CATC_RAT
ID CATC_RAT Reviewed; 462 AA.
AC P80067; P80068;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 177.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1885565; DOI=10.1016/s0021-9258(18)55298-4;
RA Ishidoh K., Muno D., Sato N., Kominami E.;
RT "Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a cysteine
RT proteinase with an extremely long propeptide.";
RL J. Biol. Chem. 266:16312-16317(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=1515062; DOI=10.1515/bchm3.1992.373.2.367;
RA Kominami E., Ishidoh K., Muno D., Sato N.;
RT "The primary structure and tissue distribution of cathepsin C.";
RL Biol. Chem. Hoppe-Seyler 373:367-373(1992).
RN [3]
RP PROTEIN SEQUENCE OF 25-47; 230-251 AND 393-427.
RC TISSUE=Liver;
RX PubMed=1740150; DOI=10.1111/j.1432-1033.1992.tb16647.x;
RA Nikawa T., Towatari T., Katunuma N.;
RT "Purification and characterization of cathepsin J from rat liver.";
RL Eur. J. Biochem. 204:381-393(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-462, SUBUNIT, GLYCOSYLATION AT
RP ASN-29 AND ASN-275, AND DISULFIDE BONDS.
RX PubMed=11602245; DOI=10.1016/s0014-5793(01)02911-8;
RA Olsen J.G., Kadziola A., Lauritzen C., Pedersen J., Larsen S., Dahl S.W.;
RT "Tetrameric dipeptidyl peptidase I directs substrate specificity by use of
RT the residual pro-part domain.";
RL FEBS Lett. 506:201-206(2001).
CC -!- FUNCTION: Thiol protease. Has dipeptidylpeptidase activity. Can act as
CC both an exopeptidase and endopeptidase (By 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:0000269|PubMed:11602245}.
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- TISSUE SPECIFICITY: Broadly distributed, but higher levels found in
CC liver, spleen, intestine, lung and kidney.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11602245}.
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; D90404; BAA14400.1; -; mRNA.
DR PIR; A41158; A41158.
DR RefSeq; NP_058793.1; NM_017097.1.
DR PDB; 1JQP; X-ray; 2.40 A; A=25-462.
DR PDBsum; 1JQP; -.
DR AlphaFoldDB; P80067; -.
DR SMR; P80067; -.
DR STRING; 10116.ENSRNOP00000022342; -.
DR BindingDB; P80067; -.
DR ChEMBL; CHEMBL3308944; -.
DR GuidetoPHARMACOLOGY; 2344; -.
DR MEROPS; C01.070; -.
DR GlyGen; P80067; 4 sites.
DR iPTMnet; P80067; -.
DR PhosphoSitePlus; P80067; -.
DR PaxDb; P80067; -.
DR PRIDE; P80067; -.
DR Ensembl; ENSRNOT00000022342; ENSRNOP00000022342; ENSRNOG00000016496.
DR GeneID; 25423; -.
DR KEGG; rno:25423; -.
DR CTD; 1075; -.
DR RGD; 2445; Ctsc.
DR eggNOG; KOG1543; Eukaryota.
DR GeneTree; ENSGT00940000155787; -.
DR HOGENOM; CLU_048219_0_0_1; -.
DR InParanoid; P80067; -.
DR OMA; HDKTVNC; -.
DR OrthoDB; 1275401at2759; -.
DR PhylomeDB; P80067; -.
DR TreeFam; TF313225; -.
DR BRENDA; 3.4.14.1; 5301.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-5694530; Cargo concentration in the ER.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR SABIO-RK; P80067; -.
DR EvolutionaryTrace; P80067; -.
DR PRO; PR:P80067; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000016496; Expressed in liver and 19 other tissues.
DR Genevisible; P80067; RN.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0051087; F:chaperone binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0031404; F:chloride ion binding; IDA:RGD.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISO:RGD.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0019902; F:phosphatase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0043621; F:protein self-association; IDA:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0031642; P:negative regulation of myelination; ISO:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1903980; P:positive regulation of microglial cell activation; ISO:RGD.
DR GO; GO:1903052; P:positive regulation of proteolysis involved in protein catabolic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0010033; P:response to organic substance; IDA:RGD.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; ISO:RGD.
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 3D-structure; Chloride; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:1740150"
FT CHAIN 25..134
FT /note="Dipeptidyl peptidase 1 exclusion domain chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026350"
FT PROPEP 135..229
FT /evidence="ECO:0000250"
FT /id="PRO_0000026351"
FT CHAIN 230..393
FT /note="Dipeptidyl peptidase 1 heavy chain"
FT /id="PRO_0000026352"
FT CHAIN 394..462
FT /note="Dipeptidyl peptidase 1 light chain"
FT /id="PRO_0000026353"
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:0000269|PubMed:11602245"
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 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11602245"
FT DISULFID 30..118
FT /evidence="ECO:0000269|PubMed:11602245"
FT DISULFID 54..136
FT /evidence="ECO:0000269|PubMed:11602245"
FT DISULFID 254..297
FT /evidence="ECO:0000269|PubMed:11602245"
FT DISULFID 290..330
FT /evidence="ECO:0000269|PubMed:11602245"
FT DISULFID 320..336
FT /evidence="ECO:0000269|PubMed:11602245"
FT CONFLICT 30
FT /note="C -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="V -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="N -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 191..192
FT /note="EE -> RR (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="L -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1JQP"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1JQP"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 99..110
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1JQP"
FT HELIX 257..273
FT /evidence="ECO:0007829|PDB:1JQP"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1JQP"
FT HELIX 284..290
FT /evidence="ECO:0007829|PDB:1JQP"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:1JQP"
FT HELIX 308..312
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:1JQP"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:1JQP"
FT HELIX 356..366
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:1JQP"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 404..413
FT /evidence="ECO:0007829|PDB:1JQP"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:1JQP"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:1JQP"
FT STRAND 454..459
FT /evidence="ECO:0007829|PDB:1JQP"
SQ SEQUENCE 462 AA; 52235 MW; F25F3953AA115D3C CRC64;
MGPWTHSLRA ALLLVLLGVC TVSSDTPANC TYPDLLGTWV FQVGPRHPRS HINCSVMEPT
EEKVVIHLKK LDTAYDEVGN SGYFTLIYNQ GFEIVLNDYK WFAFFKYEVK GSRAISYCHE
TMTGWVHDVL GRNWACFVGK KMANHSEKVY VNVAHLGGLQ EKYSERLYSH NHNFVKAINS
VQKSWTATTY EEYEKLSIRD LIRRSGHSGR ILRPKPAPIT DEIQQQILSL PESWDWRNVR
GINFVSPVRN QESCGSCYSF ASLGMLEARI RILTNNSQTP ILSPQEVVSC SPYAQGCDGG
FPYLIAGKYA QDFGVVEENC FPYTATDAPC KPKENCLRYY SSEYYYVGGF YGGCNEALMK
LELVKHGPMA VAFEVHDDFL HYHSGIYHHT GLSDPFNPFE LTNHAVLLVG YGKDPVTGLD
YWIVKNSWGS QWGESGYFRI RRGTDECAIE SIAMAAIPIP KL
