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_009982.5.
DR AlphaFoldDB; P97821; -.
DR SMR; P97821; -.
DR BioGRID; 198969; 3.
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 GlyGen; P97821; 3 sites.
DR iPTMnet; P97821; -.
DR PhosphoSitePlus; P97821; -.
DR SwissPalm; P97821; -.
DR EPD; P97821; -.
DR jPOST; P97821; -.
DR PaxDb; P97821; -.
DR PeptideAtlas; P97821; -.
DR PRIDE; P97821; -.
DR ProteomicsDB; 265550; -.
DR Antibodypedia; 31473; 289 antibodies from 31 providers.
DR DNASU; 13032; -.
DR Ensembl; ENSMUST00000032779; ENSMUSP00000032779; ENSMUSG00000030560.
DR GeneID; 13032; -.
DR KEGG; mmu:13032; -.
DR UCSC; uc009ifu.2; mouse.
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; HDKTVNC; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; P97821; -.
DR TreeFam; TF313225; -.
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 74 CRISPR screens.
DR ChiTaRS; Ctsc; mouse.
DR PRO; PR:P97821; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P97821; protein.
DR Bgee; ENSMUSG00000030560; Expressed in left lung lobe and 238 other tissues.
DR ExpressionAtlas; P97821; baseline and differential.
DR Genevisible; P97821; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0031404; F:chloride ion binding; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:MGI.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; IGI:MGI.
DR GO; GO:0019902; F:phosphatase binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
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:1903052; P:positive regulation of proteolysis involved in protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IGI: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 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:0000255"
FT CHAIN 25..134
FT /note="Dipeptidyl peptidase 1 exclusion domain chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026346"
FT PROPEP 135..230
FT /evidence="ECO:0000250"
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:0000250"
FT ACT_SITE 404
FT /evidence="ECO:0000250"
FT ACT_SITE 426
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 303
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 346
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 275
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 254..297
FT /evidence="ECO:0000250"
FT DISULFID 290..330
FT /evidence="ECO:0000250"
FT DISULFID 320..336
FT /evidence="ECO:0000250"
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
