ID   Q3U9B7_MOUSE            Unreviewed;       447 AA.
AC   Q3U9B7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   28-JUN-2023, entry version 99.
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};
DE   Flags: Fragment;
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:BAE30750.1};
RN   [1] {ECO:0000313|EMBL:BAE30750.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30750.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30750.1};
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:BAE30750.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30750.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30750.1};
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:BAE30750.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30750.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30750.1};
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:BAE30750.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30750.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30750.1};
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:BAE30750.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30750.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30750.1};
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:BAE30750.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30750.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30750.1};
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:BAE30750.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30750.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30750.1};
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:BAE30750.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE30750.1};
RC   TISSUE=Bone marrow {ECO:0000313|EMBL:BAE30750.1};
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).
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; AK151861; BAE30750.1; -; mRNA.
DR   AlphaFoldDB; Q3U9B7; -.
DR   MEROPS; C01.070; -.
DR   EPD; Q3U9B7; -.
DR   PeptideAtlas; Q3U9B7; -.
DR   AGR; MGI:109553; -.
DR   MGI; MGI:109553; Ctsc.
DR   ChiTaRS; Ctsc; mouse.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   2: Evidence at transcript 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};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT   DOMAIN          215..442
FT                   /note="Peptidase C1A papain C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00645"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAE30750.1"
SQ   SEQUENCE   447 AA;  50701 MW;  ED40A52293C3EFED CRC64;
     LLGVCTVRSD TPANCTYPDL LGTWVFQVGP RSSRSDINCS VMEATEEKVV VHLKKLDTAY
     DELGNSGHFT LIYNQGFEIV LNDYKWFAFF KYEVRGHTAI SYCHETMTGW VHDVLGRNWA
     CFVGKKVESH IEKVNMNAAH LGGLQERYSE RLYTHNHNFV KAINTVQKSW TATAYKEYEK
     MSLRDLIRRS GHSQRIPRPK PAPMTDEIQQ QILNLPESWD WRNVQGVNYV SPVRNQESCG
     SCYSFASMGM LEARIRILTN NSQTPILSPQ EVVSCSPYAQ GCDGGFPYLI AGKYAQDFGV
     VEESCFPYTA KDSPCKPREN CLRYYSSDYY YVGGFYGGCN EALMKLELVK HGPMAVAFEV
     HDDFLHYHSG IYHHTGLSDP FNPFELTNHA VLLVGYGRDP VTGIEYWIIK NSWGSNWGES
     GYFRIRRGTD ECAIESIAVA AIPIPKL
//