ID   Q3UBY5_MOUSE            Unreviewed;       462 AA.
AC   Q3UBY5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 148.
DE   RecName: Full=Dipeptidyl peptidase 1 {ECO:0000256|ARBA:ARBA00014709};
DE            EC=3.4.14.1 {ECO:0000256|ARBA:ARBA00012059};
DE   AltName: Full=Cathepsin C {ECO:0000256|ARBA:ARBA00029779};
DE   AltName: Full=Cathepsin J {ECO:0000256|ARBA:ARBA00029762};
DE   AltName: Full=Dipeptidyl peptidase I {ECO:0000256|ARBA:ARBA00032961};
DE   AltName: Full=Dipeptidyl transferase {ECO:0000256|ARBA:ARBA00030778};
GN   Name=Ctsc {ECO:0000313|MGI:MGI:109553};
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 {ECO:0000313|EMBL:BAE29829.1};
RN   [1] {ECO:0000313|EMBL:BAE29829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29829.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27487.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29829.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE29829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29829.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27487.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29829.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE29829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29829.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27487.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29829.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE29829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29829.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27487.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29829.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE29829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29829.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27487.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29829.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:BAE29829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29829.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27487.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29829.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:BAE29829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29829.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27487.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29829.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAE29829.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE29829.1};
RC   TISSUE=Amnion {ECO:0000313|EMBL:BAE27487.1}, and Bone marrow
RC   {ECO:0000313|EMBL:BAE29829.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [9] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   -!- 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:0000256|ARBA:ARBA00000738};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|ARBA:ARBA00001923};
CC   -!- SUBUNIT: Tetramer of heterotrimers consisting of exclusion domain,
CC       heavy- and light chains. {ECO:0000256|ARBA:ARBA00011610}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000256|ARBA:ARBA00008455}.
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DR   EMBL; AK146858; BAE27487.1; -; mRNA.
DR   EMBL; AK150761; BAE29829.1; -; mRNA.
DR   RefSeq; NP_001298719.1; NM_001311790.1.
DR   RefSeq; NP_034112.3; NM_009982.5.
DR   AlphaFoldDB; Q3UBY5; -.
DR   SMR; Q3UBY5; -.
DR   MEROPS; C01.070; -.
DR   MaxQB; Q3UBY5; -.
DR   Antibodypedia; 31473; 317 antibodies from 31 providers.
DR   DNASU; 13032; -.
DR   GeneID; 13032; -.
DR   KEGG; mmu:13032; -.
DR   AGR; MGI:109553; -.
DR   CTD; 1075; -.
DR   MGI; MGI:109553; Ctsc.
DR   VEuPathDB; HostDB:ENSMUSG00000030560; -.
DR   HOGENOM; CLU_048219_0_0_1; -.
DR   OMA; HWDWRNV; -.
DR   OrthoDB; 5475703at2759; -.
DR   BioGRID-ORCS; 13032; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Ctsc; mouse.
DR   ExpressionAtlas; Q3UBY5; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0031404; F:chloride ion binding; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
DR   GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR   GO; GO:1903052; P:positive regulation of proteolysis involved in protein catabolic process; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR   CDD; cd02621; Peptidase_C1A_CathepsinC; 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   PANTHER; PTHR12411:SF942; DIPEPTIDYL PEPTIDASE 1; 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 {ECO:0000256|ARBA:ARBA00023214};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..462
FT                   /note="Dipeptidyl peptidase 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014205830"
FT   DOMAIN          230..457
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
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
//