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Dipeptidyl peptidase 1 (EC 3.4.14.1) (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (DPP-I) (DPPI) (Dipeptidyl transferase) [Cleaved into: Dipeptidyl peptidase 1 exclusion domain chain (Dipeptidyl peptidase I exclusion domain chain); Dipeptidyl peptidase 1 heavy chain (Dipeptidyl peptidase I heavy chain); Dipeptidyl peptidase 1 light chain (Dipeptidyl peptidase I light chain)]

 CATC_RAT                Reviewed;         462 AA.
P80067; P80068;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 3.
22-NOV-2017, entry version 154.
RecName: Full=Dipeptidyl peptidase 1;
EC=3.4.14.1;
AltName: Full=Cathepsin C;
AltName: Full=Cathepsin J;
AltName: Full=Dipeptidyl peptidase I;
Short=DPP-I;
Short=DPPI;
AltName: Full=Dipeptidyl transferase;
Contains:
RecName: Full=Dipeptidyl peptidase 1 exclusion domain chain;
AltName: Full=Dipeptidyl peptidase I exclusion domain chain;
Contains:
RecName: Full=Dipeptidyl peptidase 1 heavy chain;
AltName: Full=Dipeptidyl peptidase I heavy chain;
Contains:
RecName: Full=Dipeptidyl peptidase 1 light chain;
AltName: Full=Dipeptidyl peptidase I light chain;
Flags: Precursor;
Name=Ctsc;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1885565;
Ishidoh K., Muno D., Sato N., Kominami E.;
"Molecular cloning of cDNA for rat cathepsin C. Cathepsin C, a
cysteine proteinase with an extremely long propeptide.";
J. Biol. Chem. 266:16312-16317(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Kidney;
PubMed=1515062;
Kominami E., Ishidoh K., Muno D., Sato N.;
"The primary structure and tissue distribution of cathepsin C.";
Biol. Chem. Hoppe-Seyler 373:367-373(1992).
[3]
PROTEIN SEQUENCE OF 25-47; 230-251 AND 393-427.
TISSUE=Liver;
PubMed=1740150; DOI=10.1111/j.1432-1033.1992.tb16647.x;
Nikawa T., Towatari T., Katunuma N.;
"Purification and characterization of cathepsin J from rat liver.";
Eur. J. Biochem. 204:381-393(1992).
[4]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-462, SUBUNIT,
GLYCOSYLATION AT ASN-29 AND ASN-275, AND DISULFIDE BONDS.
PubMed=11602245; DOI=10.1016/S0014-5793(01)02911-8;
Olsen J.G., Kadziola A., Lauritzen C., Pedersen J., Larsen S.,
Dahl S.W.;
"Tetrameric dipeptidyl peptidase I directs substrate specificity by
use of the residual pro-part domain.";
FEBS Lett. 506:201-206(2001).
-!- FUNCTION: Thiol protease. Has dipeptidylpeptidase activity. Can
act as both an exopeptidase and endopeptidase (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide, Xaa-Yaa-|-
Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.
-!- COFACTOR:
Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
Note=Binds 1 Cl(-) ion per heavy chain. {ECO:0000250};
-!- SUBUNIT: Tetramer of heterotrimers consisting of exclusion domain,
heavy- and light chains. {ECO:0000269|PubMed:11602245}.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- TISSUE SPECIFICITY: Broadly distributed, but higher levels found
in liver, spleen, intestine, lung and kidney.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:11602245}.
-!- SIMILARITY: Belongs to the peptidase C1 family.
{ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000255|PROSITE-
ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
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EMBL; D90404; BAA14400.1; -; mRNA.
PIR; A41158; A41158.
RefSeq; NP_058793.1; NM_017097.1.
UniGene; Rn.203177; -.
PDB; 1JQP; X-ray; 2.40 A; A=25-462.
PDBsum; 1JQP; -.
ProteinModelPortal; P80067; -.
SMR; P80067; -.
STRING; 10116.ENSRNOP00000022342; -.
GuidetoPHARMACOLOGY; 2344; -.
MEROPS; C01.070; -.
iPTMnet; P80067; -.
PhosphoSitePlus; P80067; -.
PaxDb; P80067; -.
PRIDE; P80067; -.
Ensembl; ENSRNOT00000022342; ENSRNOP00000022342; ENSRNOG00000016496.
GeneID; 25423; -.
KEGG; rno:25423; -.
CTD; 1075; -.
RGD; 2445; Ctsc.
eggNOG; KOG1543; Eukaryota.
eggNOG; COG4870; LUCA.
GeneTree; ENSGT00900000140859; -.
HOGENOM; HOG000068022; -.
HOVERGEN; HBG005248; -.
InParanoid; P80067; -.
KO; K01275; -.
OMA; YHHTGLR; -.
OrthoDB; EOG091G06TT; -.
PhylomeDB; P80067; -.
TreeFam; TF313225; -.
Reactome; R-RNO-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-RNO-5694530; Cargo concentration in the ER.
Reactome; R-RNO-6798695; Neutrophil degranulation.
SABIO-RK; P80067; -.
EvolutionaryTrace; P80067; -.
PRO; PR:P80067; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000016496; -.
Genevisible; P80067; RN.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0005764; C:lysosome; IDA:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0051087; F:chaperone binding; IPI:ParkinsonsUK-UCL.
GO; GO:0031404; F:chloride ion binding; IDA:RGD.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0008234; F:cysteine-type peptidase activity; ISO:RGD.
GO; GO:0042802; F:identical protein binding; IDA:RGD.
GO; GO:0016505; F:peptidase activator activity involved in apoptotic process; ISO:RGD.
GO; GO:0019902; F:phosphatase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0043621; F:protein self-association; IDA:RGD.
GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
GO; GO:1903052; P:positive regulation of proteolysis involved in cellular protein catabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0006508; P:proteolysis; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IDA:RGD.
GO; GO:0001913; P:T cell mediated cytotoxicity; ISO:RGD.
Gene3D; 2.40.128.80; -; 1.
InterPro; IPR014882; CathepsinC_exc.
InterPro; IPR036496; CathepsinC_exc_dom_sf.
InterPro; IPR025661; Pept_asp_AS.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR025660; Pept_his_AS.
InterPro; IPR013128; Peptidase_C1A.
InterPro; IPR000668; Peptidase_C1A_C.
PANTHER; PTHR12411; PTHR12411; 1.
Pfam; PF08773; CathepsinC_exc; 1.
Pfam; PF00112; Peptidase_C1; 1.
PRINTS; PR00705; PAPAIN.
SMART; SM00645; Pept_C1; 1.
SUPFAM; SSF75001; SSF75001; 1.
PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
1: Evidence at protein level;
3D-structure; Chloride; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
Reference proteome; Signal; Thiol protease; Zymogen.
SIGNAL 1 24 {ECO:0000269|PubMed:1740150}.
CHAIN 25 134 Dipeptidyl peptidase 1 exclusion domain
chain. {ECO:0000250}.
/FTId=PRO_0000026350.
PROPEP 135 229 {ECO:0000250}.
/FTId=PRO_0000026351.
CHAIN 230 393 Dipeptidyl peptidase 1 heavy chain.
/FTId=PRO_0000026352.
CHAIN 394 462 Dipeptidyl peptidase 1 light chain.
/FTId=PRO_0000026353.
ACT_SITE 257 257 {ECO:0000250}.
ACT_SITE 404 404 {ECO:0000250}.
ACT_SITE 426 426 {ECO:0000250}.
BINDING 301 301 Chloride. {ECO:0000250}.
BINDING 303 303 Chloride; via amide nitrogen.
{ECO:0000250}.
BINDING 346 346 Chloride. {ECO:0000250}.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11602245}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11602245}.
DISULFID 30 118 {ECO:0000269|PubMed:11602245}.
DISULFID 54 136 {ECO:0000269|PubMed:11602245}.
DISULFID 254 297 {ECO:0000269|PubMed:11602245}.
DISULFID 290 330 {ECO:0000269|PubMed:11602245}.
DISULFID 320 336 {ECO:0000269|PubMed:11602245}.
CONFLICT 30 30 C -> E (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 129 129 V -> Y (in Ref. 2). {ECO:0000305}.
CONFLICT 171 171 N -> H (in Ref. 2). {ECO:0000305}.
CONFLICT 191 192 EE -> RR (in Ref. 2). {ECO:0000305}.
CONFLICT 263 263 L -> I (in Ref. 2). {ECO:0000305}.
HELIX 32 35 {ECO:0000244|PDB:1JQP}.
STRAND 36 43 {ECO:0000244|PDB:1JQP}.
STRAND 62 69 {ECO:0000244|PDB:1JQP}.
TURN 70 72 {ECO:0000244|PDB:1JQP}.
STRAND 73 75 {ECO:0000244|PDB:1JQP}.
STRAND 77 79 {ECO:0000244|PDB:1JQP}.
STRAND 81 87 {ECO:0000244|PDB:1JQP}.
TURN 88 90 {ECO:0000244|PDB:1JQP}.
STRAND 91 96 {ECO:0000244|PDB:1JQP}.
STRAND 99 110 {ECO:0000244|PDB:1JQP}.
STRAND 113 121 {ECO:0000244|PDB:1JQP}.
STRAND 123 128 {ECO:0000244|PDB:1JQP}.
STRAND 133 141 {ECO:0000244|PDB:1JQP}.
STRAND 253 255 {ECO:0000244|PDB:1JQP}.
HELIX 257 273 {ECO:0000244|PDB:1JQP}.
TURN 274 276 {ECO:0000244|PDB:1JQP}.
HELIX 284 290 {ECO:0000244|PDB:1JQP}.
HELIX 302 305 {ECO:0000244|PDB:1JQP}.
HELIX 308 312 {ECO:0000244|PDB:1JQP}.
STRAND 315 317 {ECO:0000244|PDB:1JQP}.
HELIX 318 320 {ECO:0000244|PDB:1JQP}.
STRAND 338 346 {ECO:0000244|PDB:1JQP}.
HELIX 356 366 {ECO:0000244|PDB:1JQP}.
STRAND 369 373 {ECO:0000244|PDB:1JQP}.
HELIX 377 380 {ECO:0000244|PDB:1JQP}.
STRAND 384 387 {ECO:0000244|PDB:1JQP}.
STRAND 404 413 {ECO:0000244|PDB:1JQP}.
TURN 415 417 {ECO:0000244|PDB:1JQP}.
STRAND 420 425 {ECO:0000244|PDB:1JQP}.
STRAND 437 441 {ECO:0000244|PDB:1JQP}.
HELIX 446 448 {ECO:0000244|PDB:1JQP}.
STRAND 454 459 {ECO:0000244|PDB:1JQP}.
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


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